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of 13
pro vyhledávání: '"T Justin Rettenmaier"'
Autor:
Daniel A Keedy, Zachary B Hill, Justin T Biel, Emily Kang, T Justin Rettenmaier, José Brandão-Neto, Nicholas M Pearce, Frank von Delft, James A Wells, James S Fraser
Publikováno v:
eLife, Vol 7 (2018)
Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function.
Externí odkaz:
https://doaj.org/article/f31e59e6c613444c8e3b921c3cf0906f
Akademický článek
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Autor:
Daniel Lim, Michael B. Yaffe, Vladimir Joukov, William G. Dunphy, T. Justin Rettenmaier, Akiko Kumagai, James A. Wells
Publikováno v:
Sci Signal
Cell cycle-dependent redox changes can mediate transient covalent modifications of cysteine thiols to modulate the activities of regulatory kinases and phosphatases. Our previously reported finding that protein cysteine oxidation is increased during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc84ccd37861f047ba0d8f2236115356
https://resolver.caltech.edu/CaltechAUTHORS:20200722-091504306
https://resolver.caltech.edu/CaltechAUTHORS:20200722-091504306
Autor:
Gregory H. Bird, James Luccarelli, Rachel M. Guerra, Loren D. Walensky, Zachary J. Hauseman, Thomas E. Wales, John R. Engen, James A. Wells, Susan Lee, Hyuk-Soo Seo, T. Justin Rettenmaier, Sirano Dhe-Paganon, Catherine E. Newman, Edward P. Harvey, Danny Cohen, Annissa J. Huhn
Publikováno v:
Cell Chem Biol
Summary The BCL-2 family is composed of anti- and pro-apoptotic members that respectively protect or disrupt mitochondrial integrity. Anti-apoptotic overexpression can promote oncogenesis by trapping the BCL-2 homology 3 (BH3) “killer domains” of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c7b1f80414395cfe2149f38f73d4863
https://europepmc.org/articles/PMC7405809/
https://europepmc.org/articles/PMC7405809/
Autor:
Andrej Sali, Julie C. Mitchell, Rahel A. Woldeyes, Peter Cimermancic, Daniel A. Keedy, T. Justin Rettenmaier, Dina Schneidman-Duhovny, James S. Fraser, Leon Bichmann, Patrick Weinkam, James A. Wells, Omar N. A. Demerdash
Publikováno v:
Cimermancic, P; Weinkam, P; Rettenmaier, TJ; Bichmann, L; Keedy, DA; Woldeyes, RA; et al.(2016). CryptoSite: Expanding the Druggable Proteome by Characterization and Prediction of Cryptic Binding Sites. JOURNAL OF MOLECULAR BIOLOGY, 428(4), 709-719. doi: 10.1016/j.jmb.2016.01.029. UCSF: Retrieved from: http://www.escholarship.org/uc/item/1c75k2k8
Journal of molecular biology, vol 428, iss 4
Journal of molecular biology, vol 428, iss 4
Many proteins have small molecule-binding pockets that are not easily detectable in the ligand-free structures. These cryptic sites require a conformational change to become apparent; a cryptic site can therefore be defined as a site that forms a poc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd6d6587e04bd3942f1acb82cdeab423
https://doi.org/10.1016/j.jmb.2016.01.029
https://doi.org/10.1016/j.jmb.2016.01.029
Autor:
E. Kang, Justin T Biel, Z.B. Hill, José Brandão-Neto, Frank von Delft, James A. Wells, Daniel A. Keedy, James S. Fraser, Nicholas M Pearce, T. Justin Rettenmaier
Publikováno v:
eLife, Vol 7 (2018)
ELIFE, vol 7
Keedy, DA; Hill, ZB; Biel, JT; Kang, E; Rettenmaier, TJ; Brandão-Neto, J; et al.(2018). An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering. eLife, 7. doi: 10.7554/eLife.36307. UCSF: Retrieved from: http://www.escholarship.org/uc/item/4tk2c02t
Keedy, DA; Hill, ZB; Biel, JT; Kang, E; Rettenmaier, TJ; Brandao-Neto, J; et al.(2018). An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering. ELIFE, 7. doi: 10.7554/eLife.36307.001. UCSF: Retrieved from: http://www.escholarship.org/uc/item/6w5970b7
eLife
ELIFE, vol 7
Keedy, DA; Hill, ZB; Biel, JT; Kang, E; Rettenmaier, TJ; Brandão-Neto, J; et al.(2018). An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering. eLife, 7. doi: 10.7554/eLife.36307. UCSF: Retrieved from: http://www.escholarship.org/uc/item/4tk2c02t
Keedy, DA; Hill, ZB; Biel, JT; Kang, E; Rettenmaier, TJ; Brandao-Neto, J; et al.(2018). An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering. ELIFE, 7. doi: 10.7554/eLife.36307.001. UCSF: Retrieved from: http://www.escholarship.org/uc/item/6w5970b7
eLife
Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8dd86c17f8f80e5ecc812260f93d5cd
https://elifesciences.org/articles/36307
https://elifesciences.org/articles/36307
Autor:
James A. Wells, T. Justin Rettenmaier, Justin T Biel, Frank von Delft, Daniel A. Keedy, James S. Fraser, José Brandão-Neto, Nicholas M Pearce, Z.B. Hill, E. Kang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d3e479521fef1bf1c07c549e9cef8ac
https://doi.org/10.7554/elife.36307.045
https://doi.org/10.7554/elife.36307.045
Autor:
Hao Fan, Andrej Sali, Brian K. Shoichet, Joel Karpiak, James A. Wells, T. Justin Rettenmaier, Allison K. Doak
Publikováno v:
Journal of Medicinal Chemistry. 58:8285-8291
Finding small molecules that target allosteric sites remains a grand challenge for ligand discovery. In the protein kinase field, only a handful of highly selective allosteric modulators have been found. Thus, more general methods are needed to disco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9534bd941fef8bb81a6f8669dd2b836e
https://doi.org/10.1021/acs.jmedchem.5b01216
https://doi.org/10.1021/acs.jmedchem.5b01216
Autor:
Daniel A. Keedy, Zachary B. Hill, Justin T. Biel, Emily Kang, T. Justin Rettenmaier, Jose Brandao-Neto, Nicholas M. Pearce, Frank von Delft, James A. Wells, James S. Fraser
Publikováno v:
Keedy, D; Hill, Z; Biel, J; Kang, E; Rettenmaier, J; Brandao-Neto, J; et al.(2017). New routes for PTP1B allosteric inhibition by multitemperature crystallography, fragment screening and covalent tethering. UCSF: Retrieved from: http://www.escholarship.org/uc/item/1vm7g0ps
Allostery is an inherent feature of proteins and provides alternative routes to regulating function. Small-molecule allosteric inhibitors are often desirable; however, it remains challenging to identify surface sites in proteins which can bind small
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::075f1f751a04335b134654ded0e4b99e
http://www.escholarship.org/uc/item/1vm7g0ps
http://www.escholarship.org/uc/item/1vm7g0ps
Publikováno v:
MedChemComm. 5:370-375
Tethering is a screening technique for discovering small-molecule fragments that bind to pre-determined sites via formation of a disulphide bond. Tethering screens traditionally rely upon mass spectrometry to detect disulphide bind formation, which r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de86b41a5183539ec323eab71a9084cf
https://doi.org/10.1039/c3md00356f
https://doi.org/10.1039/c3md00356f