Robert Rose

Enriquez, P., Krajewski, K., Strahl, B. D., Rothbart, S. B., Dowen, R. H., & Rose, R. B. (2021). Binding specificity and function of the SWI/SNF subunit SMARCA4 bromodomain interaction with acetylated histone. JOURNAL OF BIOLOGICAL CHEMISTRY, 297(4). https://doi.org/10.1016/j.jbc.2021.101145

Buhrman, G., Enriquez, P., Dillard, L., Baer, H., Truong, V., Grunden, A. M., & Rose, R. B. (2021). Structure, Function, and Thermal Adaptation of the Biotin Carboxylase Domain Dimer from Hydrogenobacter thermophilus 2-Oxoglutarate Carboxylase. BIOCHEMISTRY, 60(4), 324–345. https://doi.org/10.1021/acs.biochem.0c00815

Khund-Sayeed, S., He, X., Holzberg, T., Wang, J., Rajagopal, D., Upadhyay, S., … Vinson, C. (2016). 5-Hydroxymethylcytosine in E-box motifs ACAT|GTG and ACAC|GTG increases DNA-binding of the B-HLH transcription factor TCF4. INTEGRATIVE BIOLOGY, 8(9), 936–945. https://doi.org/10.1039/c6ib00079g

Somalinga, V., Buhrman, G., Arun, A., Rose, R. B., & Grunden, A. M. (2016). A High-Resolution Crystal Structure of a Psychrohalophilic alpha-Carbonic Anhydrase from Photobacterium profundum Reveals a Unique Dimer Interface. PLOS ONE, 11(12). https://doi.org/10.1371/journal.pone.0168022

Lu, H., Yuan, W., Cheng, J., Rose, R. B., Classen, J. J., & Simmons, O. D. (2016). Modeling the Growth of Archaeon Halobacterium halobium Affected by Temperature and Light. Applied Biochemistry and Biotechnology, 181(3), 1080–1095. https://doi.org/10.1007/s12010-016-2270-x

Friedenberg, S. G., Buhrman, G., Chdid, L., Olby, N. J., Olivry, T., Guillaumin, J., … Meurs, K. M. (2015). Evaluation of a DLA-79 allele associated with multiple immune-mediated diseases in dogs. Immunogenetics, 68(3), 205–217. https://doi.org/10.1007/s00251-015-0894-6

Wang, D., Coco, M. W., & Rose, R. B. (2015). Interactions with the Bifunctional Interface of the Transcriptional Coactivator DCoH1 Are Kinetically Regulated. JOURNAL OF BIOLOGICAL CHEMISTRY, 290(7), 4319–4329. https://doi.org/10.1074/jbc.m114.616870

Golla, J. P., Zhao, J., Mann, I. K., Sayeed, S. K., Mandal, A., Rose, R. B., & Vinson, C. (2014). Carboxylation of cytosine (5caC) in the CG dinucleotide in the E-box motif (CGCAG vertical bar GTG) increases binding of the Tcf3 vertical bar Ascl1 helix-loop-helix heterodimer 10-fold. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 449(2), 248–255. https://doi.org/10.1016/j.bbrc.2014.05.018

Babin, V., Wang, D., Rose, R. B., & Sagui, C. (2013). Binding Polymorphism in the DNA Bound State of the Pdx1 Homeodomain. PLOS COMPUTATIONAL BIOLOGY, 9(8). https://doi.org/10.1371/journal.pcbi.1003160

Lu, X., Guanga, G. P., Wan, C., & Rose, R. B. (2012). A Novel DNA Binding Mechanism for maf Basic Region-Leucine Zipper Factors Inferred from a MafA-DNA Complex Structure and Binding Specificities. BIOCHEMISTRY, 51(48), 9706–9717. https://doi.org/10.1021/bi301248j

Martin, S. L., Guenther, R. H., Sit, T. L., Swartz, P. D., Meilleur, F., Lommel, S. A., … Section, F. (2010). Crystallization and preliminary X-ray diffraction analysis of red clover necrotic mosaic virus. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 66(Pt 11), 1458–1462. https://doi.org/10.1107/s1744309110032483

Rho, H., Jones, C. N., & Rose, R. B. (2010). Kinetic Stability May Determine the Interaction Dynamics of the Bifunctional Protein DCoH1, the Dimerization Cofactor of the Transcription Factor HNF-1 alpha. BIOCHEMISTRY, 49(47), 10187–10197. https://doi.org/10.1021/bi1015056

Serrano, V. S., Davis, M. F., Gaff, J. F., Zhang, Q., Chen, Z., D'Antonio, E. L., … Franzen, S. (2010). X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: Evidence for photoreductive dissociation of the iron-cyanide bond. Acta Crystallographica. Section D, Biological Crystallography, 66, 770–782.

Longo, A., Guanga, G. P., & Rose, R. B. (2008). Crystal structure of E47 neuroD1/Beta2 bHLH domain DNA complex: Heterodimer selectivity and DNA recognition. BIOCHEMISTRY, 47(1), 218–229. https://doi.org/10.1021/bi701527r

Longo, A., Guanga, G. P., & Rose, R. B. (2007). Structural Basis for Induced Fit Mechanisms in DNA Recognition by the Pdx1 Homeodomain†,‡. Biochemistry, 46(11), 2948–2957. https://doi.org/10.1021/bi060969l

Longo, A., Guanga, G. P., & Rose, R. (2007). Structural basis for induced fit mechanisms in DNA recognition by the Pdx1 homeodomain. Biochemistry, 46(11), 2948–2957. https://doi.org/10.1021/bi0609691

Wan, C., Tempel, W., Liu, Z. J., Wang, B. C., & Rose, R. B. (2005). Structure of the conserved transcriptional repressor enhancer of rudimentary homolog. BIOCHEMISTRY, 44(13), 5017–5023. https://doi.org/10.1021/bi047785w

Rose, R. B., Pullen, K. E., Bayle, J. H., Crabtree, G. R., & Alber, T. (2004). Biochemical and structural basis for partially redundant enzymatic and ranscriptional functions of DCoH and DCoH2. BIOCHEMISTRY, 43(23), 7345–7355. https://doi.org/10.1021/bi049620t

Rose, R. B., Craik, C. S., & Stroud, R. M. (1998). Domain flexibility in retroviral proteases: structural implications for drug resistant mutations. Biochemistry. https://doi.org/10.1021/bi9716074

Rose, R. B., Craik, C. S., Douglas, N. L., & Stroud, R. M. (1996). Three-dimensional structures of HIV-1 and SIV protease product complexes. Biochemistry. https://doi.org/10.1021/bi9612733

Rose, R. B., Salto, R., Craik, C. S., & Stroud, R. M. (1993). Structure of the protease from simian immunodeficiency virus: complex with an irreversible nonpeptide inhibitor. Biochemistry. https://doi.org/10.1021/bi00097a030