Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Thomas E Frederick"'
Autor:
Matthew A. Cruz, Thomas E. Frederick, Upasana L. Mallimadugula, Sukrit Singh, Neha Vithani, Maxwell I. Zimmerman, Justin R. Porter, Katelyn E. Moeder, Gaya K. Amarasinghe, Gregory R. Bowman
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Many viral proteins are thought to be unlikely candidates for drug discovery as they lack obvious drug binding sites. Here, the authors use computational approaches followed by experimental validation to identify a cryptic pocket within the Ebola vir
Externí odkaz:
https://doaj.org/article/b1138d9e9bae403da917984ac9c6ee9b
Autor:
Wenjie Wang, Woo-Jin Shin, Bojie Zhang, Younho Choi, Ji-Seung Yoo, Maxwell I. Zimmerman, Thomas E. Frederick, Gregory R. Bowman, Michael L. Gross, Daisy W. Leung, Jae U. Jung, Gaya K. Amarasinghe
Publikováno v:
Cell Reports, Vol 30, Iss 1, Pp 153-163.e5 (2020)
Summary: Severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne virus with 12%–30% case mortality rates and is related to the Heartland virus (HRTV) identified in the United States. Together, SFTSV and HRTV are emerging segmented
Externí odkaz:
https://doaj.org/article/7cbd66fb560d401da468d805028c6853
Autor:
Maxwell I. Zimmerman, Kathryn M. Hart, Carrie A. Sibbald, Thomas E. Frederick, John R. Jimah, Catherine R. Knoverek, Niraj H. Tolia, Gregory R. Bowman
Publikováno v:
ACS Central Science, Vol 3, Iss 12, Pp 1311-1321 (2017)
Externí odkaz:
https://doaj.org/article/74ea6caeaaeb48979b0f3c73141052a4
Autor:
Thomas E Frederick, Jeffrey W Peng
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0197241 (2018)
Increasing evidence shows that active sites of proteins have non-trivial conformational dynamics. These dynamics include active site residues sampling different local conformations that allow for multiple, and possibly novel, inhibitor binding poses.
Externí odkaz:
https://doaj.org/article/0528a901f0af4733b2fbd7ed16a77f20
Autor:
Kathryn M Hart, Katelyn E Moeder, Chris M W Ho, Maxwell I Zimmerman, Thomas E Frederick, Gregory R Bowman
Publikováno v:
PLoS ONE, Vol 12, Iss 6, p e0178678 (2017)
Allosteric drugs, which bind to proteins in regions other than their main ligand-binding or active sites, make it possible to target proteins considered "undruggable" and to develop new therapies that circumvent existing resistance. Despite growing i
Externí odkaz:
https://doaj.org/article/2e2ae9d93da7443fa8dfefba3b8eff92
Publikováno v:
The Journal of Biological Chemistry
The functional mechanisms of multidomain proteins often exploit interdomain interactions, or "cross-talk." An example is human Pin1, an essential mitotic regulator consisting of a Trp-Trp (WW) domain flexibly tethered to a peptidyl-prolyl isomerase (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae0dcae8fecb0183604f75513c53256b
https://doi.org/10.1074/jbc.ra120.015849
https://doi.org/10.1074/jbc.ra120.015849
Autor:
Sukrit Singh, Gregory R. Bowman, Neha Vithani, Thomas E. Frederick, Maxwell I. Zimmerman, Matthew A. Cruz, Justin R. Porter, Katelyn E. Moeder, Gaya K. Amarasinghe, Upasana L. Mallimadugula
Publikováno v:
Nature communications. 13(1)
Protein-protein and protein-nucleic acid interactions are often considered difficult drug targets because the surfaces involved lack obvious druggable pockets. Cryptic pockets could present opportunities for targeting these interactions, but identify
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9515edf7ff74025634ed131311a4bafc
https://pubmed.ncbi.nlm.nih.gov/35477718
https://pubmed.ncbi.nlm.nih.gov/35477718
Autor:
John S. Welch, di Martino O, Thomas E. Frederick, Anh Vu, Peter G. Ruminski, Gregory R. Bowman, Carl E. Wagner, Gayla Hadwiger, Margaret A. Ferris
The retinoids all-trans retinoic acid (ATRA) and bexarotene are active in acute myeloid leukemia (AML), but responses beyond acute promyelocytic leukemia (APL) have been more modest than APL responses. To determine whether chemical modification of be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2f9fed621593aa47e6977e3631b5346
https://doi.org/10.1101/2021.05.17.444475
https://doi.org/10.1101/2021.05.17.444475
Autor:
Shreya Raavicharla, Gregory R. Bowman, Upasana L. Mallimadugula, Catherine R. Knoverek, Lewis E. Kay, Thomas E. Frederick, Tairan Yuwen, Enrico Rennella, Sukrit Singh
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance A protein is a shape-shifter, but it is currently unclear which of the many structures a protein can adopt are relevant for its function. Here, we examine conformations that contain a “cryptic” pocket (i.e., a pocket absent in ligand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc2bbfa535eaff8c8c2d57de2e3f1e73
https://doi.org/10.1101/2021.04.14.439842
https://doi.org/10.1101/2021.04.14.439842
Autor:
Lindsey J. Moran, Jimmy A. Blair, Garrick H. Gu, Thomas E. Frederick, Bryn Falahee, Rebecca A. Dryer, Tony P. Huang, Hanna L. Shebert, Chau D. Vo, James F. Heinl, John W. Hammond, Shannon Zikovich, Peter D. Young, Taylor N. Jackvony, Douglas R. Wassarman, Juno Cho
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 27:5235-5244
To address the growing need for new antimicrobial agents, we explored whether inhibition of bacterial signaling machinery could inhibit bacterial growth. Because bacteria rely on two-component signaling systems to respond to environmental changes, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26f8cfddccc10170f0a70e8100d0776f
https://doi.org/10.1016/j.bmcl.2017.10.036
https://doi.org/10.1016/j.bmcl.2017.10.036