Found 2722 results
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Chichili, V. Priyanka R., Chew, T. Weng, Shankar, S., Er, S. Yin, Chin, C. Fei, Jobichen, C., Pan, C. Qiurong, Zhou, Y., Yeong, F. May, Low, B. Chuan, and Sivaraman, J. (2021) Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation. Proc Natl Acad Sci U S A. 10.1073/pnas.2014242118
Chien, P., Grant, R. A., Sauer, R. T., and Baker, T. A. (2007) Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors. Structure. 15, 1296-305
Chinai, J. M., Taylor, A. B., Ryno, L. M., Hargreaves, N. D., Morris, C. A., P Hart, J., and Urbach, A. R. (2011) Molecular recognition of insulin by a synthetic receptor. J Am Chem Soc. 133, 8810-3
Chitrakar, I., Iuliano, J. N., He, Y. L., Woroniecka, H. A., Collado, J. Tolentino, Wint, J. M., Walker, S. G., Tonge, P. J., and French, J. B. (2020) Structural Basis for the Regulation of Biofilm Formation and Iron Uptake in by the Blue-Light-Using Photoreceptor, BlsA. ACS Infect Dis. 6, 2592-2603
Chitrakar, I., Ahmed, S. Fardin, Torelli, A. T., and French, J. B. (2021) Structure of the E. coli agmatinase, SPEB. PLoS One. 16, e0248991
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol. 1, 16154
Cho, J., Lee, M., C Cochrane, S., Webster, C. G., Fenton, B. A., Zhao, J., Hong, J., and Zhou, P. (2020) Structural basis of the UDP-diacylglucosamine pyrophosphohydrolase LpxH inhibition by sulfonyl piperazine antibiotics. Proc Natl Acad Sci U S A. 117, 4109-4116
Cho, U. - S., and Harrison, S. C. (2011) Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Proc Natl Acad Sci U S A. 108, 9367-71
Cho, U. - S., and Harrison, S. C. (2011) Ndc10 is a platform for inner kinetochore assembly in budding yeast. Nat Struct Mol Biol. 19, 48-55
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nature Microbiology. 10.1038/nmicrobiol.2016.154
Choi, P. H., Jo, J., Lin, Y. - C., Lin, M. - H., Chou, C. - Y., Dietrich, L. E. P., and Tong, L. (2016) A distinct holoenzyme organization for two-subunit pyruvate carboxylase. Nat Commun. 7, 12713
Choi, J. Yong, Fuerst, R., Knapinska, A. M., Taylor, A. B., Smith, L., Cao, X., P Hart, J., Fields, G. B., and Roush, W. R. (2017) Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors. J Med Chem. 60, 5816-5825
Choi, M., Sukumar, N., F Mathews, S., Liu, A., and Davidson, V. L. (2011) Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface. Biochemistry. 50, 1265-73
Choi, M., Sukumar, N., Liu, A., and Davidson, V. L. (2009) Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry. 48, 9174-84
Choi, E. H., Suh, S., Sander, C. L., Hernandez, C. J. Ortiz, Bulman, E. R., Khadka, N., Dong, Z., Shi, W., Palczewski, K., and Kiser, P. D. (2018) Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65. Hum Mol Genet. 10.1093/hmg/ddy128
Choi, P. H., Vu, T. Minh Ngoc, Pham, H. Thi, Woodward, J. J., Turner, M. S., and Tong, L. (2017) Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria. Proc Natl Acad Sci U S A. 114, E7226-E7235
Chou, C. - Y., and Tong, L. (2011) Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization. J Biol Chem. 286, 24417-25
Chou, T. - H., Delmar, J. A., Wright, C. C., Kumar, N., Radhakrishnan, A., Doh, J. K., Licon, M. H., Bolla, J. Reddy, Lei, H. - T., Rajashankar, K. R., Su, C. - C., Purdy, G. E., and Yu, E. W. (2015) Crystal structure of the Mycobacterium tuberculosis transcriptional regulator Rv0302. Protein Sci. 24, 1942-55
Choudhary, D., Narui, Y., Neel, B. L., Wimalasena, L. N., Klanseck, C. F., De-la-Torre, P., Chen, C., Araya-Secchi, R., Tamilselvan, E., and Sotomayor, M. (2020) Structural determinants of protocadherin-15 mechanics and function in hearing and balance perception. Proc Natl Acad Sci U S A. 10.1073/pnas.1920444117
Chowdary, T. K., Cairns, T. M., Atanasiu, D., Cohen, G. H., Eisenberg, R. J., and Heldwein, E. E. (2010) Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL. Nat Struct Mol Biol. 17, 882-8
Chowdhury, C., Chun, S., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2016) The function of the PduJ microcompartment shell protein is determined by the genomic position of its encoding gene. Mol Microbiol. 101, 770-83
Chowdhury, C., Chun, S., Pang, A., Sawaya, M. R., Sinha, S., Yeates, T. O., and Bobik, T. A. (2015) Selective molecular transport through the protein shell of a bacterial microcompartment organelle. Proc Natl Acad Sci U S A. 112, 2990-5
Christ, B., Hochstrasser, R., Guyer, L., Francisco, R., Aubry, S., Hörtensteiner, S., and Weng, J. - K. (2017) Non-specific activities of the major herbicide-resistance gene BAR. Nat Plants. 3, 937-945
Christensen, E. M., Bogner, A. N., Vandekeere, A., Tam, G. S., Patel, S. M., Becker, D. F., Fendt, S. - M., and Tanner, J. J. (2020) Screening for Proline Analog Inhibitors of the Proline Cycle Enzyme PYCR1. J Biol Chem. 10.1074/jbc.RA120.016106
Christofk, H. R., Heiden, M. G. Vander, Wu, N., Asara, J. M., and Cantley, L. C. (2008) Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature. 452, 181-6