Publications

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Ma, W., and Goldberg, J. (2013) Rules for the recognition of dilysine retrieval motifs by coatomer. EMBO J. 32, 926-37
Ma, W., and Goldberg, J. (2016) TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats. Proc Natl Acad Sci U S A. 113, 10061-6
Ma, J. K., Carrell, C. J., F Mathews, S., and Davidson, V. L. (2006) Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated. Biochemistry. 45, 8284-93
Ma, W., Goldberg, E., and Goldberg, J. (2017) ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate. Elife. 10.7554/eLife.26624
Ma, J., Lei, H. - T., Reyes, F. E., Sanchez-Martinez, S., Sarhan, M. F., Hattne, J., and Gonen, T. (2019) Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS. Proc Natl Acad Sci U S A. 10.1073/pnas.1806206116
Macdonald, R., Mahoney, B. J., Soule, J., Goring, A. K., Ford, J., Loo, J. A., Cascio, D., and Clubb, R. T. (2023) The Shr receptor from uses a cap and release mechanism to acquire heme-iron from human hemoglobin. Proc Natl Acad Sci U S A. 120, e2211939120
Macdonald, R., Cascio, D., Collazo, M. J., Phillips, M., and Clubb, R. T. (2018) The Shr protein captures human hemoglobin using two structurally unique binding domains. J Biol Chem. 293, 18365-18377
MacDonald, E. A., Frey, G., Namchuk, M. N., Harrison, S. C., Hinshaw, S. M., and Windsor, I. W. (2021) Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease. ACS Infect Dis. 10.1021/acsinfecdis.1c00237
Maciunas, L. J., Porter, N., Lee, P. J., Gupta, K., and Loll, P. J. (2021) Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. Acta Crystallogr D Struct Biol. 77, 1027-1039
Macpherson, I. S., Kirubakaran, S., Gorla, S. Kumar, Riera, T. V., J D'Aquino, A., Zhang, M., Cuny, G. D., and Hedstrom, L. (2010) The structural basis of Cryptosporidium -specific IMP dehydrogenase inhibitor selectivity. J Am Chem Soc. 132, 1230-1
Maderbocus, R., Fields, B. L., Hamilton, K., Luo, S., Tran, T. H., Dietrich, L. E. P., and Tong, L. (2017) Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nat Commun. 8, 160
Maehigashi, T., Dunkle, J. A., Miles, S. J., and Dunham, C. M. (2014) Structural insights into +1 frameshifting promoted by expanded or modification-deficient anticodon stem loops. Proc Natl Acad Sci U S A. 111, 12740-5
Mahbub, L., Kozlov, G., Zong, P., Lee, E. L., Tetteh, S., Nethramangalath, T., Knorn, C., Jiang, J., Shahsavan, A., Yue, L., Runnels, L., and Gehring, K. (2023) Structural insights into regulation of CNNM-TRPM7 divalent cation uptake by the small GTPase ARL15. Elife. 10.7554/eLife.86129
Mahmutovic, S., Clark, L., Levis, S. C., Briggiler, A. M., Enria, D. A., Harrison, S. C., and Abraham, J. (2015) Molecular Basis for Antibody-Mediated Neutralization of New World Hemorrhagic Fever Mammarenaviruses. Cell Host Microbe. 18, 705-13
Mahoney, B. J., Goring, A. K., Wang, Y., Dasika, P., Zhou, A., Grossbard, E., Cascio, D., Loo, J. A., and Clubb, R. T. (2023) Development and atomic structure of a new fluorescence-based sensor to probe heme transfer in bacterial pathogens. J Inorg Biochem. 249, 112368
Mahoney, B. J., Takayesu, A., Zhou, A., Cascio, D., and Clubb, R. T. (2022) The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins. 10.1002/prot.26326
Maisonneuve, P., Sahmi, M., Bergeron-Labrecque, F., Ma, X. Iris, Queguiner, J., Arseneault, G., Lefrançois, M., Kurinov, I., Fronzes, R., Sicheri, F., and Therrien, M. (2024) The CNK-HYP scaffolding complex promotes RAF activation by enhancing KSR-MEK interaction. Nat Struct Mol Biol. 10.1038/s41594-024-01233-6
Maiti, A., Buffalo, C. Z., Saurabh, S., Montecinos-Franjola, F., Hachey, J. S., Conlon, W. J., Tran, G. N., Hassan, B., Walters, K. J., Drobizhev, M., Moerner, W. E., Ghosh, P., Matsuo, H., Tsien, R. Y., Lin, J. Y., and Rodriguez, E. A. (2023) Structural and photophysical characterization of the small ultra-red fluorescent protein. Nat Commun. 14, 4155
Makam, P., Yamijala, S. S. R. K. C., Tao, K., Shimon, L. J. W., Eisenberg, D. S., Sawaya, M. R., Wong, B. M., and Gazit, E. (2019) Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure. Nat Catal. 2, 977-985
Makde, R. D., England, J. R., Yennawar, H. P., and Tan, S. (2010) Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature. 467, 562-6
Makde, R. D., and Tan, S. (2013) Strategies for crystallizing a chromatin protein in complex with the nucleosome core particle. Anal Biochem. 442, 138-45
Malakhova, M., D'Angelo, I., Kim, H. - G., Kurinov, I., Bode, A. M., and Dong, Z. (2010) The crystal structure of the active form of the C-terminal kinase domain of mitogen- and stress-activated protein kinase 1. J Mol Biol. 399, 41-52
Malakhova, M., Tereshko, V., Lee, S. - Y., Yao, K., Cho, Y. - Y., Bode, A., and Dong, Z. (2008) Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2. Nat Struct Mol Biol. 15, 112-3
Malakhova, M., Kurinov, I., Liu, K., Zheng, D., D'Angelo, I., Shim, J. - H., Steinman, V., Bode, A. M., and Dong, Z. (2009) Structural diversity of the active N-terminal kinase domain of p90 ribosomal S6 kinase 2. PLoS One. 4, e8044
G Malmirchegini, R., Sjodt, M., Shnitkind, S., Sawaya, M. R., Rosinski, J., Newton, S. M., Klebba, P. E., and Clubb, R. T. (2014) Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes. J Biol Chem. 289, 34886-99

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