Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Hesam N Motlagh"'
Autor:
Jing Li, Jordan T White, Harry Saavedra, James O Wrabl, Hesam N Motlagh, Kaixian Liu, James Sowers, Trina A Schroer, E Brad Thompson, Vincent J Hilser
Publikováno v:
eLife, Vol 7 (2018)
Externí odkaz:
https://doaj.org/article/c0004bf7a3a046f2a14e1fb94a4b0b58
Autor:
Jing Li, Jordan T White, Harry Saavedra, James O Wrabl, Hesam N Motlagh, Kaixian Liu, James Sowers, Trina A Schroer, E Brad Thompson, Vincent J Hilser
Publikováno v:
eLife, Vol 6 (2017)
Intrinsically disordered proteins (IDPs) present a functional paradox because they lack stable tertiary structure, but nonetheless play a central role in signaling, utilizing a process known as allostery. Historically, allostery in structured protein
Externí odkaz:
https://doaj.org/article/81a4ece1461a4f0e95dcde41379da803
Publikováno v:
Biophysical Journal. 110:1280-1290
Single-molecule force spectroscopy has emerged as a powerful tool for studying the folding of biological macromolecules. Mechanical manipulation has revealed a wealth of mechanistic information on transient and intermediate states. To date, the major
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b7e6a31ce29308c71a8ab522733b5d3
https://doi.org/10.1016/j.bpj.2015.12.042
https://doi.org/10.1016/j.bpj.2015.12.042
Publikováno v:
Biophysical Reviews. 7:257-265
Allostery is a biological regulation mechanism of significant importance in cell signaling, metabolism, and disease. Although the ensemble basis of allostery has been known for years, only recently has emphasis shifted from interpreting allosteric me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::574008c93bf48a7a6af772cb64241212
https://doi.org/10.1007/s12551-015-0173-7
https://doi.org/10.1007/s12551-015-0173-7
Autor:
E. Brad Thompson, Jing Li, Trina A. Schroer, Kaixian Liu, James O. Wrabl, James Sowers, Harry Saavedra, Vincent J. Hilser, Jordan T. White, Hesam N. Motlagh
Publikováno v:
eLife, Vol 6 (2017)
eLife
eLife
Proteins carry out most of the key tasks inside cells. To perform these roles, proteins must fold up to form complex three-dimensional structures. Researchers used to think that the useful parts of proteins all had set structures. However, we now kno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b13b0a3506a39581056ba9281ab52c2
https://elifesciences.org/articles/30688
https://elifesciences.org/articles/30688
Autor:
Jing Li, Jordan T White, Harry Saavedra, James O Wrabl, Hesam N Motlagh, Kaixian Liu, James Sowers, Trina A Schroer, E Brad Thompson, Vincent J Hilser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e1d3029cbb6266e609964f78e235031
https://doi.org/10.7554/elife.30688.017
https://doi.org/10.7554/elife.30688.017
Publikováno v:
Nature. 508:331-339
Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5429dc8d3d0219227dbed225a09bcc70
https://doi.org/10.1038/nature13001
https://doi.org/10.1038/nature13001
Publikováno v:
Journal of Biological Chemistry. 287:26777-26787
Intrinsically disordered (ID) sequence segments are abundant in cell signaling proteins and transcription factors. Because ID regions commonly fold as part of their intracellular function, it is crucial to understand the folded states as well as the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b38e60d89d76ad7f24d9db35d607261
https://doi.org/10.1074/jbc.m112.355651
https://doi.org/10.1074/jbc.m112.355651
Publikováno v:
Annual Review of Biophysics. 41:585-609
Allostery is a biological phenomenon of fundamental importance in regulation and signaling, and efforts to understand this process have led to the development of numerous models. In spite of individual successes in understanding the structural determ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67af0939bc121db93a554e36abb69e84
https://doi.org/10.1146/annurev-biophys-050511-102319
https://doi.org/10.1146/annurev-biophys-050511-102319
Publikováno v:
Nuclear Receptors: From Structure to the Clinic ISBN: 9783319187280
Nuclear Hormone Receptors (NHRs) must respond to a variety of chemical cues to selectively induce or repress pertinent genes. Each domain of these multidomain proteins is capable of binding to various large or small molecules, and such binding may al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5dfb2c797a60f25a34ad30eb0ba5952d
https://doi.org/10.1007/978-3-319-18729-7_5
https://doi.org/10.1007/978-3-319-18729-7_5