Publications

Found 177 results
Filters: First Letter Of Last Name is M  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
M
Melly, G. C., Stokas, H., Dunaj, J. L., Hsu, F. - F., Rajavel, M., Su, C. - C., Yu, E. W., and Purdy, G. E. (2019) Structural and functional evidence that lipoprotein LpqN supports cell envelope biogenesis in . J Biol Chem. 10.1074/jbc.RA119.008781
Mélin, L., Abdullayev, S., Fnaiche, A., Vu, V., Suárez, N. González, Zeng, H., Szewczyk, M. M., Li, F., Senisterra, G., Allali-Hassani, A., Chau, I., Dong, A., Woo, S., Annabi, B., Halabelian, L., LaPlante, S. R., Vedadi, M., Barsyte-Lovejoy, D., Santhakumar, V., and Gagnon, A. (2021) Development of LM98, a Small-Molecule TEAD Inhibitor Derived from Flufenamic Acid. ChemMedChem. 16, 2982-3002
Melillo, B., Liang, S., Park, J., Schön, A., Courter, J. R., Lalonde, J. M., Wendler, D. J., Princiotto, A. M., Seaman, M. S., Freire, E., Sodroski, J., Madani, N., Hendrickson, W. A., and Smith, A. B. (2016) Small-Molecule CD4-Mimics: Structure-Based Optimization of HIV-1 Entry Inhibition. ACS Med Chem Lett. 7, 330-4
Meisner, J., Maehigashi, T., André, I., Dunham, C. M., and Moran, C. P. (2012) Structure of the basal components of a bacterial transporter. Proc Natl Acad Sci U S A. 109, 5446-51
Meisburger, S. P., Taylor, A. B., Khan, C. A., Zhang, S., Fitzpatrick, P. F., and Ando, N. (2016) Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering. J Am Chem Soc. 138, 6506-16
Mehta, R. S., Mayers, J. R., Zhang, Y., Bhosle, A., Glasser, N. R., Nguyen, L. H., Ma, W., Bae, S., Branck, T., Song, K., Sebastian, L., Pacheco, J. Avila, Seo, H. - S., Clish, C., Dhe-Paganon, S., Ananthakrishnan, A. N., Franzosa, E. A., Balskus, E. P., Chan, A. T., and Huttenhower, C. (2023) Gut microbial metabolism of 5-ASA diminishes its clinical efficacy in inflammatory bowel disease. Nat Med. 29, 700-709
Mehra-Chaudhary, R., Mick, J., Tanner, J. J., Henzl, M. T., and Beamer, L. J. (2011) Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens. Proteins. 79, 1215-29
Mehboob, S., Song, Y., Witek, M., Long, F., Santarsiero, B. D., Johnson, M. E., and Fung, L. W. - M. (2010) Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation. J Biol Chem. 285, 14572-84
Mehboob, S., Mulhearn, D. C., Truong, K., Johnson, M. E., and Santarsiero, B. D. (2010) Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution.. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1432-5
Meeks, K. R., Ji, J., Protopopov, M. V., Tarkhanova, O. O., Moroz, Y. S., and Tanner, J. J. (2024) Novel Fragment Inhibitors of PYCR1 from Docking-Guided X-ray Crystallography. J Chem Inf Model. 64, 1704-1718
McPartland, L., Heller, D. M., Eisenberg, D. S., Hochschild, A., and Sawaya, M. R. (2018) Atomic insights into the genesis of cellular filaments by globular proteins. Nat Struct Mol Biol. 25, 705-714
McNamara, D. E., Senese, S., Yeates, T. O., and Torres, J. Z. (2015) Structures of potent anticancer compounds bound to tubulin. Protein Sci. 24, 1164-72
McNamara, D. E., Cascio, D., Jorda, J., Bustos, C., Wang, T. - C., Rasche, M. E., Yeates, T. O., and Bobik, T. A. (2014) Structure of dihydromethanopterin reductase, a cubic protein cage for redox transfer. J Biol Chem. 289, 8852-64
McNally, R., Li, Q., Li, K., Dekker, C., Vangrevelinghe, E., Jones, M., Chene, P., Machauer, R., Radimerski, T., and Eck, M. J. (2019) Discovery and structural characterization of ATP-site ligands for the wild-type and V617F-mutant JAK2 pseudokinase domain. ACS Chem Biol. 10.1021/acschembio.8b00722
McNally, R., Toms, A. V., and Eck, M. J. (2016) Crystal Structure of the FERM-SH2 Module of Human Jak2. PLoS One. 11, e0156218
McMillan, B. J., Tibbe, C., Drabek, A. A., Seegar, T. C. M., Blacklow, S. C., and Klein, T. (2017) Structural Basis for Regulation of ESCRT-III Complexes by Lgd. Cell Rep. 19, 1750-1757
McMillan, B. J., Zimmerman, B., Egan, E. D., Lofgren, M., Xu, X., Hesser, A., and Blacklow, S. C. (2017) Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations. Glycobiology. 10.1093/glycob/cwx020
McMillan, B. J., Tibbe, C., Jeon, H., Drabek, A. A., Klein, T., and Blacklow, S. C. (2016) Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III Protein. Cell Rep. 16, 1211-1217
McMillan, B. J., Schnute, B., Ohlenhard, N., Zimmerman, B., Miles, L., Beglova, N., Klein, T., and Blacklow, S. C. (2015) A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. Mol Cell. 57, 912-924
McLaughlin, M. I., Lanz, N. D., Goldman, P. J., Lee, K. - H., Booker, S. J., and Drennan, C. L. (2016) Crystallographic snapshots of sulfur insertion by lipoyl synthase. Proc Natl Acad Sci U S A. 113, 9446-50
McKinney, B., Meyer, P. A., Crosas, M., and Sliz, P. (2017) Extension of research data repository system to support direct compute access to biomedical datasets: enhancing Dataverse to support large datasets. Ann N Y Acad Sci. 1387, 95-104
McKeown, M. R., Shaw, D. L., Fu, H., Liu, S., Xu, X., Marineau, J. J., Huang, Y., Zhang, X., Buckley, D. L., Kadam, A., Zhang, Z., Blacklow, S. C., Qi, J., Zhang, W., and Bradner, J. E. (2014) Biased multicomponent reactions to develop novel bromodomain inhibitors. J Med Chem. 57, 9019-27
McGrath, E., Waschbüsch, D., Baker, B. M., and Khan, A. R. (2019) LRRK2 binds to the Rab32 subfamily in a GTP-dependent manner its armadillo domain. Small GTPases. 10.1080/21541248.2019.1666623
McGinty, R. K., Henrici, R. C., and Tan, S. (2014) Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome. Nature. 514, 591-6
McGee, J. H., Shim, S. Youn, Lee, S. - J., Swanson, P. K., Jiang, Y., Durney, M. A., and Verdine, G. L. (2017) Exceptionally high-affinity Ras binders that remodel its effector domain. J Biol Chem. 10.1074/jbc.M117.816348

Pages