Publications

Found 1231 results
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2021
Tayeb-Fligelman, E., Cheng, X., Tai, C., Bowler, J. T., Griner, S., Sawaya, M. R., Seidler, P. M., Jiang, Y. Xiao, Lu, J., Rosenberg, G. M., Salwinski, L., Abskharon, R., Zee, C. - T., Hou, K., Li, Y., Boyer, D. R., Murray, K. A., Falcon, G., Anderson, D. H., Cascio, D., Saelices, L., Damoiseaux, R., Guo, F., and Eisenberg, D. S. (2021) Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 10.1101/2021.03.05.434000
Wang, W., and Hendrickson, W. A. (2021) Intermediates in allosteric equilibria of DnaK-ATP interactions with substrate peptides. Acta Crystallogr D Struct Biol. 77, 606-617
Tsai, W. - C., Gilbert, N. C., Ohler, A., Armstrong, M., Perry, S., Kalyanaraman, C., Yasgar, A., Rai, G., Simeonov, A., Jadhav, A., Standley, M., Lee, H. - W., Crews, P., Iavarone, A. T., Jacobson, M. P., Neau, D. B., Offenbacher, A. R., Newcomer, M., and Holman, T. R. (2021) Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2. Bioorg Med Chem. 46, 116349
Iketani, S., Forouhar, F., Liu, H., Hong, S. Jung, Lin, F. - Y., Nair, M. S., Zask, A., Huang, Y., Xing, L., Stockwell, B. R., Chavez, A., and Ho, D. D. (2021) Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors. Nat Commun. 12, 2016
Iketani, S., Forouhar, F., Liu, H., Hong, S. Jung, Lin, F. - Y., Nair, M. S., Zask, A., Huang, Y., Xing, L., Stockwell, B. R., Chavez, A., and Ho, D. D. (2021) Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors. Nat Commun. 12, 2016
Iketani, S., Forouhar, F., Liu, H., Hong, S. Jung, Lin, F. - Y., Nair, M. S., Zask, A., Huang, Y., Xing, L., Stockwell, B. R., Chavez, A., and Ho, D. D. (2021) Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors. Nat Commun. 12, 2016
Dussupt, V., Sankhala, R. S., Mendez-Rivera, L., Townsley, S. M., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G. C., Tran, U., Jackson, N. D., Zaky, W. I., Zemil, M., Tritsch, S. R., Chen, W. - H., Martinez, E. J., Ahmed, A., Choe, M., Chang, W. C., Hajduczki, A., Jian, N., Peterson, C. E., Rees, P. A., Rutkowska, M., Slike, B. M., Selverian, C. N., Swafford, I., Teng, I. - T., Thomas, P. V., Zhou, T., Smith, C. J., Currier, J. R., Kwong, P. D., Rolland, M., Davidson, E., Doranz, B. J., Mores, C. N., Hatziioannou, T., Reiley, W. W., Bieniasz, P. D., Paquin-Proulx, D., Gromowski, G. D., Polonis, V. R., Michael, N. L., Modjarrad, K., M Joyce, G., and Krebs, S. J. (2021) Low-dose in vivo protection and neutralization across SARS-CoV-2 variants by monoclonal antibody combinations. Nat Immunol. 10.1038/s41590-021-01068-z
Dussupt, V., Sankhala, R. S., Mendez-Rivera, L., Townsley, S. M., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G. C., Tran, U., Jackson, N. D., Zaky, W. I., Zemil, M., Tritsch, S. R., Chen, W. - H., Martinez, E. J., Ahmed, A., Choe, M., Chang, W. C., Hajduczki, A., Jian, N., Peterson, C. E., Rees, P. A., Rutkowska, M., Slike, B. M., Selverian, C. N., Swafford, I., Teng, I. - T., Thomas, P. V., Zhou, T., Smith, C. J., Currier, J. R., Kwong, P. D., Rolland, M., Davidson, E., Doranz, B. J., Mores, C. N., Hatziioannou, T., Reiley, W. W., Bieniasz, P. D., Paquin-Proulx, D., Gromowski, G. D., Polonis, V. R., Michael, N. L., Modjarrad, K., M Joyce, G., and Krebs, S. J. (2021) Low-dose in vivo protection and neutralization across SARS-CoV-2 variants by monoclonal antibody combinations. Nat Immunol. 10.1038/s41590-021-01068-z
Gu, W., Gao, S., Wang, H., Fleming, K. D., Hoffmann, R. M., Yang, J. Won, Patel, N. M., Choi, Y. Mi, Burke, J. E., Reue, K., and Airola, M. V. (2021) The middle lipin domain adopts a membrane-binding dimeric protein fold. Nat Commun. 12, 4718
Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P., Bimela, J. S., Bahna, F. A., Mannepalli, S. M., Zhang, B., Kwong, P. D., Huang, Y., Ho, D. D., Shapiro, L., and Sheng, Z. (2021) Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell Rep. 10.1016/j.celrep.2021.108950
Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P., Bimela, J. S., Bahna, F. A., Mannepalli, S. M., Zhang, B., Kwong, P. D., Huang, Y., Ho, D. D., Shapiro, L., and Sheng, Z. (2021) Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell Rep. 10.1016/j.celrep.2021.108950
Borowska, M. T., Drees, C., Yarawsky, A. E., Viswanathan, M., Ryan, S. M., Bunker, J. J., Herr, A. B., Bendelac, A., and Adams, E. J. (2021) The molecular characterization of antibody binding to a superantigen-like protein from a commensal microbe. Proc Natl Acad Sci U S A. 10.1073/pnas.2023898118
Huang, F., Lu, X., Yu, C., Sliz, P., Wang, L., and Zhu, B. (2021) Molecular Dissection of the Primase and Polymerase Activities of Deep-Sea Phage NrS-1 Primase-Polymerase. Front Microbiol. 12, 766612
Schnabl, J., Wang, J., Hohmann, U., Gehre, M., Batki, J., Andreev, V. I., Purkhauser, K., Fasching, N., Duchek, P., Novatchkova, M., Mechtler, K., Plaschka, C., Patel, D. J., and Brennecke, J. (2021) Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex. Genes Dev. 35, 392-409
Patchett, S., Lv, Z., Rut, W., Békés, M., Drag, M., Olsen, S. K., and Huang, T. T. (2021) A molecular sensor determines the ubiquitin substrate specificity of SARS-CoV-2 papain-like protease. Cell Rep. 36, 109754
Tompkins, K. J., Houtti, M., Litzau, L. A., Aird, E. J., Everett, B. A., Nelson, A. T., Pornschloegl, L., Limón-Swanson, L. K., Evans, R. L., Evans, K., Shi, K., Aihara, H., and Gordon, W. R. (2021) Molecular underpinnings of ssDNA specificity by Rep HUH-endonucleases and implications for HUH-tag multiplexing and engineering. Nucleic Acids Res. 49, 1046-1064
Deng, Y., Deng, S., Ho, Y. - H., Gardner, S. M., Huang, Z., Marmorstein, R., and Huang, R. (2021) Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D. J Med Chem. 10.1021/acs.jmedchem.1c00141
Deng, Y., Deng, S., Ho, Y. - H., Gardner, S. M., Huang, Z., Marmorstein, R., and Huang, R. (2021) Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D. J Med Chem. 10.1021/acs.jmedchem.1c00141
Deng, Y., Deng, S., Ho, Y. - H., Gardner, S. M., Huang, Z., Marmorstein, R., and Huang, R. (2021) Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D. J Med Chem. 10.1021/acs.jmedchem.1c00141
Yu, C. H., Bhattacharya, A., Persaud, M., Taylor, A. B., Wang, Z., Bulnes-Ramos, A., Xu, J., Selyutina, A., Martinez-Lopez, A., Cano, K., Demeler, B., Kim, B., Hardies, S. C., Diaz-Griffero, F., and Ivanov, D. N. (2021) Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification. Nat Commun. 12, 731
Zhang, C. - H., Spasov, K. A., Reilly, R. A., Hollander, K., Stone, E. A., Ippolito, J. A., Liosi, M. - E., Deshmukh, M. G., Tirado-Rives, J., Zhang, S., Liang, Z., Miller, S. J., Isaacs, F., Lindenbach, B. D., Anderson, K. S., and Jorgensen, W. L. (2021) Optimization of Triarylpyridinone Inhibitors of the Main Protease of SARS-CoV-2 to Low-Nanomolar Antiviral Potency. ACS Med Chem Lett. 12, 1325-1332
Sea, K. W., Taylor, A. B., Thomas, S. T., Liba, A., Bergman, I. B., Holloway, S. P., Cao, X., Gralla, E. B., Valentine, J. S., P Hart, J., and Galaleldeen, A. (2021) A pH Switch Controls Zinc Binding in Tomato Copper-Zinc Superoxide Dismutase. Biochemistry. 60, 1597-1608
Sea, K. W., Taylor, A. B., Thomas, S. T., Liba, A., Bergman, I. B., Holloway, S. P., Cao, X., Gralla, E. B., Valentine, J. S., P Hart, J., and Galaleldeen, A. (2021) A pH Switch Controls Zinc Binding in Tomato Copper-Zinc Superoxide Dismutase. Biochemistry. 60, 1597-1608
Shah, M., Taylor, V. L., Bona, D., Tsao, Y., Stanley, S. Y., Pimentel-Elardo, S. M., McCallum, M., Bondy-Denomy, J., P Howell, L., Nodwell, J. R., Davidson, A. R., Moraes, T. F., and Maxwell, K. L. (2021) A phage-encoded anti-activator inhibits quorum sensing in Pseudomonas aeruginosa. Mol Cell. 81, 571-583.e6
Chen, S., Tjin, C. Chandra, Gao, X., Xue, Y., Jiao, H., Zhang, R., Wu, M., He, Z., Ellman, J., and Ha, Y. (2021) Pharmacological inhibition of PI5P4Kα/β disrupts cell energy metabolism and selectively kills p53-null tumor cells.. Proc Natl Acad Sci U S A. 10.1073/pnas.2002486118

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