Publications

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Modak, D., and Sotomayor, M. (2019) Identification of an adhesive interface for the non-clustered δ1 protocadherin-1 involved in respiratory diseases.. Commun Biol. 2, 354
Mitcheltree, M. J., Pisipati, A., Syroegin, E. A., Silvestre, K. J., Klepacki, D., Mason, J. D., Terwilliger, D. W., Testolin, G., Pote, A. R., J Y Wu, K., Ladley, R. Porter, Chatman, K., Mankin, A. S., Polikanov, Y. S., and Myers, A. G. (2021) A synthetic antibiotic class overcoming bacterial multidrug resistance. Nature. 10.1038/s41586-021-04045-6
Mishra, A., Devarajan, B., Reardon, M. E., Dwivedi, P., Krishnan, V., Cisar, J. O., Das, A., Narayana, S. V. L., and Ton-That, H. (2011) Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development. Mol Microbiol. 81, 1205-20
Misaghi, S., Galardy, P. J., Meester, W. J. N., Ovaa, H., Ploegh, H. L., and Gaudet, R. (2005) Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J Biol Chem. 280, 1512-20
Mir, A., Chen, J., Robinson, K., Lendy, E., Goodman, J., Neau, D., and Golden, B. L. (2015) Two Divalent Metal Ions and Conformational Changes Play Roles in the Hammerhead Ribozyme Cleavage Reaction. Biochemistry. 54, 6369-81
Minuesa, G., Albanese, S. K., Xie, W., Kazansky, Y., Worroll, D., Chow, A., Schurer, A., Park, S. - M., Rotsides, C. Z., Taggart, J., Rizzi, A., Naden, L. N., Chou, T., Gourkanti, S., Cappel, D., Passarelli, M. C., Fairchild, L., Adura, C., J Glickman, F., Schulman, J., Famulare, C., Patel, M., Eibl, J. K., Ross, G. M., Bhattacharya, S., Tan, D. S., Leslie, C. S., Beuming, T., Patel, D. J., Goldgur, Y., Chodera, J. D., and Kharas, M. G. (2019) Small-molecule targeting of MUSASHI RNA-binding activity in acute myeloid leukemia. Nat Commun. 10, 2691
Min, A. B., Miallau, L., Sawaya, M. R., Habel, J., Cascio, D., and Eisenberg, D. (2012) The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex from M. tuberculosis reveals a Mg²⁺ ion in the active site and a putative RNA-binding site.. Protein Sci. 21, 1754-67
Min, J. - H., and Pavletich, N. P. (2007) Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature. 449, 570-5
Miller, B. R., and Kung, Y. (2017) Structural Features and Domain Movements Controlling Substrate Binding and Cofactor Specificity in Class II HMG-CoA Reductase. Biochemistry. 10.1021/acs.biochem.7b00999
Miller, J. E., Agdanowski, M. P., Dolinsky, J. L., Sawaya, M. R., Cascio, D., Rodriguez, J. A., and Yeates, T. O. (2024) AlphaFold-assisted structure determination of a bacterial protein of unknown function using X-ray and electron crystallography. Acta Crystallogr D Struct Biol. 80, 270-278
Miller, B. R., and Kung, Y. (2018) Structural insight into substrate and product binding in an archaeal mevalonate kinase. PLoS One. 13, e0208419
Miller, A. Kern, Morgen, M., Steimbach, R. R., Géraldy, M., Hellweg, L., Sehr, P., Ridinger, J., Witt, O., Oehme, I., Herbst-Gervasoni, C. J., Osko, J. D., Porter, N. J., Christianson, D. W., and Gunkel, N. (2020) Design and Synthesis of Dihydroxamic Acids as HDAC6/8/10 Inhibitors. ChemMedChem. 10.1002/cmdc.202000149
Mikhaylov, V., Brambley, C. A., Keller, G. L. J., Arbuiso, A. G., Weiss, L. I., Baker, B. M., and Levine, A. J. (2023) Accurate modeling of peptide-MHC structures with AlphaFold. Structure. 10.1016/j.str.2023.11.011
Mielecki, M., Krawiec, K., Kiburu, I., Grzelak, K., Zagórski, W., Kierdaszuk, B., Kowa, K., Fokt, I., Szymanski, S., Swierk, P., Szeja, W., Priebe, W., Lesyng, B., and LaRonde-LeBlanc, N. (2013) Development of novel molecular probes of the Rio1 atypical protein kinase. Biochim Biophys Acta. 1834, 1292-301
Mieher, J. L., Larson, M. R., Schormann, N., Purushotham, S., Wu, R., Rajashankar, K. R., Wu, H., and Deivanayagam, C. (2018) Glucan Binding Protein C of Mediates both Sucrose-Independent and Sucrose-Dependent Adherence. Infect Immun. 10.1128/IAI.00146-18
Mieher, J. L., Schormann, N., Wu, R., Patel, M., Purushotham, S., Wu, H., Scoffield, J., and Deivanayagam, C. (2021) Structure-Function Characterization of Streptococcus intermedius Surface Antigen Pas. J Bacteriol. 203, e0017521
Miallau, L., Jain, P., Arbing, M. A., Cascio, D., Phan, T., Ahn, C. J., Chan, S., Chernishof, I., Maxson, M., Chiang, J., Jacobs, W. R., and Eisenberg, D. S. (2013) Comparative proteomics identifies the cell-associated lethality of M. tuberculosis RelBE-like toxin-antitoxin complexes. Structure. 21, 627-37
Miallau, L., Faller, M., Chiang, J., Arbing, M., Guo, F., Cascio, D., and Eisenberg, D. (2009) Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J Biol Chem. 284, 276-83
Mi, L. - Z., Brown, C. T., Gao, Y., Tian, Y., Le, V. Q., Walz, T., and Springer, T. A. (2015) Structure of bone morphogenetic protein 9 procomplex. Proc Natl Acad Sci U S A. 112, 3710-5
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Metrick, C. M., and Heldwein, E. E. (2016) Novel Structure and Unexpected RNA-Binding Ability of the C-Terminal Domain of Herpes Simplex Virus 1 Tegument Protein UL21. J Virol. 90, 5759-69
Metelev, M., Osterman, I. A., Ghilarov, D., Khabibullina, N. F., Yakimov, A., Shabalin, K., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M., Artamonova, T., Khodorkovskii, M., Konevega, A. L., Sergiev, P. V., Severinov, K., and Polikanov, Y. S. (2017) Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel. Nat Chem Biol. 10.1038/nchembio.2462
Merz, G. E., Borbat, P. P., Muok, A. R., Srivastava, M., Bunck, D. N., Freed, J. H., and Crane, B. R. (2018) Site-Specific Incorporation of a Cu Spin-Label Into Proteins for Measuring Distances by Pulsed Dipolar ESR Spectroscopy. J Phys Chem B. 10.1021/acs.jpcb.8b05619
Melton, S. D., Brackhahn, E. A. E., Orlin, S. J., Jin, P., and Chenoweth, D. M. (2020) Rules for the design of aza-glycine stabilized triple-helical collagen peptides. Chem Sci. 11, 10638-10646
Melnikov, S. V., Khabibullina, N. F., Mairhofer, E., Vargas-Rodriguez, O., Reynolds, N. M., Micura, R., Söll, D., and Polikanov, Y. S. (2018) Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site. Nucleic Acids Res. 10.1093/nar/gky1211

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