Koji Sode

Yanase, T., Okuda-Shimazaki, J., Asano, R., Ikebukuro, K., Sode, K., & Tsugawa, W. (2023). Development of a Versatile Method to Construct Direct Electron Transfer-Type Enzyme Complexes Employing SpyCatcher/SpyTag System. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 24(3). https://doi.org/10.3390/ijms24031837

Nagata, M., Lee, J., Saito, T., Ikebukuro, K., & Sode, K. (2023). Development of an Anti-Idiotype Aptamer-Based Electrochemical Sensor for a Humanized Therapeutic Antibody Monitoring. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 24(6). https://doi.org/10.3390/ijms24065277

Probst, D., Lee, I., Dick, J. E., & Sode, K. (2023). Surface area independent response of closed bipolar electrodes. Sensors and Actuators Reports. https://doi.org/10.1016/j.snr.2023.100138

Fitriana, M., Hiraka, K., Ikebukuro, K., Sode, K., & Tsugawa, W. (2022). A Thiol-reactive Phenazine Ethosulfate - A Novel Redox Mediator for Quasi-direct Electron-transfer-type Sensors. SENSORS AND MATERIALS, 34(6), 2105–2124. https://doi.org/10.18494/SAM3898

Nagata, M., Lee, J., Henley, S., Ikebukuro, K., & Sode, K. (2022). An Amine-Reactive Phenazine Ethosulfate (arPES)-A Novel Redox Probe for Electrochemical Aptamer-Based Sensor. SENSORS, 22(5). https://doi.org/10.3390/s22051760

Moriuchi, T., Otaki, Y., Satou, H., Chai, F., Hayashida, Y., Aikawa, R., … Sode, K. (2022). Clinical Study of a High Accuracy Green Design Blood Glucose Monitor Using an Innovative Optical Transmission Absorbance System. JOURNAL OF DIABETES SCIENCE AND TECHNOLOGY, 16(5), 1069–1075. https://doi.org/10.1177/19322968211060865

Saito, T., Shimizu, Y., Tsukakoshi, K., Abe, K., Lee, J., Ueno, K., … Ikebukuro, K. (2022). Development of a DNA aptamer that binds to the complementarity-determining region of therapeutic monoclonal antibody and affinity improvement induced by pH-change for sensitive detection. BIOSENSORS & BIOELECTRONICS, 203. https://doi.org/10.1016/j.bios.2022.114027

Khanwalker, M., Fujita, R., Lee, J., Wilson, E., Ito, K., Asano, R., … Sode, K. (2022). Development of a POCT type insulin sensor employing anti-insulin single chain variable fragment based on faradaic electrochemical impedance spectroscopy under single frequency measurement. Biosensors and Bioelectronics, 200, 113901. https://doi.org/10.1016/j.bios.2021.113901

Lee, J., Kane, B. J., Khanwalker, M., & Sode, K. (2022). Development of an electrochemical impedance spectroscopy based biosensor for detection of ubiquitin C-Terminal hydrolase L1. BIOSENSORS & BIOELECTRONICS, 208. https://doi.org/10.1016/j.bios.2022.114232

Lee, I., Wakako, T., Ikebukuro, K., & Sode, K. (2022). In Vitro Continuous 3 Months Operation of Direct Electron Transfer Type Open Circuit Potential Based Glucose Sensor: Heralding the Next CGM Sensor. JOURNAL OF DIABETES SCIENCE AND TECHNOLOGY, 16(5), 1107–1113. https://doi.org/10.1177/19322968221092449

Inoue, Y., Kusaka, Y., Shinozaki, K., Lee, I., & Sode, K. (2022). In Vitro Evaluation of Miniaturized Amperometric Enzyme Sensor Based on the Direct Electron Transfer Principle for Continuous Glucose Monitoring. Journal of Diabetes Science and Technology, 1, 193229682110706. https://doi.org/10.1177/19322968211070614

Kobayashi, S., Atsumi, S., Ikebukuro, K., Sode, K., & Asano, R. (2022). Light-induced production of isobutanol and 3-methyl-1-butanol by metabolically engineered cyanobacteria. MICROBIAL CELL FACTORIES, 21(1). https://doi.org/10.1186/s12934-021-01732-x

Okuda-Shimazaki, J., Yoshida, H., Lee, I., Kojima, K., Suzuki, N., Tsugawa, W., … Sode, K. (2022). Microgravity environment grown crystal structure information based engineering of direct electron transfer type glucose dehydrogenase. COMMUNICATIONS BIOLOGY, 5(1). https://doi.org/10.1038/s42003-022-04286-9

Hiraka, K., Yoshida, H., Tsugawa, W., Asano, R., La Belle, J. T., Ikebukuro, K., & Sode, K. (2022). Structure of lactate oxidase from Enterococcus hirae revealed new aspects of active site loop function: Product-inhibition mechanism and oxygen gatekeeper. PROTEIN SCIENCE, 31(10). https://doi.org/10.1002/pro.4434

Takamatsu, S., Lee, I., Lee, J., Asano, R., Tsugawa, W., Ikebukuro, K., … Sode, K. (2022). Transient potentiometry based d-serine sensor using engineered d-amino acid oxidase showing quasi-direct electron transfer property. Biosensors and Bioelectronics, 200, 113927. https://doi.org/10.1016/j.bios.2021.113927

Shono, C., Ariyanti, D., Abe, K., Sakai, Y., Sakamoto, I., Tsukakoshi, K., … Ikebukuro, K. (2021). A Green Light-Regulated T7 RNA Polymerase Gene Expression System for Cyanobacteria. Marine Biotechnology, 23(1), 31–38. https://doi.org/10.1007/s10126-020-09997-w

Lee, I., Okuda-Shimazaki, J., Tsugawa, W., Ikebukuro, K., & Sode, K. (2021). A self-powered glucose sensor based on BioCapacitor principle with micro-sized enzyme anode employing direct electron transfer type FADGDH. JOURNAL OF PHYSICS-ENERGY, 3(3). https://doi.org/10.1088/2515-7655/abee32

Ariyanti, D., Ikebukuro, K., & Sode, K. (2021). Artificial complementary chromatic acclimation gene expression system in Escherichia coli. MICROBIAL CELL FACTORIES, 20(1). https://doi.org/10.1186/s12934-021-01621-3

Takamatsu, S., Lee, J., Asano, R., Tsugawa, W., Ikebukuro, K., & Sode, K. (2021). Continuous electrochemical monitoring of L-glutamine using redox-probe-modified L-glutamine-binding protein based on intermittent pulse amperometry. SENSORS AND ACTUATORS B-CHEMICAL, 346. https://doi.org/10.1016/j.snb.2021.130554

Lee, I., Probst, D., Klonoff, D., & Sode, K. (2021). Continuous glucose monitoring systems-Current status and future perspectives of the flagship technologies in biosensor research. BIOSENSORS & BIOELECTRONICS, 181. https://doi.org/10.1016/j.bios.2021.113054

Lee, J., Teramoto, K., Yokoyama, T., Ueno, K., Tsukakoshi, K., Sode, K., & Ikebukuro, K. (2021, June). Data on G-quadruplex topology, and binding ability of G-quadruplex forming sequences found in the promoter region of biomarker proteins and those relations to the presence of nuclear localization signal in the proteins. DATA IN BRIEF, Vol. 36. https://doi.org/10.1016/j.dib.2021.107028

Probst, D., Lee, I., Dick, J. E., & Sode, K. (2021). Detection of Chloride Using Microelectrodes in Closed Bipolar Electrode Scheme. ECS Meeting Abstracts. https://doi.org/10.1149/MA2021-02551609mtgabs

Hatada, M., Loew, N., Okuda-Shimazaki, J., Khanwalker, M., Tsugawa, W., Mulchandani, A., & Sode, K. (2021). Development of an Interdigitated Electrode-Based Disposable Enzyme Sensor Strip for Glycated Albumin Measurement. MOLECULES, 26(3). https://doi.org/10.3390/molecules26030734

Hatada, M., Saito, S., Yonehara, S., Tsugawa, W., Asano, R., Ikebukuro, K., & Sode, K. (2021). Development of glycated peptide enzyme sensor based flow injection analysis system for haemoglobin A1c monitoring using quasi-direct electron transfer type engineered fructosyl peptide oxidase. BIOSENSORS & BIOELECTRONICS, 177. https://doi.org/10.1016/j.bios.2021.112984

Li, C.-zhong, Liu, J., & Sode, K. (2021, December 15). Editorial preface of the special issue on "the progress and perspectives of biosensing research in North America". BIOSENSORS & BIOELECTRONICS, Vol. 194. https://doi.org/10.1016/j.bios.2021.113578

Vannoy, K. J., Lee, I., Sode, K., & Dick, J. E. (2021). Electrochemical quantification of accelerated FADGDH rates in aqueous nanodroplets. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 118(25). https://doi.org/10.1073/pnas.2025726118

Vannoy, K. J., Lee, I., Sode, K., & Dick, J. E. (2021). Electrochemical quantification of accelerated FADGDH rates in aqueous nanodroplets. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 118(25). https://doi.org/10.1073/pnas.2025726118|1of5

Tsukakoshi, K., Yamagishi, Y., Kanazashi, M., Nakama, K., Oshikawa, D., Savory, N., … Ikebukuro, K. (2021). G-quadruplex-forming aptamer enhances the peroxidase activity of myoglobin against luminol. NUCLEIC ACIDS RESEARCH, 49(11), 6069–6081. https://doi.org/10.1093/nar/gkab388

Miura, D., Kimura, H., Tsugawa, W., Ikebukuro, K., Sode, K., & Asano, R. (2021). Rapid, convenient, and highly sensitive detection of human hemoglobin in serum using a high-affinity bivalent antibody-enzyme complex. TALANTA, 234. https://doi.org/10.1016/j.talanta.2021.122638

Hiraka, K., Tsugawa, W., Asano, R., Yokus, M. A., Ikebukuro, K., Daniele, M. A., & Sode, K. (2021). Rational design of direct electron transfer type L-lactate dehydrogenase for the development of multiplexed biosensor. BIOSENSORS & BIOELECTRONICS, 176. https://doi.org/10.1016/j.bios.2020.112933

Ito, K., Okuda-Shimazaki, J., Kojima, K., Mori, K., Tsugawa, W., Asano, R., … Sode, K. (2021). Strategic design and improvement of the internal electron transfer of heme b domain-fused glucose dehydrogenase for use in direct electron transfer-type glucose sensors. BIOSENSORS & BIOELECTRONICS, 176. https://doi.org/10.1016/j.bios.2020.112911

Sode, K. (2020). (Keynote) Continuous Glucose Monitoring Systems - Current Status and Future Perspectives of the Flagship Technologies in Biosensor Research -. ECS Meeting Abstracts, MA2020-02(44), 2777–2777. https://doi.org/10.1149/MA2020-02442777mtgabs

Hiraka, K., Tsugawa, W., & Sode, K. (2020). [Review of Alteration of Electron Acceptor Preferences in the Oxidative Half-Reaction of Flavin-Dependent Oxidases and Dehydrogenases]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 21(11). https://doi.org/10.3390/ijms21113797

Lee, J., Tatsumi, A., Tsukakoshi, K., Wilson, E. D., Abe, K., Sode, K., & Ikebukuro, K. (2020). Application of a Glucose Dehydrogenase-Fused with Zinc Finger Protein to Label DNA Aptamers for the Electrochemical Detection of VEGF. SENSORS, 20(14). https://doi.org/10.3390/s20143878

Shimazaki, J., Yoshida, H., & Sode, K. (2020). Construction of Super-Stabilized Direct Electron Transfer Type Glucose Dehydrogenase for Long Term Continuous Glucose Sensing System. ECS Meeting Abstracts, MA2020-02(44), 2831–2831. https://doi.org/10.1149/MA2020-02442831mtgabs

Yanase, T., Okuda-Shimazaki, J., Mori, K., Kojima, K., Tsugawa, W., & Sode, K. (2020). Creation of a novel DET type FAD glucose dehydrogenase harboring Escherichia coli derived cytochrome b562 as an electron transfer domain. Biochemical and Biophysical Research Communications, 530(1), 82–86. https://doi.org/10.1016/j.bbrc.2020.06.132

Khanwalker, M., Lee, J., LaBelle, J., Cook, C., Caplan, M., Morrow, B., … Sode, K. (2020). Development of Insulin Sensors Based on Faradaic and Non-Faradaic Electrochemical Impedance Spectroscopy Detection Principle Using Single Chain Antibody (scFv). ECS Meeting Abstracts, MA2020-02(44), 2783–2783. https://doi.org/10.1149/MA2020-02442783mtgabs

Lee, J., Hirano, H., Tsugawa, W., & Sode, K. (2020). Development of an Electrochemical Biosensor of Ubiquitin C-Terminal Hydrolase L1 (UCH-L1) for the Assessment of Traumatic Brain Injury (TBI). ECS Meeting Abstracts, MA2020-02(44), 2784–2784. https://doi.org/10.1149/MA2020-02442784mtgabs

Hatano, Y., Lee, J., Kim, S. H., Ikebukuro, K., Asano, R., Gu, M. B., & Sode, K. (2020). Electrochemical Aptasensor Employing Enzyme-Aptamer One-to-One Complex Showing Quasi-Direct Electron Transfer Ability. ECS Meeting Abstracts, MA2020-02(44), 2834–2834. https://doi.org/10.1149/MA2020-02442834mtgabs

Suzuki, N., Lee, J., Loew, N., Takahashi-Inose, Y., Okuda-Shimazaki, J., Kojima, K., … Sode, K. (2020). Engineered Glucose Oxidase Capable of Quasi-Direct Electron Transfer after a Quick-and-Easy Modification with a Mediator. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 21(3). https://doi.org/10.3390/ijms21031137

Okuda-Shimazaki, J., Yoshida, H., & Sode, K. (2020). FAD dependent glucose dehydrogenases - Discovery and engineering of representative glucose sensing enzymes -. BIOELECTROCHEMISTRY, 132. https://doi.org/10.1016/j.bioelechem.2019.107414

Hiraka, K., Kojima, K., Tsugawa, W., Asano, R., Ikebukuro, K., & Sode, K. (2020). Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor. BIOSENSORS & BIOELECTRONICS, 151. https://doi.org/10.1016/j.bios.2019.111974

Wilson, E., Lee, J., Henley, S., Asano, R., Ikebukuro, K., & Sode, K. (2020). The Abtamer: A Novel Antibody-Aptamer Conjugate for Electrochemical Biosensing Applications. ECS Meeting Abstracts, MA2020-02(44), 2835–2835. https://doi.org/10.1149/MA2020-02442835mtgabs

Lee, I., Shimazaki, J., Tsugawa, W., Ikebukuro, K., Dick, J. E., Daniele, M., & Sode, K. (2020). The Continuous 3 Month Operation of Open Circuit Potential Based Glucose Sensor Employing Direct Electron Transfer Type Fad Dependent Glucose Dehydrogenase. ECS Meeting Abstracts, MA2020-02(44), 2779–2779. https://doi.org/10.1149/MA2020-02442779mtgabs

Hatada, M., Tran, T.-T., Tsugawa, W., Sode, K., & Mulchandani, A. (2019). Affinity sensor for haemoglobin A1c based on single-walled carbon nanotube field-effect transistor and fructosyl amino acid binding protein. BIOSENSORS & BIOELECTRONICS, 129, 254–259. https://doi.org/10.1016/j.bios.2018.09.069

Kobayashi, S., Nakajima, M., Asano, R., Ferreira, E. A., Abe, K., Tamagnini, P., … Sode, K. (2019). Application of an engineered chromatic acclimation sensor for red-light-regulated gene expression in cyanobacteria. ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS, 44. https://doi.org/10.1016/j.algal.2019.101691

Ito, K., Okuda-Shimazaki, J., Mori, K., Kojima, K., Tsugawa, W., Ikebukuro, K., … Sode, K. (2019). Designer fungus FAD glucose dehydrogenase capable of direct electron transfer. BIOSENSORS & BIOELECTRONICS, 123, 114–123. https://doi.org/10.1016/j.bios.2018.07.027

Lee, I., Loew, N., Tsugawa, W., Ikebukuro, K., & Sode, K. (2019). Development of a third-generation glucose sensor based on the open circuit potential for continuous glucose monitoring. BIOSENSORS & BIOELECTRONICS, 124, 216–223. https://doi.org/10.1016/j.bios.2018.09.099

Hoshi, K., Yamazaki, T., Sugiyama, Y., Tsukakoshi, K., Tsugawa, W., Sode, K., & Ikebukuro, K. (2019). G-Quadruplex Structure Improves the Immunostimulatory Effects of CpG Oligonucleotides. NUCLEIC ACID THERAPEUTICS, 29(4), 224–229. https://doi.org/10.1089/nat.2018.0761

Ito, Y., Okuda-Shimazaki, J., Tsugawa, W., Loew, N., Shitanda, I., Lin, C.-E., … Sode, K. (2019). Third generation impedimetric sensor employing direct electron transfer type glucose dehydrogenase. BIOSENSORS & BIOELECTRONICS, 129, 189–197. https://doi.org/10.1016/j.bios.2019.01.018

Yoshida, H., Kojima, K., Shiota, M., Yoshimatsu, K., Yamazaki, T., Ferri, S., … Sode, K. (2019). X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 75, 841–851. https://doi.org/10.1107/S2059798319010878

Lin, C. E., Ito, Y., Deng, A., Johns, J., Matloff, D., Cook, C. B., … La Belle, J. T. (2018). A Disposable Tear Glucose Biosensor-Part 5: Improvements in Reagents and Tear Sampling Component. Journal of Diabetes Science and Technology, 12(4), 842–846. https://doi.org/10.1177/1932296818769944

Sode, K. (2018). Biomolecular engineering of redox enzymes: Alteration of the electron acceptor preference; from oxygen to direct electron transfer. Abstracts of Papers of the American Chemical Society, 255. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000435537700584&KeyUID=WOS:000435537700584

Asano, R., Kuroki, Y., Honma, S., Akabane, M., Watanabe, S., Mayuzumi, S., … Sode, K. (2018). Comprehensive study of domain rearrangements of single-chain bispecific antibodies to determine the best combination of configurations and microbial host cells. Mabs, 10(6), 854–863. https://doi.org/10.1080/19420862.2018.1476815

Okuda-Shimazaki, J., Loew, N., Hirose, N., Kojima, K., Mori, K., Tsugawa, W., & Sode, K. (2018). Construction and characterization of flavin adenine dinucleotide glucose dehydrogenase complex harboring a truncated electron transfer subunit. ELECTROCHIMICA ACTA, 277, 276–286. https://doi.org/10.1016/j.electacta.2018.04.060

Hatada, M., Loew, N., Inose-Takahashi, Y., Okuda-Shimazaki, J., Tsugawa, W., Mulchandani, A., & Sode, K. (2018). Development of a glucose sensor employing quick and easy modification method with mediator for altering electron acceptor preference. BIOELECTROCHEMISTRY, 121, 185–190. https://doi.org/10.1016/j.bioelechem.2018.02.001

Lee, J., Yoshida, W., Hiraoka, D., Tatsumi, A., Abe, K., Nakabayashi, K., … Ikebukuro, K. (2018). Development of an electrochemical detection system for CpG methylation of human genome using methyl CpG binding domain and zinc finger protein. Abstracts of Papers of the American Chemical Society, 256. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000447600001002&KeyUID=WOS:000447600001002

Lin, C.-E., Hiraka, K., Matloff, D., Johns, J., Deng, A., Sode, K., & La Belle, J. (2018). Development toward a novel integrated tear lactate sensor using Schirmer test strip and engineered lactate oxidase. SENSORS AND ACTUATORS B-CHEMICAL, 270, 525–529. https://doi.org/10.1016/j.snb.2018.05.061

Yamashita, Y., Lee, I., Loew, N., & Sode, K. (2018). Direct electron transfer (DET) mechanism of FAD dependent dehydrogenase complexes ∼from the elucidation of intra- and inter-molecular electron transfer pathway to the construction of engineered DET enzyme complexes∼. Current Opinion in Electrochemistry. https://doi.org/10.1016/j.coelec.2018.07.013

Miyazaki, R., Yamazaki, T., Yoshimatsu, K., Kojima, K., Asano, R., Sode, K., & Tsugawa, W. (2018, August). Elucidation of the intra- and inter-molecular electron transfer pathways of glucoside 3-dehydrogenase. BIOELECTROCHEMISTRY, Vol. 122, pp. 115–122. https://doi.org/10.1016/j.bioelechem.2018.03.001

Okurita, M., Suzuki, N., Loew, N., Yoshida, H., Tsugawa, W., Mori, K., … Sode, K. (2018). Engineered fungus derived FAD-dependent glucose dehydrogenase with acquired ability to utilize hexaammineruthenium(III) as an electron acceptor. Bioelectrochemistry, 123, 62–69. https://doi.org/10.1016/j.bioelechem.2018.04.007

Tsukakoshi, K., Yoshida, W., Kobayashi, M., Kobayashi, N., Kim, J., Kaku, T., … Sode, K. (2018). Esterification of PQQ Enhances Blood-Brain Barrier Permeability and Inhibitory Activity against Amyloidogenic Protein Fibril Formation. ACS Chemical Neuroscience. https://doi.org/10.1021/acschemneuro.8b00355

Badary, A., Takamatsu, S., Nakajima, M., Ferri, S., Lindblad, P., & Sode, K. (2018). Glycogen Production in Marine Cyanobacterial Strain Synechococcus sp NKBG 15041c. Marine Biotechnology, 20(2), 109–117. https://doi.org/10.1007/s10126-017-9792-2

Sakamoto, I., Abe, K., Kawai, S., Tsukakoshi, K., Sakai, Y., Sode, K., & Ikebukuro, K. (2018). Improving the induction fold of riboregulators for cyanobacteria. Rna Biology, 15(3), 353–358. https://doi.org/10.1080/15476286.2017.1422470

Hiraka, K., Kojima, K., Lin, C.-E., Tsugawa, W., Asano, R., La Belle, J. T., & Sode, K. (2018). Minimizing the effects of oxygen interference on L-lactate sensors by a single amino acid mutation in Aerococcus viridans L-lactate oxidase. Biosensors & Bioelectronics, 103, 163–170. https://doi.org/10.1016/j.bios.2017.12.018

Yamashita, Y., Suzuki, N., Hirose, N., Kojima, K., Tsugawa, W., & Sode, K. (2018). Mutagenesis Study of the Cytochrome c Subunit Responsible for the Direct Electron Transfer-Type Catalytic Activity of FAD-Dependent Glucose Dehydrogenase. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 19(4). https://doi.org/10.3390/ijms19040931

Loew, N., Suzuki, N., Tsugawa, W., Inose-Takahashi, Y., Hatada, M., Mori, K., & Sode, K. (2018). Quasi-direct electron transfer-type glucose sensor based on engineered glucose oxidase. Abstracts of Papers of the American Chemical Society, 256. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000447600001209&KeyUID=WOS:000447600001209

Lee, I., Loew, N., Tsugawa, W., Ikebukuro, K., & Sode, K. (2018). Self-powered, wireless continuous glucose sensing system based direct electron transfer. Abstracts of Papers of the American Chemical Society, 256. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000447600000887&KeyUID=WOS:000447600000887

Tsukakoshi, K., Nishio, M., Sasaki, I., Ma, Y., Nagasawa, K., Kato, Y., … Ikebukuro, K. (2018). Smart aptamers forming G-quadruplex: Structural and functional change of aptamers forming G-quadruplex in response to surrounding conditions and its regulation with the ligands. Abstracts of Papers of the American Chemical Society, 256. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000447600001223&KeyUID=WOS:000447600001223

Hoshi, K., Yamazaki, T., Yoshikawa, C. H., Tsugawa, W., Ikebukuro, K., & Sode, K. (2018). Synthesis of a hemin-containing copolymer as a novel immunostimulator that induces IFN-gamma production. International Journal of Nanomedicine, 13, 4461–4472. https://doi.org/10.2147/IJN.S166259

Lee, I., Loew, N., Tsugawa, W., Lin, C.-E., Probst, D., Belle, J. T. L., & Sode, K. (2018). The electrochemical behavior of a FAD dependent glucose dehydrogenase with direct electron transfer subunit by immobilization on self-assembled monolayers. Bioelectrochemistry, 121, 1–6. https://doi.org/10.1016/j.bioelechem.2017.12.008

Sode, K., Loew, N., Lee, I., Ito, Y., & Tsugawa, W. (2018). Wearable and implantable biosensing technologies based on the direct electron transfer principle. Abstracts of Papers of the American Chemical Society, 256. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000447600001124&KeyUID=WOS:000447600001124

Ueno, K., Sakai, Y., Shono, C., Sakamoto, I., Tsukakoshi, K., Hihara, Y., … Ikebukuro, K. (2017). Applying a riboregulator as a new chromosomal gene regulation tool for higher glycogen production in Synechocystis sp PCC 6803. Applied Microbiology and Biotechnology, 101(23-24), 8465–8474. https://doi.org/10.1007/s00253-017-8570-4

Loew, N., Fitriana, M., Hiraka, K., Sode, K., & Tsugawa, W. (2017). Characterization of Electron Mediator Preference of Aerococcus viridans-Derived Lactate Oxidase for Use in Disposable Enzyme Sensor Strips. Sensors and Materials, 29(12), 1703–1711. https://doi.org/10.18494/SAM.2017.1731

Lee, I., Sode, T., Loew, N., Tsugawa, W., Lowe, C. R., & Sode, K. (2017). Continuous operation of an ultra-low-power microcontroller using glucose as the sole energy source. Biosensors & Bioelectronics, 93, 335–339. https://doi.org/10.1016/j.bios.2016.09.095

Hatada, M., Tsugawa, W., Kamio, E., Loew, N., Klonoff, D. C., & Sode, K. (2017). Development of a screen-printed carbon electrode based disposable enzyme sensor strip for the measurement of glycated albumin. Biosensors & Bioelectronics, 88, 167–173. https://doi.org/10.1016/j.bios.2016.08.005

Lee, J., Yoshida, W., Abe, K., Nakabayashi, K., Wakeda, H., Hata, K., … Ikebukuro, K. (2017). Development of an electrochemical detection system for measuring DNA methylation levels using methyl CpG-binding protein and glucose dehydrogenase-fused zinc finger protein. Biosensors & Bioelectronics, 93, 118–123. https://doi.org/10.1016/j.bios.2016.09.060

Loew, N., Tsugawa, W., Nagae, D., Kojima, K., & Sode, K. (2017). Mediator Preference of Two Different FAD-Dependent Glucose Dehydrogenases Employed in Disposable Enzyme Glucose Sensors. Sensors, 17(11). https://doi.org/10.3390/s17112636

Sharma, S., Takagi, E., Cass, T., Tsugawa, W., & Sode, K. (2017). Minimally invasive microneedle array electrodes employing direct electron transfer type glucose dehydrogenase for the development of continuous glucose monitoring sensors. In Biosensors 2016 (Vol. 27, pp. 208–209). https://doi.org/10.1016/j.protcy.2017.04.087

Sode, K., Loew, N., Ohnishi, Y., Tsuruta, H., Mori, K., Kojima, K., … Klonoff, D. C. (2017). Novel fungal FAD glucose dehydrogenase derived from Aspergillus niger for glucose enzyme sensor strips. Biosensors & Bioelectronics, 87, 305–311. https://doi.org/10.1016/j.bios.2016.08.053

Shimasaki, T., Yoshida, H., Kamitori, S., & Sode, K. (2017). X-ray structures of fructosyl peptide oxidases revealing residues responsible for gating oxygen access in the oxidative half reaction. Scientific Reports, 7(1). https://doi.org/10.1038/s41598-017-02657-5

Shiota, M., Yamazaki, T., Yoshimatsu, K., Kojima, K., Tsugawa, W., Ferri, S., & Sode, K. (2016). An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes. Bioelectrochemistry, 112, 178–183. https://doi.org/10.1016/j.bioelechem.2016.01.010

Sode, K., Yamazaki, T., Lee, I., Hanashi, T., & Tsugawa, W. (2016). BioCapacitor: A novel principle for biosensors. Biosensors & Bioelectronics, 76, 20–28. https://doi.org/10.1016/j.bios.2015.07.065

Nakajima, M., Ferri, S., Rogner, M., & Sode, K. (2016). Construction of a Miniaturized Chromatic Acclimation Sensor from Cyanobacteria with Reversed Response to a Light Signal. Scientific Reports, 6. https://doi.org/10.1038/srep37595

Nakajima, M., Abe, K., Ferri, S., & Sode, K. (2016). Development of a light-regulated cell-recovery system for non-photosynthetic bacteria. Microbial Cell Factories, 15(1). https://doi.org/10.1186/s12934-016-0426-6

Kameya, M., Tsugawa, W., Yamada-Tajima, M., Hatada, M., Suzuki, K., Sakaguchi-Mikami, A., … Sode, K. (2016). Electrochemical sensing system employing fructosamine 6-kinase enables glycated albumin measurement requiring no proteolytic digestion. Biotechnology Journal, 11(6), 797–804. https://doi.org/10.1002/biot.201500442

Tsukakoshi, K., Ikuta, Y., Abe, K., Yoshida, W., Iida, K., Ma, Y., … Ikebukuro, K. (2016). Structural regulation by a G-quadruplex ligand increases binding abilities of G-quadruplex-forming aptamers. Chemical Communications, 52(85), 12646–12649. https://doi.org/10.1039/c6cc07552e

Sekimoto, S., Shinozaki, K., Murase, Y., Kusaka, Y., Tsugawa, W., & Sode, K. (2015). 3RD GENERATION CGM SENSOR EMPLOYING DIRECT ELECTRON TRANSFER PRINCIPLE WITH IMPROVED OPERATIONAL CONDITIONS. Diabetes Technology & Therapeutics, 17, A90. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000349317500203&KeyUID=WOS:000349317500203

Kameya, M., Sakaguchi-Mikami, A., Ferri, S., Tsugawa, W., & Sode, K. (2015). Advancing the development of glycated protein biosensing technology: next-generation sensing molecules. Journal of Diabetes Science and Technology, 9(2), 183–191. https://doi.org/10.1177/1932296814565784

Yoshida, H., Sakai, G., Mori, K., Kojima, K., Kamitori, S., & Sode, K. (2015). Crystal structure of Aspergillus flavus FAD glucose dehydrogenase. Worldwide Protein Data Bank. https://doi.org/10.2210/pdb4ynt/pdb

Yoshida, H., Sakai, G., Mori, K., Kojima, K., Kamitori, S., & Sode, K. (2015). Crystal structure of Aspergillus flavus FADGDH in complex with D-glucono-1,5-lactone. Worldwide Protein Data Bank. https://doi.org/10.2210/pdb4ynu/pdb

Tsugawa, W., Futagami, H., & Sode, K. (2015). Development of an electrochemical adenosine diphosphate (ADP) sensing principle employing ADP-dependent kinase. Sensors and Materials, 27(9), 839–845. https://doi.org/10.18494/SAM.2015.1120

Tajima, Y., Yamamoto, Y., Fukui, K., Nishio, Y., Hashiguchi, K., Usuda, Y., & Sode, K. (2015). Effects of Eliminating Pyruvate Node Pathways and of Coexpression of Heterogeneous Carboxylation Enzymes on Succinate Production by Enterobacter aerogenes. Applied and Environmental Microbiology, 81(3), 929–937. https://doi.org/10.1128/AEM.03213-14

Ferri, S., Nakamura, M., Ito, A., Nakajima, M., Abe, K., Kojima, K., & Sode, K. (2015). Efficient surface-display of autotransporter proteins in cyanobacteria. Algal Research-Biomass Biofuels and Bioproducts, 12, 337–340. https://doi.org/10.1016/j.algal.2015.09.013

Abe, K., Murakami, Y., Tatsumi, A., Sumida, K., Kezuka, A., Fukaya, T., … Ikebukuro, K. (2015). Enzyme linking to DNA aptamers via a zinc finger as a bridge. Chemical Communications, 51(57), 11467–11469. https://doi.org/10.1039/c5cc02906f

Tajima, Y., Yamamoto, Y., Fukui, K., Nishio, Y., Hashiguchi, K., Usuda, Y., & Sode, K. (2015). Impact of an energy-conserving strategy on succinate production under weak acidic and anaerobic conditions in Enterobacter aerogenes. Microbial Cell Factories, 14(1), (11 June 2015). https://doi.org/10.1186/s12934-015-0269-6

Fukaya, T., Abe, K., Savory, N., Tsukakoshi, K., Yoshida, W., Ferri, S., … Ikebukuro, K. (2015). Improvement of the VEGF binding ability of DNA aptamers through in silico maturation and multimerization strategy. Journal of Biotechnology, 212, 99–105. https://doi.org/10.1016/j.jbiotec.2015.08.011

Clark, D. S., Karube, I., Sode, K., Bulow, L., Brueggemann, O., Lowe, C. R., … Langer, R. S. (2015). Klaus Mosbach Tribute. Biotechnology and Bioengineering, 112(4), 645–647. https://doi.org/10.1002/bit.25507

Sakai, Y., Abe, K., Nakashima, S., Ellinger, J. J., Ferri, S., Sode, K., & Ikebukuro, K. (2015). Scaffold-fused riboregulators for enhanced gene activation in Synechocystis sp PCC 6803. Microbiologyopen, 4(4), 533–540. https://doi.org/10.1002/mbo3.257

Sakai, G., Kojima, K., Mori, K., Oonishi, Y., & Sode, K. (2015). Stabilization of fungi-derived recombinant FAD-dependent glucose dehydrogenase by introducing a disulfide bond. Biotechnology Letters, 37(5), 1091–1099. https://doi.org/10.1007/s10529-015-1774-8

Yoshida, H., Sakai, G., Mori, K., Kojima, K., Kamitori, S., & Sode, K. (2015). Structural analysis of fungus-derived FAD glucose dehydrogenase. Scientific Reports, 5. https://doi.org/10.1038/srep13498

Badary, A., Abe, K., Ferri, S., Kojima, K., & Sode, K. (2015). The Development and Characterization of an Exogenous Green-Light-Regulated Gene Expression System in Marine Cyanobacteria. Marine Biotechnology, 17(3), 245–251. https://doi.org/10.1007/s10126-015-9616-1

Yoshida, H., Sakai, G., Kojima, K., Kamitori, S., & Sode, K. (2015). X-ray structure of recombinant nonglycosylated FAD glucose dehydrogenase derived from Aspergillus flavus. Febs Journal, 282, 279. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000362570605056&KeyUID=WOS:000362570605056

Miyake, K., Abe, K., Ferri, S., Nakajima, M., Nakamura, M., Yoshida, W., … Sode, K. (2014). A green-light inducible lytic system for cyanobacterial cells. Biotechnology For Biofuels, 7(1), (9 April 2014). https://doi.org/10.1186/1754-6834-7-56

Abe, K., Sakai, Y., Nakashima, S., Araki, M., Yoshida, W., Sode, K., & Ikebukuro, K. (2014). Design of riboregulators for control of cyanobacterial (Synechocystis) protein expression. Biotechnology Letters, 36(2), 287–294. https://doi.org/10.1007/s10529-013-1352-x

Lee, J., Tatsumi, A., Abe, K., Yoshida, W., Sode, K., & Ikebukuro, K. (2014). Electrochemical detection of pathogenic bacteria by using a glucose dehydrogenase fused zinc finger protein. Analytical Methods, 6(14), 4991–4994. https://doi.org/10.1039/c4ay00977k

Horaguchi, Y., Saito, S., Kojima, K., Tsugawa, W., Ferri, S., & Sode, K. (2014). Engineering glucose oxidase to minimize the influence of oxygen on sensor response. Electrochimica Acta, 126, 158–161. https://doi.org/10.1016/j.electacta.2013.09.018

Abe, K., Miyake, K., Nakamura, M., Kojima, K., Ferri, S., Ikebukuro, K., & Sode, K. (2014). Engineering of a green-light inducible gene expression system in Synechocystis sp PCC6803. Microbial Biotechnology, 7(2), 177–183. https://doi.org/10.1111/1751-7915.12098

Sakai, Y., Abe, K., Nakashima, S., Yoshida, W., Ferri, S., Sode, K., & Ikebukuro, K. (2014). Improving the Gene-Regulation Ability of Small RNAs by Scaffold Engineering in Escherichia coli. Acs Synthetic Biology, 3(3), 152–162. https://doi.org/10.1021/sb4000959

Savory, N., Takahashi, Y., Tsukakoshi, K., Hasegawa, H., Takase, M., Abe, K., … Ikebukuro, K. (2014). Simultaneous Improvement of Specificity and Affinity of Aptamers Against Streptococcus mutans by In Silico Maturation for Biosensor Development. Biotechnology and Bioengineering, 111(3), 454–461. https://doi.org/10.1002/bit.25111

Tajima, Y., Kaida, K., Hayakawa, A., Fukui, K., Nishio, Y., Hashiguchi, K., … Sode, K. (2014). Study of the role of anaerobic metabolism in succinate production by Enterobacter aerogenes. Applied Microbiology and Biotechnology, 98(18), 7803–7813. https://doi.org/10.1007/s00253-014-5884-3

Sekimoto, S., Shinozaki, K., Murase, Y., Kusaka, Y., Kojima, K., Tsugawa, W., & Sode, K. (2014). THE 3RD GENERATION CGM SENSOR UTILIZING DIRECT ELECTRON TRANSFER PRINCIPLE. Diabetes Technology & Therapeutics, 16, A78–A79. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000331218000205&KeyUID=WOS:000331218000205

Hanashi, T., Yamazaki, T., Tanaka, H., Ikebukuro, K., Tsugawa, W., & Sode, K. (2014). The development of an autonomous self-powered bio-sensing actuator. Sensors and Actuators B-Chemical, 196, 429–433. https://doi.org/10.1016/j.snb.2014.01.117

Koshiba, M., Senoo, A., Karino, G., Shirakawa, Y., Mimura, K., Sagawa, T., … Nakamura, S. (2013). Blood Glucose Dependence on Emotional Behaviors and Body Surface Temperatures in Common Marmoset's Socio-Psychological Learning with Peers - for 'Development of Human-Environment Interface by Sensing and Multivariate Analysis of Bio-Ecosystem'. Bioengineering Based on Electrochemistry, 50(28), 9–14. https://doi.org/10.1149/05028.0009ecst

Sakaguchi-Mikami, A., Kameya, M., Ferri, S., Tsugawa, W., & Sode, K. (2013). Cloning and Characterization of Fructosamine-6-Kinase from Arthrobacter aurescens. Applied Biochemistry and Biotechnology, 170(3), 710–717. https://doi.org/10.1007/s12010-013-0229-8

Yamashita, Y., Ferri, S., Huynh, M. L., Shimizu, H., Yamaoka, H., & Sode, K. (2013). Direct electron transfer type disposable sensor strip for glucose sensing employing an engineered FAD glucose dehydrogenase. Enzyme and Microbial Technology, 52(2), 123–128. https://doi.org/10.1016/j.enzmictec.2012.11.002

Ferri, S., Miyamoto, Y., Sakaguchi-Mikami, A., Tsugawa, W., & Sode, K. (2013). Engineering Fructosyl Peptide Oxidase to Improve Activity Toward the Fructosyl Hexapeptide Standard for HbA1c Measurement. Molecular Biotechnology, 54(3), 939–943. https://doi.org/10.1007/s12033-012-9644-2

Sakaguchi-Mikami, A., Ferri, S., Katayama, S., Tsugawa, W., & Sode, K. (2013). Identification and functional analysis of fructosyl amino acid-binding protein from Gram-positive bacterium Arthrobacter sp. Journal of Applied Microbiology, 114(5), 1449–1456. https://doi.org/10.1111/jam.12152

Kojima, K., Kobayashi, T., Tsugawa, W., Ferri, S., & Sode, K. (2013). Mutational analysis of the oxygen-binding site of cholesterol oxidase and its impact on dye-mediated dehydrogenase activity. Journal of Molecular Catalysis B-Enzymatic, 88, 41–46. https://doi.org/10.1016/j.molcatb.2012.11.001

Yoshida, W., Kobayashi, N., Sasaki, Y., Ikebukuro, K., & Sode, K. (2013). Partial Peptide of alpha-Synuclein Modified with Small-Molecule Inhibitors Specifically Inhibits Amyloid Fibrillation of alpha-Synuclein. International Journal of Molecular Sciences, 14(2), 2590–2600. https://doi.org/10.3390/ijms14022590

Kim, J., Sasaki, Y., Yoshida, W., Kobayashi, N., Veloso, A. J., Kerman, K., … Sode, K. (2013). Rapid Cytotoxicity Screening Platform for Amyloid Inhibitors Using a Membrane-Potential Sensitive Fluorescent Probe. Analytical Chemistry, 85(1), 185–192. https://doi.org/10.1021/ac302442q

Abe, K., Yoshida, W., Terada, K., Yagi-Ishii, Y., Ferri, S., Ikebukuro, K., & Sode, K. (2013). Screening of Peptide Ligands for Pyrroloquinoline Quinone Glucose Dehydrogenase Using Antagonistic Template-Based Biopanning. International Journal of Molecular Sciences, 14(12), 23244–23256. https://doi.org/10.3390/ijms141223244

Kojima, K., Mikami-Sakaguchi, A., Kameya, M., Miyamoto, Y., Ferri, S., Tsugawa, W., & Sode, K. (2013). Substrate specificity engineering of Escherichia coli derived fructosamine 6-kinase. Biotechnology Letters, 35(2), 253–258. https://doi.org/10.1007/s10529-012-1062-9

Hanashi, T., Yamazaki, T., Tsugawa, W., Ikebukuro, K., & Sode, K. (2012). BioLC-Oscillator: A Self-Powered Wireless Glucose-Sensing System with the Glucose Dependent Resonance Frequency. Electrochemistry, 80(5), 367–370. https://doi.org/10.5796/electrochemistry.80.367

Ferri, S., & Sode, K. (2012). Biomolecular Engineering of Biosensing Molecules - The Challenges in Creating Sensing Molecules for Glycated Protein Biosensing. Electrochemistry, 80(5), 293–298. https://doi.org/10.5796/electrochemistry.80.293

Horaguchi, Y., Saito, S., Kojima, K., Tsugawa, W., Ferri, S., & Sode, K. (2012). Construction of Mutant Glucose Oxidases with Increased Dye-Mediated Dehydrogenase Activity. International Journal of Molecular Sciences, 13(11), 14149–14157. https://doi.org/10.3390/ijms131114149

Kim, S., Nibe, E., Tsugawa, W., Kojima, K., Ferri, S., & Sode, K. (2012). Construction of engineered fructosyl peptidyl oxidase for enzyme sensor applications under normal atmospheric conditions. Biotechnology Letters, 34(3), 491–497. https://doi.org/10.1007/s10529-011-0787-1

Abe, K., Kumagai, T., Takahashi, C., Kezuka, A., Murakami, Y., Osawa, Y., … Ikebukuro, K. (2012). Detection of Pathogenic Bacteria by Using Zinc Finger Protein Fused with Firefly Luciferase. Analytical Chemistry, 84(18), 8028–8032. https://doi.org/10.1021/ac3018845

Abe, K., Kiyohara, C., Saito, Y., Sode, K., & Ikebukuro, K. (2012). Electrochemical SNP Detection Using Glucose Dehydrogenase. Electrochemistry, 80(5), 345–347. https://doi.org/10.5796/electrochemistry.80.345

Tsugawa, W., Shimizu, H., Tatara, M., Ueno, Y., Kojima, K., & Sode, K. (2012). Nitrous Oxide Sensing using Oxygen-Insensitive Direct-Electron-Transfer-Type Nitrous Oxide Reductase. Electrochemistry, 80(5), 371–374. https://doi.org/10.5796/electrochemistry.80.371

Tsukakoshi, K., Abe, K., Sode, K., & Ikebukuro, K. (2012). Selection of DNA Aptamers That Recognize alpha-Synuclein Oligomers Using a Competitive Screening Method. Analytical Chemistry, 84(13), 5542–5547. https://doi.org/10.1021/ac300330g

Ueda, T., Nomoto, N., Koga, M., Ogasa, H., Ogawa, Y., Matsumoto, M., … Shimada, I. (2012). Structural Basis of Efficient Electron Transport between Photosynthetic Membrane Proteins and Plastocyanin in Spinach Revealed Using Nuclear Magnetic Resonance. Plant Cell, 24(10), 4173–4186. https://doi.org/10.1105/tpc.112.102517

Abe, K., Ogasawara, D., Yoshida, W., Sode, K., & Ikebukuro, K. (2011). Aptameric sensors based on structural change for diagnosis. Faraday Discussions, 149, 93–105. https://doi.org/10.1039/c005359g

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Hanashi, T., Yamazaki, T., Tsugawa, W., Ikebukuro, K., & Sode, K. (2011). BioRadioTransmitter: A self-powered wireless glucose-sensing system. Journal of Diabetes Science and Technology, 5(5), 1030–1035. https://doi.org/10.1177/193229681100500502

Sakaguchi-Mikami, A., Taniguchi, A., Sode, K., & Yamazaki, T. (2011). Construction of a Novel Glucose-Sensing Molecule Based on a Substrate-Binding Protein for Intracellular Sensing. Biotechnology and Bioengineering, 108(4), 725–733. https://doi.org/10.1002/bit.23006

Morita, Y., Yoshida, W., Savory, N., Han, S. W., Tera, M., Nagasawa, K., … Ikebukuro, K. (2011). Development of a novel biosensing system based on the structural change of a polymerized guanine-quadruplex DNA nanostructure. Biosensors & Bioelectronics, 26(12), 4837–4841. https://doi.org/10.1016/j.bios.2011.05.050

Madou, M., Hoff, A., Landheer, D., Nagahara, L., Sode, K., Thundat, T., & Wang, C. (2011). ECS Transactions: Preface. ECS Transactions, 35(7). Retrieved from http://www.scopus.com/inward/record.url?eid=2-s2.0-79960806989&partnerID=MN8TOARS

Kokko, C., Sode, K. J., Brito, A. F., Hovey, R. C., & Berthiaume, R. (2011). Effect of time of cutting and maceration on forage composition, nutrient flow, microbial protein synthesis, and digestibility in dual-flow continuous culture. Canadian Journal of Animal Science, 91(3), 486–487. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000294744800042&KeyUID=WOS:000294744800042

Nagae, D., Nakajima, M., Ferri, S., & Sode, K. (2011). Glucose Specific GDH-PQQ based Sensor Strip: Application of Engineered GDH-PQQ Harboring a de novo Designed Loop Region. Bioelectronics, Biointerfaces, and Biomedical Applications 4, 35(7), 117–119. https://doi.org/10.1149/1.3571983

Sakaguchi-Mikami, A., Ferri, S., Tsugawa, W., & Sode, K. (2011). Hemoglobin A1c biosensors. Japanese Journal of Clinical Chemistry, 40(4), 304–311. Retrieved from http://www.scopus.com/inward/record.url?eid=2-s2.0-82155186699&partnerID=MN8TOARS

Ferri, S., Kojima, K., & Sode, K. (2011). Review of glucose oxidases and glucose dehydrogenases: A bird's eye view of glucose sensing enzymes. Journal of Diabetes Science and Technology, 5(5), 1068–1076. https://doi.org/10.1177/193229681100500507

Mori, K., Nakajima, M., Kojima, K., Murakami, K., Ferri, S., & Sode, K. (2011). Screening of Aspergillus-derived FAD-glucose dehydrogenases from fungal genome database. Biotechnology Letters, 33(11), 2255–2263. https://doi.org/10.1007/s10529-011-0694-5

Ferri, S., Nibe, E., Miyamoto, Y., Kim, S., Tsugawa, W., & Sode, K. (2011). Tuning Fructosyl Peptidyl Oxidase into Dehydrogenase and Its Application for the Construction of an Enzyme Electrode. Bioelectronics, Biointerfaces, and Biomedical Applications 4, 35(7), 113–116. https://doi.org/10.1149/1.3571982

Desriani, Ferri, S., & Sode, K. (2010). Amino acid substitution at the substrate-binding subsite alters the specificity of the Phanerochaete chrysosporium cellobiose dehydrogenase. Biochemical and Biophysical Research Communications, 391(2), 1246–1250. https://doi.org/10.1016/j.bbrc.2009.12.052

Abe, K., Sode, K., & Ikebukuro, K. (2010). Constructing an improved pyrroloquinoline quinone glucose dehydrogenase binding aptamer for enzyme labeling. Biotechnology Letters, 32(9), 1293–1298. https://doi.org/10.1007/s10529-010-0292-y

Kim, S., Nibe, E., Ferri, S., Tsugawa, W., & Sode, K. (2010). Engineering of dye-mediated dehydrogenase property of fructosyl amino acid oxidases by site-directed mutagenesis studies of its putative proton relay system. Biotechnology Letters, 32(8), 1123–1129. https://doi.org/10.1007/s10529-010-0267-z

Desriani, Ferri, S., & Sode, K. (2010). Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli. Biotechnology Letters, 32(6), 855–859. https://doi.org/10.1007/s10529-010-0215-y

Kim, S., Ferri, S., Tsugawa, W., Mori, K., & Sode, K. (2010). Motif-Based Search for a Novel Fructosyl Peptide Oxidase From Genome Databases. Biotechnology and Bioengineering, 106(3), 358–366. https://doi.org/10.1002/bit.22710

Kim, J., Kobayashi, M., Fukuda, M., Ogasawara, D., Kobayashi, N., Han, S., … Sode, K. (2010). Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins. Prion, 4(1). https://doi.org/10.4161/pri.4.1.10889

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Nonaka, Y., Sode, K., & Ikebukuro, K. (2010). Screening and Improvement of an Anti-VEGF DNA Aptamer. Molecules, 15(1), 215–225. https://doi.org/10.3390/molecules15010215

Tsukakoshi, K., Harada, R., Sode, K., & Ikebukuro, K. (2010). Screening of DNA aptamer which binds to alpha-synuclein. Biotechnology Letters, 32(5), 643–648. https://doi.org/10.1007/s10529-010-0200-5

Savory, N., Abe, K., Sode, K., & Ikebukuro, K. (2010). Selection of DNA aptamer against prostate specific antigen using a genetic algorithm and application to sensing. Biosensors & Bioelectronics, 26(4), 1386–1391. https://doi.org/10.1016/j.bios.2010.07.057

Kim, J., Harada, R., Kobayashi, M., Kobayashi, N., & Sode, K. (2010). The inhibitory effect of pyrroloquinoline quinone on the amyloid formation and cytotoxicity of truncated alpha-synuclein. Molecular Neurodegeneration, 5(1). https://doi.org/10.1186/1750-1326-5-20

Yoshimatsu, K., Reimhult, K., Krozer, A., Mosbach, K., Sode, K., & Ye, L. (2010). Uniform molecularly imprinted microspheres and nanoparticles prepared by precipitation polymerization: The control of particle size suitable for different analytical applications (vol 584, pg 112, 2007). Analytica Chimica Acta, 657(2), 215. https://doi.org/10.1016/j.aca.2009.10.032

Endo, H., Takahashi, E., Murata, M., Ohnuki, H., Ren, H., Tsugawa, W., & Sode, K. (2010). Wireless monitoring of blood glucose levels in flatfish with a needle biosensor. Fisheries Science, 76(4), 687–694. https://doi.org/10.1007/s12562-010-0256-0

Fukasawa, M., Yoshida, W., Yamazaki, H., Sode, K., & Ikebukuro, K. (2009). An Aptamer-Based Bound/Free Separation System for Protein Detection. Electroanalysis, 21(11), 1297–1302. https://doi.org/10.1002/elan.200804555

Hanashi, T., Yamazaki, T., Tsugawa, W., Ferri, S., Nakayama, D., Tomiyama, M., … Sode, K. (2009). BioCapacitor-A novel category of biosensor. Biosensors & Bioelectronics, 24(7), 1837–1842. https://doi.org/10.1016/j.bios.2008.09.014

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Osawa, Y., Takase, M., Sode, K., & Ikebukuro, K. (2009). DNA Aptamers that Bind to PQQGDH as an Electrochemical Labeling Tool. Electroanalysis, 21(11), 1303–1308. https://doi.org/10.1002/elan.200804559

Ogasawara, D., Hachiya, N. S., Kaneko, K., Sode, K., & Ikebukuro, K. (2009). Detection system based on the conformational change in an aptamer and its application to simple bound/free separation. Biosensors & Bioelectronics, 24(5), 1372–1376. https://doi.org/10.1016/j.bios.2008.07.082

Yagi, Y. I., Abe, K., Ikebukuro, K., & Sode, K. (2009). Kinetic Mechanism and Inhibitor Characterization of WNK1 Kinase. Biochemistry, 48(43), 10255–10266. https://doi.org/10.1021/bi900666n

Ferri, S., Kim, S., Tsugawa, W., & Sode, K. (2009). Review of fructosyl amino acid oxidase engineering research: A glimpse into the future of hemoglobin A1c biosensing. Journal of Diabetes Science and Technology, 3(3), 585–592. https://doi.org/10.1177/193229680900300324

Yoshida, W., Mochizuki, E., Takase, M., Hasegawa, H., Morita, Y., Yamazaki, H., … Ikebukuro, K. (2009). Selection of DNA aptamers against insulin and construction of an aptameric enzyme subunit for insulin sensing. Biosensors & Bioelectronics, 24(5), 1116–1120. https://doi.org/10.1016/j.bios.2008.06.016

Taneoka, A., Sakaguchi-Mikami, A., Yamazaki, T., Tsugawa, W., & Sode, K. (2009). The construction of a glucose-sensing luciferase. Biosensors & Bioelectronics, 25(1), 76–81. https://doi.org/10.1016/j.bios.2009.06.004

Harada, R., Kobayashi, N., Kim, J., Nakamura, C., Han, S.-W., Ikebukuro, K., & Sode, K. (2009). The effect of amino acid substitution in the imperfect repeat sequences of alpha-synuclein on fibrillation. Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1792(10), 998–1003. https://doi.org/10.1016/j.bbadis.2009.06.010

Kobayashi, N., Kim, J., Ikebukuro, K., & Sode, K. (2009). The inhibition of amyloid fibrillation using the proteolytic products of PQQ-modified α-synuclein. Open Biotechnology Journal, 3, 40–45. https://doi.org/10.2174/1874070700903010040

Endo, H., Yonemori, Y., Hibi, K., Ren, H., Hayashi, T., Tsugawa, W., & Sode, K. (2009). Wireless enzyme sensor system for real-time monitoring of blood glucose levels in fish. Biosensors & Bioelectronics, 24(5), 1417–1423. https://doi.org/10.1016/j.bios.2008.08.038

Osawa, Y., Ikebukuro, K., Kumagai, T., Motoki, H., Matsuo, T., Horiuchi, M., & Sode, K. (2009). Zn finger-based direct detection system for PCR products of Salmonella spp. and the Influenza A virus. Biotechnology Letters, 31(5), 735. https://doi.org/10.1007/s10529-009-9955-y

Osawa, Y., Ikebukuro, K., & Sode, K. (2009). Zn finger-based direct detection system for PCR products of Salmonella spp. and the Influenza A virus. Biotechnology Letters, 31(5), 725–733. https://doi.org/10.1007/s10529-009-9927-2

Osawa, Y., Ikebukuro, K., Kobayashi, N., Han, S., Nakamura, C., & Sode, K. (2008). Aggregation and fibrillation study of a-synuclein under applied voltage. Electrochemistry, 76(8), 614–618. https://doi.org/10.5796/electrochemistry.76.614

Ikebukuro, K., Yoshida, W., & Sode, K. (2008). Aptameric enzyme subunit for homogeneous DNA sensing. Biotechnology Letters, 30(2), 243–252. https://doi.org/10.1007/s10529-007-9526-z

Okuda-Shimazaki, J., Kakehi, N., Yamazaki, T., Tomiyama, M., & Sode, K. (2008). Biofuel cell system employing thermostable glucose dehydrogenase. Biotechnology Letters, 30(10), 1753–1758. https://doi.org/10.1007/s10529-008-9749-7

Ikebukuro, K., Yoshida, W., & Sode, K. (2008). Biosensors Using the Aptameric Enzyme Subunit: The Use of Aptamers in the Allosteric Control of Enzymes. In Aptamers in Bioanalysis (pp. 129–138). https://doi.org/10.1002/9780470380772.ch6

Yamazaki, T., Okuda-Shimazaki, J., Sakata, C., Tsuya, T., & Sode, K. (2008). Construction and Characterization of Direct Electron Transfer-Type Continuous Glucose Monitoring System Employing Thermostable Glucose Dehydrogenase Complex. Analytical Letters, 41(13), 2363–2373. https://doi.org/10.1080/00032710802350567

Ishikawa, M., Yamamura, S., Ikeda, R., Takamura, Y., Sode, K., Tamiya, E., & Tomiyama, M. (2008). Development of a compact stacked flatbed reactor with immobilized high-density bacteria for hydrogen production. International Journal of Hydrogen Energy, 33(5), 1593–1597. https://doi.org/10.1016/j.ijhydene.2007.09.035

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Hasegawa, H., Taira, K.-ichi, Sode, K., & Ikebukuro, K. (2008). Improvement of aptamer affinity by dimerization. Sensors, 8(2), 1090–1098. https://doi.org/10.3390/s8021090

Yoshida, W., Sode, K., & Ikebukuro, K. (2008). Label-free homogeneous detection of immunoglobulin E by an aptameric enzyme subunit. Biotechnology Letters, 30(3), 421–425. https://doi.org/10.1007/s10529-007-9575-3

Tatara, M., Makiuchi, T., Ueno, Y., Goto, M., & Sode, K. (2008). Methanogenesis from acetate and propionate by thermophilic down-flow anaerobic packed-bed reactor. Bioresource Technology, 99(11), 4786–4795. https://doi.org/10.1016/j.biortech.2007.09.069

Kobayashi, N., Han, S., Nakamura, C., & Sode, K. (2008). Nanostructure fabrication based on engineered α-synuclein. Nanobiotechnology, 4(1-4), 50–55. https://doi.org/10.1007/s12030-008-9011-3

Yamazaki, T., Ohta, S., & Sode, K. (2008). Operational condition of a molecular imprinting catalyst-based fructosyl-valine sensor. Electrochemistry, 76(8), 590–593. https://doi.org/10.5796/electrochemistry.76.590

Sode, K., Tsugawa, W., Aoyagi, M., Rajashekhara, E., & Watanabe, K. (2008). Propionate sensor using coenzyme-A transferase and acyl-CoA oxidase. Protein and Peptide Letters, 15(8), 779–781. https://doi.org/10.2174/092986608785203737

Hasegawa, H., Sode, K., & Ikebukuro, K. (2008). Selection of DNA aptamers against VEGF(165) using a protein competitor and the aptamer blotting method. Biotechnology Letters, 30(5), 829–834. https://doi.org/10.1007/s10529-007-9629-6

Yamaoka, H., Yamashita, Y., Ferri, S., & Sode, K. (2008). Site directed mutagenesis studies of FAD-dependent glucose dehydrogenase catalytic subunit of Burkholderia cepacia. Biotechnology Letters, 30(11), 1967–1972. https://doi.org/10.1007/s10529-008-9777-3

Osawa, Y., Ikebukuro, K., Motoki, H., Matsuo, T., Horiuchi, M., & Sode, K. (2008). The simple and rapid detection of specific PCR products from bacterial genomes using Zn finger proteins. Nucleic Acids Research, 36(11). https://doi.org/10.1093/nar/gkn274

Osawa, Y., Motoki, H., Matsuo, T., Horiuchi, M., Sode, K., & Ikebukuro, K. (2008). Zinc finger protein-based detection system of PCR products for pathogen diagnosis. Nucleic Acids Symposium Series (2004), (52), 23–24. https://doi.org/10.1093/nass/nrn012

Kakehi, N., Yamazaki, T., Tsugawa, W., & Sode, K. (2007). A novel wireless glucose sensor employing direct electron transfer principle based enzyme fuel cell. Biosensors & Bioelectronics, 22(9-10), 2250–2255. https://doi.org/10.1016/j.bios.2006.11.004

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Chino, S., Sakaguchi, A., Yamoto, R., Ferri, S., & Sode, K. (2007). Branched-chain amino acid biosensing using fluorescent modified engineered leucine/isoleucine/valine binding protein. International Journal of Molecular Sciences, 8(6), 513–525. https://doi.org/10.3390/i8060513

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Yagi, Y., Terada, K., Noma, T., Ikebukuro, K., & Sode, K. (2007). In silico panning for a non-competitive peptide inhibitor. Bmc Bioinformatics, 8. https://doi.org/10.1186/1471-2105-8-11

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Ueno, Y., Tatara, M., Fukui, H., Makiuchi, T., Goto, M., & Sode, K. (2007). Production of hydrogen and methane from organic solid wastes by phase-separation of anaerobic process. Bioresource Technology, 98(9), 1861–1865. https://doi.org/10.1016/j.biortech.2006.06.017

Yamaoka, H., & Sode, K. (2007). SPCE based glucose sensor employing novel thermostable glucose dehydrogenase, FADGDH: Blood glucose measurement with 150nL sample in one second. Journal of Diabetes Science and Technology, 1(1), 28–35. https://doi.org/10.1177/193229680700100105

Ogasawara, D., Hasegawa, H., Kaneko, K., Sode, K., & Ikebukuro, K. (2007). Screening of DNA aptamer against mouse prion protein by competitive selection. Prion, 1(4), 248–254. https://doi.org/10.4161/pri.1.4.5803

Ikebukuro, K., Hasegawa, H., & Sode, K. (2007). Selection and characterization of DNA aptamers against VEGF165 with aptamer blotting method and its application. Nucleic Acids Symposium Series (2004), (51), 399–400. https://doi.org/10.1093/nass/nrm200

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Ikebukuro, K., Kumagai, T., Motoki, H., Osawa, Y., Matuo, T., Horiuchi, M., & Sode, K. (2007). Specific detection of PCR product from Legionella pneumophila strain Philadelphia1 using zinc finger protein Sp2. Nucleic Acids Symposium Series (2004), (51), 285–286. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=MEDLINE&KeyUT=MEDLINE:18029698&KeyUID=MEDLINE:18029698

Okuda, J., Yamazaki, T., Fukasawa, M., Kakehi, N., & Sode, K. (2007). The application of engineered glucose dehydrogenase to a direct electron-transfer-type continuous glucose monitoring system and a compartmentless biofuel cell. Analytical Letters, 40(3), 431–440. https://doi.org/10.1080/00032710600964692

Yoshimatsu, K., Reimhult, K., Krozer, A., Mosbach, K., Sode, K., & Ye, L. (2007). Uniform molecularly imprinted microspheres and nanoparticles prepared by precipitation polymerization: The control of particle size suitable for different analytical applications. Analytica Chimica Acta, 584(1), 112–121. https://doi.org/10.1016/j.aca.2006.11.004

Tachino, A., Igarashi, S., & Sode, K. (2007). W-motif exchange between beta-propeller proteins. Protein Journal, 26(3), 153–158. https://doi.org/10.1007/s10930-006-9056-x

Noma, T., Ikebukuro, K., Sode, K., Ohkubo, T., Sakasegawa, Y., Hachiya, N., & Kaneko, K. (2006). A screening method for DNA aptamers that bind to specific, unidentified protein in tissue samples. Biotechnology Letters, 28(17), 1377–1381. https://doi.org/10.1007/s10529-006-9106-7

Miura, S., Ferri, S., Tsugawa, W., Kiin, S., & Sode, K. (2006). Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis. Biotechnology Letters, 28(23), 1895–1900. https://doi.org/10.1007/s10529-006-9173-9

Ikebukuro, K., Yoshida, W., Noma, T., & Sode, K. (2006). Analysis of the evolution of the thrombin-inhibiting DNA aptamers using a genetic algorithm. Biotechnology Letters, 28(23), 1933–1937. https://doi.org/10.1007/s10529-006-9174-8

Yoshida, W., Sode, K., & Ikebukuro, K. (2006). Aptameric enzyme subunit for biosensing based on enzymatic activity measurement. Analytical Chemistry, 78(10), 3296–3303. https://doi.org/10.1021/ac060254o

Noma, T., Sode, K., & Ikebukuro, K. (2006). Characterization and application of aptamers for Taq DNA polymerase selected using an evolution-mimicking algorithm. Biotechnology Letters, 28(23), 1939–1944. https://doi.org/10.1007/s10529-006-9178-4

Tsuya, T., Ferri, S., Fujikawa, M., Yamaoka, H., & Sode, K. (2006). Cloning and functional expression of glucose dehydrogenase complex of Burkholderia cepacia in Escherichia coli. Journal of Biotechnology, 123(2), 127–136. https://doi.org/10.1016/j.jbiotec.2005.10.017

Ishikawa, M., Yamamura, S., Takamura, Y., Sode, K., Tamiya, E., & Tomiyama, M. (2006). Development of a compact high-density microbial hydrogen reactor for portable bio-fuel cell system. International Journal of Hydrogen Energy, 31(11), 1484–1489. https://doi.org/10.1016/j.ijhydene.2006.06.014

Yoshida, W., Sode, K., & Ikebukuro, K. (2006). Homogeneous DNA sensing using enzyme-inhibiting DNA aptamers. Biochemical and Biophysical Research Communications, 348(1), 245–252. https://doi.org/10.1016/j.bbrc.2006.07.069

Kobayashi, M., Kim, J., Kobayashi, N., Han, S., Nakamura, C., Ikebukuro, K., & Sode, K. (2006). Pyrroloquinoline quinone (PQQ) prevents fibril formation of alpha-synuclein. Biochemical and Biophysical Research Communications, 349(3), 1139–1144. https://doi.org/10.1016/j.bbrc.2006.08.144

Rajashekhara, E., Hosoda, A., Sode, K., Ikenaga, H., & Watanabe, K. (2006). Volatile fatty acid-sensing system involving coenzyme-A transferase. Biotechnology Progress, 22(1), 334–337. https://doi.org/10.1021/bp050240o

Meng, Z. H., Yamazaki, T., & Sode, K. (2005). Construction of artificial cyclic amide amidohydrolases using molecular imprinting technique. Biotechnology Letters, 27(7), 471–475. https://doi.org/10.1007/s10529-005-2223-x

Yuhashi, N., Tomiyama, M., Okuda, J., Igarashi, S., Ikebukuro, K., & Sode, K. (2005). Development of a novel glucose enzyme fuel cell system employing protein engineered PQQ glucose dehydrogenase. Biosensors & Bioelectronics, 20(10), 2145–2150. https://doi.org/10.1016/j.bios.2004.08.017

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Tatara, M., Yamazawa, A., Ueno, Y., Fukui, H., Goto, M., & Sode, K. (2005). High-rate thermophilic methane fermentation on short-chain fatty acids in a down-flow anaerobic packed-bed reactor. Bioprocess and Biosystems Engineering, 27(2), 105–113. https://doi.org/10.1007/s00449-004-0387-8

Tanaka, S., Igarashi, S., Ferri, S., & Sode, K. (2005). Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface. BMC Biochemistry, 6. https://doi.org/10.1186/1471-2091-6-1

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Sakaguchi, A., Ferri, S., & Sode, K. (2005). SocA is a novel periplasmic binding protein for fructosyl amino acid. Biochemical and Biophysical Research Communications, 336(4), 1074–1080. https://doi.org/10.1016/j.bbrc.2005.08.230

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Igarashi, S., & Sode, K. (2004). Construction and characterization of heterodimeric, soluble quinoprotein glucose dehydrooenase. Journal of Biochemical and Biophysical Methods, 61(3), 331–338. https://doi.org/10.1016/j.jbbm.2004.06.009

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Ikebukuro, W., & Sode, K. (2004). Highly sensitive detection of DNA hybridization using enzyme electrode. Electrochemistry, 72(8), 598–600. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000223239200012&KeyUID=WOS:000223239200012

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Igarashi, S., & Sode, K. (2003). Stabilization of quaternary structure of water-soluble quinoprotein glucose dehydrogenase. Molecular Biotechnology, 24(2), 97–103. https://doi.org/10.1385/MB:24:2:97

Koh, H., Igarashi, S., & Sode, K. (2003). Surface charge engineering of PQQ glucose dehydrogenase for downstream processing. Biotechnology Letters, 25(20), 1695–1701. https://doi.org/10.1023/A:1026038201193

Ikebukuro, K., Kohiki, Y., & Sode, K. (2002). Amperometric DNA sensor using the pyrroquinoline quinone glucose dehydrogenase-avidin conjugate. Biosensors & Bioelectronics, 17(11-12), 1075–1080. https://doi.org/10.1016/S0956-5663(02)00101-X

Hamafuji, T., Tsugawa, W., & Sode, K. (2002). Clinical application of the serum 1,5-anhydroglucitol assay method using glucose 3-dehydrogenase. Journal of Clinical Laboratory Analysis, 16(6), 299–303. https://doi.org/10.1002/jcla.10054

Sode, K., Igarashi, S., Morimoto, A., & Yoshida, H. (2002). Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity. Biocatalysis and Biotransformation, 20(6), 405–412. https://doi.org/10.1080/1024242021000058694

Ogawa, K., Stollner, D., Scheller, F., Warsinke, A., Ishimura, F., Tsugawa, W., … Sode, K. (2002). Development of a flow-injection analysis (FIA) enzyme sensor for fructosyl amine monitoring. Analytical and Bioanalytical Chemistry, 373(4-5), 211–214. https://doi.org/10.1007/s00216-002-1319-6

Hamafuji, T., Tsugawa, W., & Sode, K. (2002). Isolation and identification of N-carbamoyl-beta-D-glucopyranosylamine from human serum. Journal of Biochemistry, Molecular Biology, and Biophysics : JBMBB : the Official Journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB), 6(5), 315–318. https://doi.org/10.1080/1025814021000003247

Hamafuji, T., Takano, Y., Tsugawa, W., & Sode, K. (2002). Multi-sugar analysis system using a novel glucose-3-dehydrogenase electrode. Instrumentation Science & Technology, 30(1), 97–105. https://doi.org/10.1081/CI-100108774

Yoshida, H., Araki, N., Tomisaka, A., & Sode, K. (2002). Secretion of water soluble pyrroloquinoline quinone glucose dehydrogenase by recombinant Pichia pastoris. Enzyme and Microbial Technology, 30(3), 312–318. https://doi.org/10.1016/S0141-0229(01)00492-6

Okuda, J., Wakai, J., & Sode, K. (2002). The application of cytochromes as the interface molecule to facilitate the electron transfer for PQQ glucose dehydrogenase employing mediator type glucose sensor. Analytical Letters, 35(9), 1465–1478. https://doi.org/10.1081/AL-120006723

Sode, K., Takahashi, Y., Ohta, S., Tsugawa, W., & Yamazaki, T. (2001). A new concept for the construction of an artificial dehydrogenase for fructosylamine compounds and its application for an amperometric fructosylamine sensor. Analytica Chimica Acta, 435(1), 151–156. https://doi.org/10.1016/S0003-2670(00)01304-0

Yamazaki, T., Meng, Z., Mosbach, K., & Sode, K. (2001). A novel amperometric sensor for organophosphotriester insecticides detection employing catalytic polymer mimicking phosphotriesterase catalytic center. Electrochemistry, 69(12), 969–972. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000172742300016&KeyUID=WOS:000172742300016

Yamazaki, T., Tsugawa, W., & Sode, K. (2001). Biodegradation of formaldehyde by a formaldehyde-resistant bacterium isolated from seawater. Applied Biochemistry and Biotechnology, 91-3, 213–217. https://doi.org/10.1385/ABAB:91-93:1-9:213

Kojima, K., Tsugawa, W., & Sode, K. (2001). Cloning and expression of glucose 3-dehydrogenase from Halomonas sp alpha-15 in Escherichia coli. Biochemical and Biophysical Research Communications, 282(1), 21–27. https://doi.org/10.1006/bbrc.2001.4511

Sode, K., Akaike, E., Sugiura, H., & Tsugawa, W. (2001). Enzymatic synthesis of a novel trehalose derivative, 3,3 '-diketotrehalose, and its potential application as the trehalase enzyme inhibitor. Febs Letters, 489(1), 42–45. https://doi.org/10.1016/S0014-5793(00)02427-3

Tsugawa, W., Ogawa, K., Ishimura, F., & Sode, K. (2001). Fructosyl amine sensing based on Prussian blue modified enzyme electrode. Electrochemistry, 69(12), 973–975. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000172742300017&KeyUID=WOS:000172742300017

Witarto, A. B., & Sode, K. (2001). Increasing the hydrophobic interaction between terminal W-motifs enhances the stability of Salmonella typhimurium sialidase. A general strategy for the stabilization of beta-propeller protein fold. Protein Engineering, 14(11), 891–896. https://doi.org/10.1093/protein/14.11.891

Sode, K., Ishimura, F., & Tsugawa, W. (2001). Screening and characterization of fructosyl-valine-utilizing marine microorganisms. Marine Biotechnology, 3(2), 126–132. https://doi.org/10.1007/s101260000065

Yamazaki, T., Yilmaz, E., Mosbach, K., & Sode, K. (2001). Towards the use of molecularly imprinted polymers containing imidazoles and bivalent metal complexes for the detection and degradation of organophosphotriester pesticides. Analytica Chimica Acta, 435(1), 209–214. https://doi.org/10.1016/S0003-2670(01)00933-3

Takeuchi, A., & Sode, K. (2000). A Salmonella detection system using an engineered DNA binding protein that specifically captured a DNA sequence. Analytical Chemistry, 72(13), 2809–2813. https://doi.org/10.1021/ac991232n

Takahashi, Y., Igarashi, S., Nakazawa, Y., Tsugawa, W., & Sode, K. (2000). Construction and characterization of glucose enzyme sensor employing engineered water soluble PQQ glucose dehydrogenase with improved thermal stability. Electrochemistry, 68(11), 907–911. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000165420800021&KeyUID=WOS:000165420800021

Yoshida, H., Iguchi, T., & Sode, K. (2000). Construction of multi-chimeric pyrroloquinoline quinone glucose dehydrogenase with improved enzymatic properties and application in glucose monitoring. Biotechnology Letters, 22(18), 1505–1510. https://doi.org/10.1023/A:1005658316948

Tsugawa, W., Ishimura, F., Ogawa, K., & Sode, K. (2000). Development of an enzyme sensor utilizing a novel fructosyl amine oxidase from a marine yeast. Electrochemistry, 68(11), 869–871. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000165420800009&KeyUID=WOS:000165420800009

Sode, K., Sugiura, H., Tsugawa, W., Watazu, Y., & Hamafuji, T. (2000). Enzyme electrochemical preparation of a 3-keto derivative of 1,5-anhydro-D-glucitol using glucose-3-dehydrogenase. Applied Biochemistry and Biotechnology, 84-6, 947–954. https://doi.org/10.1385/ABAB:84-86:1-9:947

Yamazaki, T., Kojima, K., & Sode, K. (2000). Extended-range glucose sensor employing engineered glucose dehydrogenases. Analytical Chemistry, 72(19), 4689–4693. https://doi.org/10.1021/ac000151k

Masuko, M., Ohuchi, S., Sode, K., Ohtani, H., & Shimadzu, A. (2000). Fluorescence resonance energy transfer from pyrene to perylene labels for nucleic acid hybridization assays under homogeneous solution conditions. Nucleic Acids Research, 28(8), 34. https://doi.org/10.1093/nar/28.8.e34

Tsugawa, W., Nakamura, H., Sode, K., & Ohuchi, S. (2000). Improvement of enantioselectivity of chiral organophosphate insecticide hydrolysis by bacterial phosphotriesterase. Applied Biochemistry and Biotechnology, 84-6, 311–317. https://doi.org/10.1385/ABAB:84-86:1-9:311

Sode, K., Ootera, T., Shirahane, M., Witarto, A. B., Igarashi, S., & Yoshida, H. (2000). Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. Enzyme and Microbial Technology, 26(7), 491–496. https://doi.org/10.1016/S0141-0229(99)00196-9

Yoshida, H., & Sode, K. (2000). Novel approaches toward bioelectrochemical applications of genetically engineered proteins - 2. Engineering of substrate specificity of PQQ glucose dehydrogenase. Electrochemistry, 68(5), 348–352. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000087236200008&KeyUID=WOS:000087236200008

Yamazaki, T., Yasutake, N., & Sode, K. (2000). Surface deposition method; A novel protein immobilization procedure on a sensor surface. Electrochemistry, 68(11), 882–885. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000165420800013&KeyUID=WOS:000165420800013

Kojima, K., Witarto, A. B., & Sode, K. (2000). The production of soluble pyrroloquinoline quinone glucose dehydrogenase by Klebsiella pneumoniae, the alternative host of PQQ enzymes. Biotechnology Letters, 22(16), 1343–1347. https://doi.org/10.1023/A:1005615400089

Okuda, J., Yoshida, H., Kojima, K., Himi, M., & Sode, K. (2000). The role of conserved His775/781 in membrane-binding PQQ glucose dehydrogenase of Escherichia coli and Acinetobacter calcoaceticus. Journal of Biochemistry, Molecular Biology and Biophysics, 4(6), 415–422. Retrieved from http://www.scopus.com/inward/record.url?eid=2-s2.0-0034524811&partnerID=MN8TOARS

Sode, K., Shirahane, M., & Yoshida, H. (1999). Construction and characterization of a linked-dimeric pyrroloquinoline quinone glucose dehydrogenase. Biotechnology Letters, 21(8), 707–710. https://doi.org/10.1023/A:1005518610946

Sode, K., Watanabe, M., Makimoto, H., & Tomiyama, M. (1999). Construction and characterization of fermentative lactate dehydrogenase Escherichia coli mutant and its potential for bacterial hydrogen production. Applied Biochemistry and Biotechnology, 77-9, 317–323. https://doi.org/10.1385/ABAB:77:1-3:317

Igarashi, S., Ohtera, T., Yoshida, H., Witarto, A. B., & Sode, K. (1999). Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K-m values - Site-directed mutagenesis studies on the putative active site. Biochemical and Biophysical Research Communications, 264(3), 820–824. https://doi.org/10.1006/bbrc.1999.1157

Takeuchi, A., & Sode, K. (1999). Design of new primers that can detect Salmonella without decrease of detection threshold in the presence of contaminant organisms. Biotechnology Techniques, 13(1), 81–85. https://doi.org/10.1023/A:1008851814727

Kojima, K., Tsugawa, W., Hamahuji, T., Watazu, Y., & Sode, K. (1999). Effect of growth substrates on production of new soluble glucose 3-dehydrogenase in Halomonas (Deleya) sp alpha-15. Applied Biochemistry and Biotechnology, 77-9, 827–834. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000081133100076&KeyUID=WOS:000081133100076

Yoshida, H., Kojima, K., Witarto, A. B., & Sode, K. (1999). Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity. Protein Engineering, 12(1), 63–70. https://doi.org/10.1093/protein/12.1.63

Yamazaki, T., Tsugawa, W., & Sode, K. (1999). Increased thermal stability of glucose dehydrogenase by cross-linking chemical modification. Biotechnology Letters, 21(3), 199–202. https://doi.org/10.1023/A:1005455911753

Witarto, A. B., Oh-Uchi, S., Narita, M., & Sode, K. (1999). Secondary structure study of pyrroloquinoline quinone glucose dehydrogenase. Journal of Biochemistry, Molecular Biology and Biophysics, 2(3), 209–213. Retrieved from http://www.scopus.com/inward/record.url?eid=2-s2.0-0032956367&partnerID=MN8TOARS

Narita, M., Sode, K., & Ohuchi, S. (1999). Single amino acid preferences for specific locations at type-I alpha-turns in globular proteins. Bulletin of the Chemical Society of Japan, 72(8), 1807–1813. https://doi.org/10.1246/bcsj.72.1807

Witarto, A. B., Ohtera, T., & Sode, K. (1999). Site-directed mutagenesis study on the thermal stability of a chimeric PQQ glucose dehydrogenase and its structural interpretation. Applied Biochemistry and Biotechnology, 77-9, 159–168. https://doi.org/10.1385/ABAB:77:1-3:159

Yamazaki, T., Tsugawa, W., & Sode, K. (1999). Subunit analyses of a novel thermostable glucose dehydrogenase showing different temperature properties according to its quaternary structure. Applied Biochemistry and Biotechnology, 77-9, 325–335. https://doi.org/10.1385/ABAB:77:1-3:325

Sode, K., Yamamoto, Y., & Hatano, N. (1998). Construction of a marine cyanobacterial strain with increased heavy metal ion tolerance by in introducing exogenic metallothionein gene. Journal of Marine Biotechnology, 6(3), 174–177. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000075383800008&KeyUID=WOS:000075383800008

Sode, K., Watanabe, M., Makimoto, H., & Tomiyama, M. (1998). Effect of hydrogenase 3 over-expression and disruption of nitrate reductase on fermamentive hydrogen production in Escherichia coli - A metabolic engineering approach. Biohydrogen, 73–79. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000078629000009&KeyUID=WOS:000078629000009

Tsugawa, W., Ogasawara, N., & Sode, K. (1998). Fluorescent measurement of 1,5-anhydro-D-glucitol based on a novel marine bacterial glucose dehydrogenase. Enzyme and Microbial Technology, 22(4), 269–274. https://doi.org/10.1016/S0141-0229(97)00194-4

Narita, M., Sode, K., Ohuchi, S., Murakawa, Y., & Hitomi, M. (1998). Statistical characterization of eleven kinds of helix elements with amino acid residues in the middle of triplets. Bulletin of the Chemical Society of Japan, 71(2), 385–395. https://doi.org/10.1246/bcsj.71.385

Narita, M., Sode, K., Ohuchi, S., Hitomi, M., & Murakawa, Y. (1997). A new type of phi,psi-representation of the protein tertiary structure and the analysis of the amino acid preferences for specific locations at type-II beta-turn by using 8000 possible kinds of amino acid residues. Bulletin of the Chemical Society of Japan, 70(7), 1639–1648. https://doi.org/10.1246/bcsj.70.1639

Yamazaki, T., Tsugawa, W., & Sode, K. (1997). Alteration of substrate specificity of galactose oxidase by chemical cross-linking. Denki Kagaku, 65(6), 435–439. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1997XG00300003&KeyUID=WOS:A1997XG00300003

Ohuchi, S., Nakamura, H., Sugiura, H., Narita, M., & Sode, K. (1997). An optical resolution of racemic organophosphorous esters by phosphotriesterase-catalyzing hydrolysis. Applied Biochemistry and Biotechnology, 63-5, 659–665. https://doi.org/10.1007/BF02920464

Takeuchi, A., & Sode, K. (1997). Biochemical properties and colony formation patterns of salmonella-like strains. Biocontrol Science, 2(2), 93–97. https://doi.org/10.4265/bio.2.93

Sode, K., & Nakamura, H. (1997). Compatibility of phosphotriesterase from Flavobacterium sp. with detergents. Biotechnology Letters, 19(12), 1239–1242. https://doi.org/10.1023/A:1018402407802

Sode, K., & Yoshida, H. (1997). Construction and characterization of a chimeric Escherichia coli PQQ glucose dehydrogenase (PQQGDH) with increased EDTA tolerance. Denki Kagaku, 65(6), 444–451. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1997XG00300005&KeyUID=WOS:A1997XG00300005

Tsugawa, W., & Sode, K. (1997). Growth properties of a marine bacterium capable of assimilating 1,5-anhydro-D-glucitol as the sole carbon source. Journal of Marine Biotechnology, 5(4), 201–204. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1997XR47000003&KeyUID=WOS:A1997XR47000003

Sode, K., & Kojima, K. (1997). Improved substrate specificity and dynamic range for glucose measurement of Escherichia coli PQQ glucose dehydrogenase by site directed mutagenesis. Biotechnology Letters, 19(11), 1073–1077. https://doi.org/10.1023/A:1018428224215

Sode, K., Oonari, R., & Oozeki, M. (1997). Induction of a temperate marine cyanophage by heavy metal. Journal of Marine Biotechnology, 5(2-3), 178–180. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1997XJ35800021&KeyUID=WOS:A1997XJ35800021

Sode, K., & Yasutake, N. (1997). Preparation of lyophilized pyrroloquinoline quinone glucose dehydrogenase using trehalose as an additive. Biotechnology Techniques, 11(8), 577–580. https://doi.org/10.1023/A:1018494923558

Sode, K., Tsugawa, W., Yamazaki, T., Watanabe, M., Ogasawara, N., & Tanaka, M. (1996). A novel thermostable glucose dehydrogenase varying temperature properties by altering its quaternary structures. Enzyme and Microbial Technology, 19(2), 82–85. https://doi.org/10.1016/0141-0229(95)00170-0

Sode, K., Ohuchi, S., Nakamura, H., & Narita, M. (1996). A novel transesterification catalyzed by phosphotriesterase in an organic solvent. Biotechnology Letters, 18(8), 923–926. https://doi.org/10.1007/BF00154622

Sode, K., Hatano, N., & Tatara, M. (1996). Cloning of a marine cyanobacterial promoter for foreign gene expression using a promoter probe vector. Applied Biochemistry and Biotechnology, 59(3), 349–360. https://doi.org/10.1007/BF02783576

Sode, K., Togo, H., Yamazaki, T., Tsugawa, W., Ohuchi, S., Narita, M., & Yagiuda, K. (1996). Development of a novel conductometric determination of organophosphate insecticides using phosphotriesterase. Denki Kagaku, 64(12), 1234–1238. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1996VY99100005&KeyUID=WOS:A1996VY99100005

Sode, K., Ito, K., Witarto, A. B., Watanabe, K., Yoshida, H., & Postma, P. (1996). Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis. Journal of Biotechnology, 49(1-3), 239–243. https://doi.org/10.1016/0168-1656(96)01540-4

Sode, K., Burgess, J. G., & Matsunaga, T. (1996). Marine Biotechnology Based on Marine Microorganisms. In Advances in Molecular and Cell Biology (Vol. 15, pp. 95–102). https://doi.org/10.1016/S1569-2558(08)60302-1

Tsugawa, W., Horiuchi, S., Tanaka, M., Wake, H., & Sode, K. (1996). Purification of a marine bacterial glucose dehydrogenase from Cytophaga marinoflava and its application for measurement of 1,5-anhydro-D-glucitol. Applied Biochemistry and Biotechnology, 56(3), 301–310. https://doi.org/10.1007/BF02786960

Sode, K., Hayashi, T., Tatara, M., Hatano, N., Yoshida, H., Takeyama, H., … Matsunaga, T. (1996). Recovery of a marine cyanobacterial recombinant product using fish-feed organisms. Journal of Marine Biotechnology, 4(2), 82–86. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=BCI&KeyUT=BCI:BCI199799471382&KeyUID=BCI:BCI199799471382

Sode, K., Shimakita, T., Ohuchi, S., & Yamazaki, T. (1996). Stabilization of pyrroloquinoline quinone glucose dehydrogenase by cross-linking chemical modification. Biotechnology Letters, 18(9), 997–1002. https://doi.org/10.1007/BF00129720

Tsugawa, W., & Sode, K. (1995). A marine bacterial electrode for sensitive detection of 1,5-anhydro-D-glucitol. Denki Kagaku, 63(12), 1131–1133. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1995TK61200010&KeyUID=WOS:A1995TK61200010

Nakamura, C., Burgess, J. G., Sode, K., & Matsunaga, T. (1995). An iron-regulated gene, magA, encoding an iron transport protein of Magnetospirillum sp. strain AMB-1. Journal of Biological Chemistry, 270(47), 28392–28396. https://doi.org/10.1074/jbc.270.47.28392

Nakamura, C., Burgess, J. G., Sode, K., & Matsunaga, T. (1995). Analysis of a gene, magA, required for magnetite biomineralization in the bacterium Magnetospirillum sp. AMB-1. Bulletin De l'Institut Oceanographique (Monaco), 0(SPEC. ISSUE 14 PART 2), 121–126. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=BCI&KeyUT=BCI:BCI199698775342&KeyUID=BCI:BCI199698775342

NISHII, K., SODE, K., & KARUBE, I. (1995). CONTINUOUS 2-STEP BIOCONVERSION OF 4-OXOISOPHORONE (OIP) TO 4-HYDROXY-2,2,6-TRIMETHYLCYCLOHEXANONE (4-HTMCH) BY THERMOPHILIC BACTERIA. Biotechnology Letters, 17(8), 785–790. https://doi.org/10.1007/BF00129005

Sode, K., Yoshida, H., & Yasutake, N. (1995). Determination of the metal binding region of pyrroloquinoline quinone glucose dehydrogenase. Protein Engineering, 8(9), 51. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1995TL57300062&KeyUID=WOS:A1995TL57300062

SODE, K., SUGIMOTO, S., WATANABE, M., & TSUGAWA, W. (1995). EFFECT OF PQQ GLUCOSE-DEHYDROGENASE OVEREXPRESSION IN ESCHERICHIA-COLI ON SUGAR-DEPENDENT RESPIRATION. Journal of Biotechnology, 43(1), 41–44. https://doi.org/10.1016/0168-1656(95)00112-X

SODE, K., YOSHIDA, H., MATSUMURA, K., KIKUCHI, T., WATANABE, M., YASUTAKE, N., … SANO, H. (1995). ELUCIDATION OF THE REGION RESPONSIBLE FOR EDTA TOLERANCE IN PQQ GLUCOSE DEHYDROGENASES BY CONSTRUCTING ESCHERICHIA-COLI AND ACINETOBACTER-CALCOACETICUS CHIMERIC ENZYMES. Biochemical and Biophysical Research Communications, 211(1), 268–273. https://doi.org/10.1006/bbrc.1995.1806

Ohuchi, S., Narita, M., & Sode, K. (1995). Preference of a specific primary structure in the helix of proteins and its regiospecificity. Protein Engineering, 8(9), 48. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1995TL57300059&KeyUID=WOS:A1995TL57300059

MATSUNAGA, T., TAKEYAMA, H., MIURA, Y., YAMAZAKI, T., FURUYA, H., & SODE, K. (1995). SCREENING OF MARINE CYANOBACTERIA FOR HIGH PALMITOLEIC ACID PRODUCTION. Fems Microbiology Letters, 133(1-2), 137–141. https://doi.org/10.1111/j.1574-6968.1995.tb07874.x

WACHI, Y., SODE, K., HORIKOSHI, K., TAKEYAMA, H., & MATSUNAGA, T. (1995). SCREENING OF MELANIN BIOSYNTHESIS INHIBITORS FROM MARINE MICROALGAE USING STREPTOMYCES-BIKINIENSIS BIOASSAY. Biotechnology Techniques, 9(9), 633–636. https://doi.org/10.1007/BF00156347

Matsunaga, T., Takeyama, H., Miura, Y., Yamazaki, T., Furuya, h., & Sode, K. (1995). Screening of marine cyanobacteria for high palmitoleic acid production. FEMS Microbiology Letters, 133(1-2), 137–141. https://doi.org/10.1016/0378-1097(95)00350-E

SODE, K., WATANABE, K., ITO, S., MATSUMURA, K., & KIKUCHI, T. (1995). THERMOSTABLE CHIMERIC PQQ GLUCOSE-DEHYDROGENASE. Febs Letters, 364(3), 325–327. https://doi.org/10.1016/0014-5793(95)00418-9

SODE, K., KIKUCHI, T., WATANABE, M., NODA, K., & MATSUMURA, K. (1994). CONSTRUCTION AND CHARACTERIZATION OF CHIMERIC QUINOPROTEIN GLUCOSE-DEHYDROGENASE BETWEEN ESCHERICHIA-COLI AND ACINETOBACTER-CALCOACETICUS. Protein Engineering, 7(9), 1154. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1994PG50700021&KeyUID=WOS:A1994PG50700021

SODE, K., TSUGAWA, W., KUMAZAWA, S., & MATSUNAGA, T. (1994). ENZYME SENSOR FOR MEASUREMENT OF 1,5-ANHYDRO-D-GLUCITOL UTILIZING A NOVEL MARINE BACTERIAL GLUCOSE DEHYDROGENASE. In Advanced Materials '93, Ii - a & B (Vol. 15, pp. 445–447). Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1994BC69F00099&KeyUID=WOS:A1994BC69F00099

SODE, K., TATARA, M., HATANO, N., & MATSUNAGA, T. (1994). FOREIGN GENE-EXPRESSION IN MARINE CYANOBACTERIA UNDER PSEUDOCONTINUOUS CULTURE. Journal of Biotechnology, 33(3), 243–248. https://doi.org/10.1016/0168-1656(94)90072-8

SODE, K., & SANO, H. (1994). GLU742 SUBSTITUTION TO LYS ENHANCES THE EDTA TOLERANCE OF ESCHERICHIA-COLI PQQ GLUCOSE-DEHYDROGENASE. Biotechnology Letters, 16(5), 455–460. https://doi.org/10.1007/BF01023325

Sode, K., Witarto, A. B., Watanabe, K., Noda, K., Ito, S., & Tsugawa, W. (1994). Over expression of PQQ glucose dehydrogenase in Escherichia coli under holo enzyme forming condition. Biotechnology Letters, 16(12), 1265–1268. https://doi.org/10.1007/BF00149629

SODE, K., HATANO, N., & TATARA, M. (1994). PSEUDOCONTINUOUS CULTURE OF MARINE RECOMBINANT CYANOBACTERIA UNDER A LIGHT-DARK CYCLE. Biotechnology Letters, 16(9), 973–976. https://doi.org/10.1007/BF00128636

MATSUNAGA, T., SAKAGUCHI, T., SODE, K., KUDO, S., & NAKAMURA, N. (1994). SELECTIVE DETECTION OF MESSENGER-RNA BY OLIGO-DNA IMMOBILIZED BACTERIAL MAGNETITE. Advanced Materials '93, Ii - a & B, 15(A -B), 449–454. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1994BC69F00100&KeyUID=WOS:A1994BC69F00100

SODE, K., KUDO, S., SAKAGUCHI, T., NAKAMURA, N., & MATSUNAGA, T. (1993). APPLICATION OF BACTERIAL MAGNETIC PARTICLES FOR HIGHLY SELECTIVE MESSENGER-RNA RECOVERY-SYSTEM. Biotechnology Techniques, 7(9), 688–694. https://doi.org/10.1007/BF00151871

NAKAMURA, C., SAKAGUCHI, T., KUDO, S., BURGESS, J. G., SODE, K., & MATSUNAGA, T. (1993). CHARACTERIZATION OF IRON UPTAKE IN THE MAGNETIC BACTERIUM AQUASPIRILLUM SP AMB-1. Applied Biochemistry and Biotechnology, 39(1), 169–176. https://doi.org/10.1007/BF02918987

SODE, K., NAKASONO, S., TANAKA, M., & MATSUNAGA, T. (1993). CONSTRUCTION AND CHARACTERIZATION OF LOW-TEMPERATURE-OPERATING BIOSENSORS. Sensors and Actuators B-Chemical, 14(1-3), 663–664. https://doi.org/10.1016/0925-4005(93)85135-W

NAKAMURA, N., KUMAZAWA, S., SODE, K., & MATSUNAGA, T. (1993). DEVELOPMENT OF RAPID DETECTION SYSTEM FOR ALLERGIC REACTION USING RAT BASOPHILIC LEUKEMIA (RBL-1) CELLS. Sensors and Actuators B-Chemical, 13(1-3), 312–314. https://doi.org/10.1016/0925-4005(93)85389-R

Burgess, J. G., Iwamoto, K., Sode, K., & Matsunaga, T. (1993). Docosahexaenoic acid production by the unicellular alga Isochrysis galbana using a photobioreactor. Japanese Journal of Phycology, 41(4), 414. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=BCI&KeyUT=BCI:BCI199497157951&KeyUID=BCI:BCI199497157951

BURGESS, J. G., SUDO, H., SODE, K., & MATSUNAGA, T. (1993). EFFICIENT GENE-TRANSFER OF HIGH COPY NUMBER MOBILIZABLE PLASMIDS CONTAINING A MARINE RHODOBACTER ORIGIN OF REPLICATION. Current Microbiology, 26(2), 105–108. https://doi.org/10.1007/BF01577344

Miura, Y., Sode, K., Narasaki, Y., & Matsunaga, T. (1993). Light-induced antimicrobial activity of extracts from marine  . Journal of Marine Biotechnology, 1(3), 143–146. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=CABI&KeyUT=CABI:19941301477&KeyUID=CABI:19941301477

MIURA, Y., SODE, K., NAKAMURA, N., MATSUNAGA, N., & MATSUNAGA, T. (1993). PRODUCTION OF GAMMA-LINOLENIC ACID FROM THE MARINE GREEN-ALGA CHLORELLA SP NKG-042401. Fems Microbiology Letters, 107(2-3), 163–167. https://doi.org/10.1111/j.1574-6968.1993.tb06024.x

SODE, K., NAKASONO, S., TANAKA, M., & MATSUNAGA, T. (1993). SUBZERO TEMPERATURE OPERATING BIOSENSOR UTILIZING AN ORGANIC-SOLVENT AND QUINOPROTEIN GLUCOSE-DEHYDROGENASE. Biotechnology and Bioengineering, 42(2), 251–254. https://doi.org/10.1002/bit.260420214

LEE, S., SODE, K., NAKANISHI, K., MARTY, J. L., TAMIYA, E., & KARUBE, I. (1992). A NOVEL MICROBIAL SENSOR USING LUMINOUS BACTERIA. Biosensors & Bioelectronics, 7(4), 273–277. https://doi.org/10.1016/0956-5663(92)87005-A

MARTY, J. L., SODE, K., & KARUBE, I. (1992). BIOSENSOR FOR DETECTION OF ORGANOPHOSPHATE AND CARBAMATE INSECTICIDES. Electroanalysis, 4(2), 249–252. https://doi.org/10.1002/elan.1140040217

TAKANO, H., TAKEYAMA, H., NAKAMURA, N., SODE, K., BURGESS, J. G., MANABE, E., … MATSUNAGA, T. (1992). CO2 REMOVAL BY HIGH-DENSITY CULTURE OF A MARINE CYANOBACTERIUM SYNECHOCOCCUS SP USING AN IMPROVED PHOTOBIOREACTOR EMPLOYING LIGHT-DIFFUSING OPTICAL FIBERS. Applied Biochemistry and Biotechnology, 34-5(1), 449–458. https://doi.org/10.1007/BF02920568

Sode, K., Tatara, M., Takeyama, H., Burgess, J. G., & Matsunaga, T. (1992). Conjugative gene transfer in marine cyanobacteria: Synechococcus sp., Synechocystis sp. and Pseudanabaena sp. Applied Microbiology and Biotechnology, 37(3), 369–373. https://doi.org/10.1007/BF00210994

MATSUNAGA, T., NAKASONO, S., TAKAMUKU, T., BURGESS, J. G., NAKAMURA, N., & SODE, K. (1992). DISINFECTION OF DRINKING-WATER BY USING A NOVEL ELECTROCHEMICAL REACTOR EMPLOYING CARBON-CLOTH ELECTRODES. Applied and Environmental Microbiology, 58(2), 686–689. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1992HC49400037&KeyUID=WOS:A1992HC49400037

NAKASONO, S., NAKAMURA, N., SODE, K., & MATSUNAGA, T. (1992). ELECTROCHEMICAL DISINFECTION OF MARINE-BACTERIA ATTACHED ON A PLASTIC ELECTRODE. Bioelectrochemistry and Bioenergetics, 27(2), 191–198. https://doi.org/10.1016/0302-4598(92)87042-S

Nakasono, S., Nakamura, N., Sode, K., & Matsunaga, T. (1992). Electrochemical disinfection of marine bacteria attached on a plastic electrode. Journal of Electroanalytical Chemistry, 342(2), 191–198. https://doi.org/10.1016/0022-0728(92)85049-9

Matsunaga, T., Nakamura, C., Burgess, J. G., & Sode, K. (1992). Gene transfer in magnetic bacteria: Transposon mutagenesis and cloning of genomic DNA fragments required for magnetosome synthesis. Journal of Bacteriology, 174(9), 2748–2753. https://doi.org/10.1128/jb.174.9.2748-2753.1992

MANABE, E., HIRANO, M., TAKANO, H., ISHIKAWADOI, N., SODE, K., & MATSUNAGA, T. (1992). INFLUENCE OF AMMONIUM-CHLORIDE ON GROWTH AND FATTY-ACID PRODUCTION BY SPIRULINA-PLATENSIS. Applied Biochemistry and Biotechnology, 34-5(1), 273–281. https://doi.org/10.1007/BF02920551

SODE, K., TATARA, M., OGAWA, S., & MATSUNAGA, T. (1992). MAINTENANCE OF BROAD HOST RANGE VECTOR PKT230 IN MARINE UNICELLULAR CYANOBACTERIA. Fems Microbiology Letters, 99(1), 73–78. https://doi.org/10.1111/j.1574-6968.1992.tb05544.x

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NAVERA, E. N., SODE, K., TAMIYA, E., & KARUBE, I. (1991). DEVELOPMENT OF ACETYLCHOLINE SENSOR USING CARBON-FIBER (AMPEROMETRIC DETERMINATION). Biosensors & Bioelectronics, 6(8), 675–680. https://doi.org/10.1016/0956-5663(91)87021-3

MATSUNAGA, T., TAKEYAMA, H., SUDO, H., OYAMA, N., ARIURA, S., TAKANO, H., … NAKAMURA, N. (1991). GLUTAMATE PRODUCTION FROM CO2 BY MARINE CYANOBACTERIUM SYNECHOCOCCUS SP USING A NOVEL BIOSOLAR REACTOR EMPLOYING LIGHT-DIFFUSING OPTICAL FIBERS. Applied Biochemistry and Biotechnology, 28-9(1), 157–167. https://doi.org/10.1007/BF02922597

SODE, K., HORIKOSHI, K., TAKEYAMA, H., NAKAMURA, N., & MATSUNAGA, T. (1991). ONLINE MONITORING OF MARINE CYANOBACTERIAL CULTIVATION BASED ON PHYCOCYANIN FLUORESCENCE. Journal of Biotechnology, 21(3), 209–217. https://doi.org/10.1016/0168-1656(91)90042-T

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ENDO, H., SUZUKI, M., SODE, K., TAMIYA, E., & KARUBE, I. (1991). RAPID-DETERMINATION OF PLASMID-CARRYING YEAST-CELLS BY USING AN IMAGING SENSOR SYSTEM. Biotechnology and Bioengineering, 38(11), 1331–1336. https://doi.org/10.1002/bit.260381111

TAKEYAMA, H., BURGESS, J. G., SUDO, H., SODE, K., & MATSUNAGA, T. (1991). SALINITY-DEPENDENT COPY NUMBER INCREASE OF A MARINE CYANOBACTERIAL ENDOGENOUS PLASMID. Fems Microbiology Letters, 90(1), 95–98. https://doi.org/10.1111/j.1574-6968.1991.tb05132.x

Takeyama, H., Grant Burgess, J., Sudo, H., Sode, K., & Matsunaga, T. (1991). Salinity-dependent copy number increase of a marine cyanobacterial endogenous plasmid. FEMS Microbiology Letters, 90(1), 95–98. https://doi.org/10.1016/0378-1097(91)90653-R

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NISHII, K., SODE, K., & KARUBE, I. (1990). AIR-BUBBLING, HOLLOW-FIBER REACTOR WITH CELL BLEEDING AND CROSS-FLOW FILTRATION. Biotechnology and Bioengineering, 35(11), 1155–1160. https://doi.org/10.1002/bit.260351112

MARTY, J. L., SODE, K., & KARUBE, I. (1990). AMPEROMETRIC DETERMINATION OF CHOLINE AND ACETYLCHOLINE WITH ENZYMES IMMOBILIZED IN A PHOTOCROSS-LINKABLE POLYMER. Analytica Chimica Acta, 228(1), 49–53. https://doi.org/10.1016/S0003-2670(00)80477-8

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FUKUOKA, S., KAMISHIMA, H., SODE, K., & KARUBE, I. (1990). FACILE ISOLATION OF ENDO-PECTATE LYASE FROM ERWINIA-CAROTOVORA BASED ON ELECTROSTATIC INTERACTION. Applied Biochemistry and Biotechnology, 26(3), 239–248. https://doi.org/10.1007/BF02921505

YAMAMOTO, T., TOMIYAMA, M., MITA, H., SODE, K., & KARUBE, I. (1990). IDENTIFICATION OF PROTEINS ENCODED IN ESCHERICHIA-COLI HYDA, HYDB AND ANALYSIS OF THE HYDA LOCUS. Fems Microbiology Letters, 66(1-3), 187–192. https://doi.org/10.1111/j.1574-6968.1990.tb03994.x

Yamamoto, T., Tomiyama, M., Mita, H., Sode, K., & Karube, I. (1990). Identification of proteins encoded in Escherichia coli hydA, hydB and analysis of the hydA locus. FEMS Microbiology Letters, 66(1-3), 187–192. https://doi.org/10.1016/0378-1097(90)90280-4

KARUBE, I., SODE, K., & TAMIYA, E. (1990). MICROBIOSENSORS. Journal of Biotechnology, 15(3), 267–281. https://doi.org/10.1016/0168-1656(90)90032-7

ENDO, H., SODE, K., KARUBE, I., & MURAMATSU, H. (1990). ONLINE MONITORING OF THE VISCOSITY IN DEXTRAN FERMENTATION USING PIEZOELECTRIC QUARTZ CRYSTAL. Biotechnology and Bioengineering, 36(6), 636–641. https://doi.org/10.1002/bit.260360612

Sode, K., Sugiyama, T., Yamamoto, T., Tomiyama, M., & Karube, I. (1990). Restoration of escherichia coli hyd b mutant hydrogenase by cultivation in media containing various metals. Biocatalysis and Biotransformation, 4(2-3), 211–217. https://doi.org/10.3109/10242429008992092

Nishii, K., Sode, K., & Karube, I. (1990). Sequential two-step conversion of 4-oxoisophorone to 4-hydroxy-2,2,6-trimethylcyclohexanone by thermophilic bacteria. Applied Microbiology and Biotechnology, 33(3), 245–250. https://doi.org/10.1007/BF00164515

SODE, K., TAMIYA, E., KARUBE, I., & KAMEDA, Y. (1989). AMPEROMETRIC DETERMINATION OF FREE FATTY-ACIDS BY UTILIZING 5 SEQUENTIAL ENZYME-REACTIONS. Electroanalysis, 1(1), 69–74. https://doi.org/10.1002/elan.1140010111

I, K. A. R. U. B. E., K, H. I. R. A. M. O. T. O., M, K. A. W. A. R. A. I., & K, S. O. D. E. (1989). BIOSENSOR FOR TOXIC COMPOUNDS USING IMMOBILIZED ANIMAL CELL MEMBRANE. Membrane, 14(5), 311–318. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=BCI&KeyUT=BCI:BCI199089044064&KeyUID=BCI:BCI199089044064

Karube, I., Hiramoto, K., Kawarai, M., & Sode, K. (1989). Biosensor for toxic compounds using immobilized animal cell membrane. Membrane, 14(5), 311–318. https://doi.org/10.5360/membrane.14.311

ENDO, H., SODE, K., OGURA, K., OHYA, K., & KARUBE, I. (1989). DETERMINATION OF MICROBIAL CONCENTRATION WITH A PIEZOELECTRIC GUM SENSOR. Journal of Biotechnology, 12(3-4), 307–316. https://doi.org/10.1016/0168-1656(89)90050-3

FUKUOKA, S., KAMISHIMA, H., SODE, K., & KARUBE, I. (1989). EXTRACELLULAR LIPOPOLYSACCHARIDE PRODUCTION BY ERWINIA-CAROTOVORA. Journal of Fermentation and Bioengineering, 68(5), 320–324. https://doi.org/10.1016/0922-338X(89)90005-6

YOKOYAMA, K., SODE, K., TAMIYA, E., & KARUBE, I. (1989). INTEGRATED BIOSENSOR FOR GLUCOSE AND GALACTOSE. Analytica Chimica Acta, 218(1), 137–142. https://doi.org/10.1016/S0003-2670(00)80291-3

SODE, K., KARUBE, I., ARAKI, R., & MIKAMI, Y. (1989). MICROBIAL CONVERSION OF BETA-IONONE BY IMMOBILIZED ASPERGILLUS-NIGER IN THE PRESENCE OF AN ORGANIC-SOLVENT. Biotechnology and Bioengineering, 33(9), 1191–1195. https://doi.org/10.1002/bit.260330915

NISHII, K., SODE, K., & KARUBE, I. (1989). MICROBIAL CONVERSION OF DIHYDROOXOISOPHORONE (DOIP) TO 4-HYDROXY-2,2,6-TRIMETHYLCYCLOHEXANONE (4-HTMCH) BY THERMOPHILIC BACTERIA. Journal of Biotechnology, 9(2), 117–128. https://doi.org/10.1016/0168-1656(89)90081-3

KARUBE, I., SODE, K., SUZUKI, M., & NAKAHARA, T. (1989). MICROBIAL SENSOR FOR PRELIMINARY SCREENING OF MUTAGENS UTILIZING A PHAGE INDUCTION TEST. Analytical Chemistry, 61(21), 2388–2391. https://doi.org/10.1021/ac00196a013

Karube, I., Sode, K., Tamiya, E., & Yokoyama, K. (1989). Microbial bod sensor utilizing thermophilic bacteria. Analytical Letters, 22(4), 791–801. https://doi.org/10.1080/00032718908051367

SODE, K., TAMIYA, E., KARUBE, I., & KAMEDA, Y. (1989). SENSOR FOR FREE FATTY-ACIDS BASED ON ACYL COENZYME-A SYNTHETASE AND ACYL COENZYME-A OXIDASE. Analytica Chimica Acta, 220(1), 251–255. https://doi.org/10.1016/S0003-2670(00)80268-8

KARUBE, I., TAMIYA, E., SODE, K., YOKOYAMA, K., KITAGAWA, Y., SUZUKI, H., & ASANO, Y. (1988). APPLICATION OF MICROBIOLOGICAL SENSORS IN FERMENTATION PROCESSES. Analytica Chimica Acta, 213(1-2), 69–77. https://doi.org/10.1016/S0003-2670(00)81341-0

KANAYAMA, H., SODE, K., & KARUBE, I. (1988). CONTINUOUS HYDROGEN EVOLUTION BY IMMOBILIZED RECOMBINANT ESCHERICHIA-COLI USING A BIOREACTOR. Biotechnology and Bioengineering, 32(3), 396–399. https://doi.org/10.1002/bit.260320321

SODE, K., MORITA, T., PETERHANS, A., MEUSSDOERFFER, F., MOSBACH, K., & KARUBE, I. (1988). CONTINUOUS PRODUCTION OF ALPHA-PEPTIDE USING IMMOBILIZED RECOMBINANT YEAST-CELLS - A MODEL FOR CONTINUOUS PRODUCTION OF FOREIGN PEPTIDE BY RECOMBINANT YEAST. Journal of Biotechnology, 8(2), 113–122. https://doi.org/10.1016/0168-1656(88)90073-9

SODE, K., BRODELIUS, P., MEUSSDOERFFER, F., MOSBACH, K., & ERNST, J. F. (1988). CONTINUOUS PRODUCTION OF SOMATOMEDIN-C WITH IMMOBILIZED TRANSFORMED YEAST-CELLS. Applied Microbiology and Biotechnology, 28(3), 215–221. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1988N050900001&KeyUID=WOS:A1988N050900001

GREBER, U. F., SODE, K., & MEUSSDOERFFER, F. (1988). EFFECT OF THE GLUCOSIDASE INHIBITOR 1-DEOXYNOJIRIMYCIN ON PROTEIN SECRETION FROM SACCHAROMYCES-CEREVISIAE. Enzyme and Microbial Technology, 10(4), 246–251. https://doi.org/10.1016/0141-0229(88)90074-9

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KANAYAMA, H., SODE, K., & KARUBE, I. (1987). BASIC STUDIES OF HYDROGEN EVOLUTION BY ESCHERICHIA-COLI CONTAINING A CLONED CITROBACTER-FREUNDII HYDROGENASE GENE. Applied Biochemistry and Biotechnology, 15(2), 97–106. https://doi.org/10.1007/BF02801311

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