@misc{conkling_song_mendu_2010, title={Tobacco products with increased nicotine}, volume={7,645,925}, number={2010 Jan. 12}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={2010} }
 @misc{conkling_song_mendu_2009, title={Regulation of quinolate phosphoribosyl transferase expression}, volume={7,605,308}, number={1999 Oct. 20}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={2009} }
 @misc{conkling_song_mendu_2008, title={Methods and compositions for protein production in tobacco plants with reduced nicotine}, volume={7,425,670}, number={2008 Sep. 16}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={2008} }
 @misc{conkling_li_2007, title={Plant promoter sequence}, volume={7,192,771}, number={2007 Mar. 20}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. and Li, Y.}, year={2007} }
 @misc{conkling_li_2007, title={Putrescine-n-methyltransferase promoter}, volume={7,189,570}, number={2007 Mar. 13}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. and Li, Y.}, year={2007} }
 @misc{conkling_song_mendu_2007, title={Regulation of quinolate phosphoribosyl transferase expression}, volume={7,304,220}, number={2007 Dec. 4}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={2007} }
 @misc{conkling_2005, title={Modifying nicotine and nitrosamine levels in tobacco}, volume={6,907,887}, number={2005 Jun. 21}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A.}, year={2005} }
 @misc{conkling_li_2005, title={Promoter fragment that is recognized by the product of the tobacco Nic gene}, volume={6,911,541}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Li, Y.}, year={2005} }
 @article{xie_wehner_wollenberg_purugganan_conkling_2003, title={Intron and polypeptide evolution of conserved NPA to NPA motif regions in plant aquaporins}, volume={128}, number={4}, journal={Journal of the American Society for Horticultural Science}, author={Xie, J. H. and Wehner, T. C. and Wollenberg, K. and Purugganan, M. D. and Conkling, M. A.}, year={2003}, pages={591–597} }
 @misc{conkling_song_mendu_2003, title={Regulation of quinolate phosphoribosyl transferase expression}, volume={7,408,098}, number={2003 Dec 30}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={2003} }
 @misc{conkling_song_mendu_2003, title={Regulation of quinolate phosphoribosyl transferase expression by transformation with a tobacco quinolate phosphoribosyl transferase nucleic acid}, volume={6,586,661}, number={2003 July 1}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={2003} }
 @article{xie_wehner_conkling_2002, title={PCR-based single-strand conformation polymorphism (SSCP) analysis to clone nine aquaporin genes in cucumber}, volume={127}, number={6}, journal={Journal of the American Society for Horticultural Science}, author={Xie, J. H. and Wehner, T. C. and Conkling, M. A.}, year={2002}, pages={925–930} }
 @misc{conkling_opperman_acedo_song_1999, title={Nematode-resistant transgenic plants}, volume={6,008,436}, number={1999 Dec. 28}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Opperman, C. H. and Acedo, G. N. and Song, W.}, year={1999} }
 @article{pharr_prata_jennings_williamson_zamski_yamamoto_conkling_1999, title={Regulation of mannitol dehydrogenase: Relationship to plant growth and stress tolerance}, volume={34}, number={6}, journal={HortScience}, author={Pharr, D. M. and Prata, R. T. N. and Jennings, D. B. and Williamson, J. D. and Zamski, E. and Yamamoto, Y. T. and Conkling, M. A.}, year={1999}, pages={1027–1032} }
 @misc{conkling_song_mendu_1999, title={Regulation of quinolate phosphoribosyl transferase expression}, volume={6,423,520}, number={1999 Oct 29}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Song, W. and Mendu, N.}, year={1999} }
 @article{fitzmaurice_nguyen_wernsman_thompson_conkling_1999, title={Transposon tagging of the sulfur gene of tobacco using engineered maize Ac/Ds elements}, volume={153}, number={4}, journal={Genetics}, author={Fitzmaurice, W. P. and Nguyen, L. V. and Wernsman, E. A. and Thompson, W. F. and Conkling, M. A.}, year={1999}, pages={1919–1928} }
 @misc{klaenhammer_conkling_o'sullivan_djordjevic_walker_taylor_1998, title={Bacteriophage-triggered cell suicide systems and fermentation methods employing the same}, volume={5,792,625}, number={1998 Aug. 11}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Klaenhammer, T. R. and Conkling, M. A. and O'Sullivan, D. and Djordjevic, G. and Walker, S. A. and Taylor, C. G.}, year={1998} }
 @inbook{opperman_conkling_1998, title={Bioengineering resistance to plant-parasitic nematodes}, booktitle={Plant and nematode interactions / co-eds Kenneth R. Barker, Gary A. Pederson, Gary L. Windham. Madison, Wis.: American Society of Agronomy, Inc.: Crop Science Society of America, Inc.: Soil Science Society of  America, Inc.,  1998.}, publisher={Madison, Wis.: American Society of Agronomy, Inc.: Crop Science Society of America, Inc.: Soil Science Society of  America, Inc.}, author={Opperman, C.H. and Conkling, M.A.}, year={1998}, pages={239–250} }
 @article{stoop_williamson_conkling_mackay_pharr_1998, title={Characterization of NAD-dependent mannitol dehydrogenase from celery as affected by ions, chelators, reducing agents and metabolites}, volume={131}, ISSN={["0168-9452"]}, DOI={10.1016/S0168-9452(97)00243-4}, abstractNote={NAD-dependent mannitol dehydrogenase (MTD) from celery (Apium graveolens L. var. dulce (Mill.) Pers.) provides the initial step by which mannitol is committed to central metabolism and plays a critical role in regulating mannitol concentration in the plant. The pH optimum for mannitol oxidation occurs at pH 9.5 whereas the optimum for mannose reduction occurs at pH 6.5. Michaelis–Menten kinetics were exhibited for mannitol and NAD with Km values of 64 and 0.14 mM, respectively at pH 9.5. The Km for mannose and NADH were 745 mM and 1.27 μM, respectively at pH 6.5. The high Km for mannose is consistent with a reaction in situ favoring mannitol oxidation rather than mannose reduction. The observed down-regulation of MTD in salt stressed celery is not due to a direct inhibition by NaCl or macronutrients. Inhibition by the chelator 1,10-phenanthroline suggests that zinc is required for MTD activity. Reducing agents DTT, DTE and β-mercaptoethanol inactivated MTD reversibly. At pH 7.0, ADP and to a lesser extend AMP and ATP were competitive inhibitors, with respect to NAD, having apparent Ki’s of 0.24, 0.64 and 1.10 mM, respectively.}, number={1}, journal={PLANT SCIENCE}, author={Stoop, JMH and Williamson, JD and Conkling, MA and MacKay, JJ and Pharr, DM}, year={1998}, month={Jan}, pages={43–51} }
 @article{kjemtrup_sampson_peele_nguyen_conkling_thompson_robertson_1998, title={Gene silencing from plant DNA carried by a Geminivirus}, volume={14}, ISSN={["0960-7412"]}, DOI={10.1046/j.1365-313X.1998.00101.x}, abstractNote={SummaryThe geminivirus tomato golden mosaic virus (TGMV) replicates in nuclei and expresses genes from high copy number DNA episomes. The authors used TGMV as a vector to determine whether episomal DNA can cause silencing of homologous, chromosomal genes. Two markers were used to asses silencing: (1) the sulfur allele (su) of magnesium chelatase, an enzyme required for chlorophyll formation; and (2) the firefly luciferase gene (luc). Various portions of both marker genes were inserted into TGMV in place of the coat protein open‐reading frame and the constructs were introduced into intact plants using particle bombardment. When TGMV vectors carrying fragments of su (TGMV::su) were introduced into leaves of wild type Nicotiana benthamiana, circular, yellow spots with an area of several hundred cells formed after 3‐5 days. Systemic movement of TGMV::su subsequently produced varigated leaf and stem tissue. Fragments that caused silencing included a 786 bp 5' fragment of the 1392 bp su cDNA in sense and anti‐sense orientation, and a 403 bp 3' fragment. TGMV::su‐induced silencing was propogated through tissue culture, along with the viral episome, but was not retained through meiosis. Systemic downregulation of a constitutively expresse luciferase transgene in plants was achieved following infection with TGMV vectors carrying a 623 bp portion of luc in sense or anti‐sense orientation. These results establish that homologous DNA sequences localized in nuclear episomes can modulate the expression of active chromosomal genes.}, number={1}, journal={PLANT JOURNAL}, author={Kjemtrup, S and Sampson, KS and Peele, CG and Nguyen, LV and Conkling, MA and Thompson, WF and Robertson, D}, year={1998}, month={Apr}, pages={91–100} }
 @misc{conkling_opperman_taylor_1998, title={Pathogen-resistant transgenic plants}, volume={5,750,386}, number={1998 May 12}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Opperman, C. H. and Taylor, C. G.}, year={1998} }
 @misc{conkling_mendu_song_1998, title={Root cortex specific gene promoter}, volume={5,837,876}, number={1998 Nov. 17}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Mendu, N. and Song, W.}, year={1998} }
 @article{djordjevic_osullivan_walker_conkling_klaenhammer_1997, title={A triggered-suicide system designed as a defense against bacteriophages}, volume={179}, ISSN={["0021-9193"]}, DOI={10.1128/jb.179.21.6741-6748.1997}, abstractNote={A novel bacteriophage protection system for Lactococcus lactis based on a genetic trap, in which a strictly phage-inducible promoter isolated from the lytic phage phi31 is used to activate a bacterial suicide system after infection, was developed. The lethal gene of the suicide system consists of the three-gene restriction cassette LlaIR+, which is lethal across a wide range of gram-positive bacteria. The phage-inducible trigger promoter (phi31P) and the LlaIR+ restriction cassette were cloned in Escherichia coli on a high-copy-number replicon to generate pTRK414H. Restriction activity was not apparent in E. coli or L. lactis prior to phage infection. In phage challenges of L. lactis(pTRK414H) with phi31, the efficiency of plaquing was lowered to 10(-4) and accompanied by a fourfold reduction in burst size. Center-of-infection assays revealed that only 15% of infected cells released progeny phage. In addition to phage phi31, the phi31P/LlaIR+ suicide cassette also inhibited four phi31-derived recombinant phages at levels at least 10-fold greater than that of phi31. The phi31P/LlaIR+-based suicide system is a genetically engineered form of abortive infection that traps and eliminates phages potentially evolving in fermentation environments by destroying the phage genome and killing the propagation host. This type of phage-triggered suicide system could be designed for any bacterium-phage combination, given a universal lethal gene and an inducible promoter which is triggered by the infecting bacteriophage.}, number={21}, journal={JOURNAL OF BACTERIOLOGY}, author={Djordjevic, GM and OSullivan, DJ and Walker, SA and Conkling, MA and Klaenhammer, TR}, year={1997}, month={Nov}, pages={6741–6748} }
 @article{yamamoto_zamski_williamson_conkling_pharr_1997, title={Subcellular localization of celery mannitol dehydrogenase - A cytosolic metabolic enzyme in nuclei}, volume={115}, ISSN={["0032-0889"]}, DOI={10.1104/pp.115.4.1397}, abstractNote={Abstract
               Mannitol dehydrogenase (MTD) is the first enzyme in mannitol catabolism in celery (Apium graveolens L. var dulce [Mill] Pers. Cv Florida 638). Mannitol is an important photoassimilate, as well as providing plants with resistance to salt and osmotic stress. Previous work has shown that expression of the celery Mtd gene is regulated by many factors, such as hexose sugars, salt and osmotic stress, and salicylic acid. Furthermore, MTD is present in cells of sink organs, phloem cells, and mannitol-grown suspension cultures. Immunogold localization and biochemical analyses presented here demonstrate that celery MTD is localized in the cytosol and nuclei. Although the cellular density of MTD varies among different cell types, densities of nuclear and cytosolic MTD in a given cell are approximately equal. Biochemical analyses of nuclear extracts from mannitol-grown cultured cells confirmed that the nuclear-localized MTD is enzymatically active. The function(s) of nuclear-localized MTD is unknown.}, number={4}, journal={PLANT PHYSIOLOGY}, author={Yamamoto, YT and Zamski, E and Williamson, JD and Conkling, MA and Pharr, DM}, year={1997}, month={Dec}, pages={1397–1403} }
 @article{prata_williamson_conkling_pharr_1997, title={Sugar repression of mannitol dehydrogenase activity in celery cells}, volume={114}, ISSN={["0032-0889"]}, DOI={10.1104/pp.114.1.307}, abstractNote={Abstract
               We present evidence that the activity of the mannitol-catabolizing enzyme mannitol dehydrogenase (MTD) is repressed by sugars in cultured celery (Apium graveolens L.) cells. Furthermore, this sugar repression appears to be mediated by hexokinases (HKs) in a manner comparable to the reported sugar repression of photosynthetic genes. Glucose (Glc)-grown cell cultures expressed little MTD activity during active growth, but underwent a marked increase in MTD activity, protein, and RNA upon Glc starvation. Replenishment of Glc in the medium resulted in decreased MTD activity, protein, and RNA within 12 h. Addition of mannoheptulose, a competitive inhibitor of HK, derepressed MTD activity in Glc-grown cultures. In contrast, the addition of the sugar analog 2-deoxyglucose, which is phosphorylated by HK but not further metabolized, repressed MTD activity in mannitol-grown cultures. Collectively, these data suggest that HK and sugar phosphorylation are involved in signaling MTD repression. In vivo repression of MTD activity by galactose (Gal), which is not a substrate of HK, appeared to be an exception to this hypothesis. Further analyses, however, showed that the products of Gal catabolism, Glc and fructose, rather than Gal itself, were correlated with MTD repression.}, number={1}, journal={PLANT PHYSIOLOGY}, author={Prata, RTN and Williamson, JD and Conkling, MA and Pharr, DM}, year={1997}, month={May}, pages={307–314} }
 @article{zamski_yamamoto_williamson_conkling_pharr_1996, title={Immunolocalization of mannitol dehydrogenase in celery plants and cells}, volume={112}, ISSN={["0032-0889"]}, DOI={10.1104/pp.112.3.931}, abstractNote={Abstract
               Immunolocalization of mannitol dehydrogenase (MTD) in celery (Apium graveolens L.) suspension cells and plants showed that MTD is a cytoplasmic enzyme. MTD was found in the meristems of celery root apices, in young expanding leaves, in the vascular cambium, and in the phloem, including sieve-element/companion cell complexes, parenchyma, and in the exuding phloem sap of cut petioles. Suspension cells that were grown in medium with mannitol as the sole carbon source showed a high anti-MTD cross-reaction in the cytoplasm, whereas cells that were grown in sucrose-containing medium showed little or no cross-reaction. Gel-blot analysis of proteins from vascular and nonvascular tissues of mature celery petioles showed a strong anti-MTD sera cross-reactive band, corresponding to the 40-kD molecular mass of MTD in vascular extracts, but no cross-reactive bands in nonvascular extracts. The distribution pattern of MTD within celery plants and in cell cultures that were grown on different carbon sources is consistent w ith the hypothesis that the Mtd gene may be regulated by sugar repression. Additionally, a developmental component may regulate the distribution of MTD within celery plants.}, number={3}, journal={PLANT PHYSIOLOGY}, author={Zamski, E and Yamamoto, YT and Williamson, JD and Conkling, MA and Pharr, DM}, year={1996}, month={Nov}, pages={931–938} }
 @inbook{pharr_stoop_studer feusi_williamson_massel_conkling_1995, title={Mannitol catabolism in plant sink tissues}, booktitle={Carbon Partitioning and Source-Sink Interactions in Plants, Current Topics in Plant Physiology, Vol. 13 (Madore, MA and Lucas, WJ, eds.)}, publisher={American Society of Plant Physiologists, Rockville, MD}, author={Pharr, D.M. and Stoop, J.M.H. and Studer Feusi, M.E. and Williamson, J.D. and Massel, M.O. and Conkling, M.A.}, editor={Madore, MA and Lucas, WJEditors}, year={1995}, pages={180–194} }
 @article{stoop_willamson_conkling_pharr_1995, title={PURIFICATION OF NAD-DEPENDENT MANNITOL DEHYDROGENASE FROM CELERY SUSPENSION-CULTURES}, volume={108}, ISSN={["0032-0889"]}, DOI={10.1104/pp.108.3.1219}, abstractNote={Mannitol dehydrogenase, a mannitol:mannose 1-oxidoreductase, constitutes the first enzymatic step in the catabolism of mannitol in nonphotosynthetic tissues of celery (Apium graveolens L.). Endogenous regulation of the enzyme activity in response to environmental cues is critical in modulating tissue concentration of mannitol, which, importantly, contributes to stress tolerance of celery. The enzyme was purified to homogeneity from celery suspension cultures grown on D-mannitol as the carbon source. Mannitol dehydrogenase was purified 589-fold to a specific activity of 365 [mu]mol h-1 mg-1 protein with a 37% yield of enzyme activity present in the crude extract. A highly efficient and simple purification protocol was developed involving polyethylene glycol fractionation, diethylaminoethyl-anion-exchange chromatography, and NAD-agarose affinity chromatography using NAD gradient elution. Sodium dodecyl sulfate gel electrophoresis of the final preparation revealed a single 40-kD protein. The molecular mass of the native protein was determined to be approximately 43 kD, indicating that the enzyme is a monomer. Polyclonal antibodies raised against the enzyme inhibited enzymatic activity of purified mannitol dehydrogenase. Immunoblots of crude protein extracts from mannitol-grown celery cells and sink tissues of celery, celeriac, and parsley subjected to sodium dodecyl sulfate gel electrophoresis showed a single major immunoreactive 40-kD protein.}, number={3}, journal={PLANT PHYSIOLOGY}, author={STOOP, JMH and WILLAMSON, JD and CONKLING, MA and PHARR, DM}, year={1995}, month={Jul}, pages={1219–1225} }
 @misc{conkling_yamamoto_1995, title={Root specific gene promoter}, volume={5,459,252}, number={1995 Oct. 17}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Yamamoto, Y. T.}, year={1995} }
 @article{williamson_stoop_massel_conkling_pharr_1995, title={SEQUENCE-ANALYSIS OF A MANNITOL DEHYDROGENASE CDNA FROM PLANTS REVEALS A FUNCTION FOR THE PATHOGENESIS-RELATED PROTEIN ELI3}, volume={92}, ISSN={["0027-8424"]}, DOI={10.1073/pnas.92.16.7148}, abstractNote={Mannitol is the most abundant sugar alcohol in nature, occurring in bacteria, fungi, lichens, and many species of vascular plants. Celery (Apium graveolens L.), a plant that forms mannitol photosynthetically, has high photosynthetic rates thought to results from intrinsic differences in the biosynthesis of hexitols vs. sugars. Celery also exhibits high salt tolerance due to the function of mannitol as an osmoprotectant. A mannitol catabolic enzyme that oxidizes mannitol to mannose (mannitol dehydrogenase, MTD) has been identified. In celery plants, MTD activity and tissue mannitol concentration are inversely related. MTD provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level. We have now isolated, sequenced, and characterized a Mtd cDNA from celery. Analyses showed that Mtd RNA was more abundant in cells grown on mannitol and less abundant in salt-stressed cells. A protein database search revealed that the previously described ELI3 pathogenesis-related proteins from parsley and Arabidopsis are MTDs. Treatment of celery cells with salicylic acid resulted in increased MTD activity and RNA. Increased MTD activity results in an increased ability to utilize mannitol. Among other effects, this may provide an additional source of carbon and energy for response to pathogen attack. These responses of the primary enzyme controlling mannitol pool size reflect the importance of mannitol metabolism in plant responses to divergent types of environmental stress.}, number={16}, journal={PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA}, author={WILLIAMSON, JD and STOOP, JMH and MASSEL, MO and CONKLING, MA and PHARR, DM}, year={1995}, month={Aug}, pages={7148–7152} }
 @article{pharr_stoop_williamson_feusi_massel_conkling_1995, title={The dual role of mannitol as osmoprotectant and photoassimilate in celery}, volume={30}, number={6}, journal={HortScience}, author={Pharr, D. M. and Stoop, J. M. H. and Williamson, J. D. and Feusi, M. E. S. and Massel, M. O. and Conkling, M. A.}, year={1995}, pages={1182–1188} }