Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Dustin S Whitney"'
Autor:
Douglas P Anderson, Dustin S Whitney, Victor Hanson-Smith, Arielle Woznica, William Campodonico-Burnett, Brian F Volkman, Nicole King, Joseph W Thornton, Kenneth E Prehoda
Publikováno v:
eLife, Vol 5 (2016)
Externí odkaz:
https://doaj.org/article/d163b99aabce4d4e869921863c92c4b2
Autor:
Douglas P Anderson, Dustin S Whitney, Victor Hanson-Smith, Arielle Woznica, William Campodonico-Burnett, Brian F Volkman, Nicole King, Joseph W Thornton, Kenneth E Prehoda
Publikováno v:
eLife, Vol 5 (2016)
To form and maintain organized tissues, multicellular organisms orient their mitotic spindles relative to neighboring cells. A molecular complex scaffolded by the GK protein-interaction domain (GKPID) mediates spindle orientation in diverse animal ta
Externí odkaz:
https://doaj.org/article/7a65c4bcff1e44fe918790d2f5a1f597
Autor:
Brian F. Volkman, Dustin S. Whitney
Publikováno v:
Biophysical Reviews. 7:183-190
Allostery is commonly described as a functional connection between two distant sites in a protein, where a binding event at one site alters affinity at the other. Here, we review the conformational dynamics that encode an allosteric switch in the PDZ
Conformational flexibility allows proteins to adopt multiple functionally important conformations, but can also lead to non-functional structures. We analyzed the dynamic behavior of the enzyme Guanylate Kinase as it evolved into the GK protein inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2177ba87a6904fdfacbdff3be718a79d
https://europepmc.org/articles/PMC5661941/
https://europepmc.org/articles/PMC5661941/
Autor:
Brian F. Volkman, Kenneth E. Prehoda, Dustin S. Whitney, Francis C. Peterson, John M. Egner, Aaron W. Kittell
Par-6 is a scaffold protein that organizes other proteins into a complex required to initiate and maintain cell polarity. Cdc42-GTP binds the CRIB module of Par-6 and alters the binding affinity of the adjoining PDZ domain. Allosteric regulation of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c0c1dc16437ca3b64d04fe2c7f88924
https://europepmc.org/articles/PMC5433836/
https://europepmc.org/articles/PMC5433836/
Autor:
Joseph W. Thornton, Brian F. Volkman, Nicole King, Victor Hanson-Smith, Arielle Woznica, William Campodonico-Burnett, Douglas P Anderson, Kenneth E. Prehoda, Dustin S. Whitney
Publikováno v:
eLife, Vol 5 (2016)
Autor:
William Campodonico-Burnett, Joseph W. Thornton, Nicole King, Douglas P Anderson, Brian F. Volkman, Kenneth E. Prehoda, Dustin S. Whitney, Victor Hanson-Smith, Arielle Woznica
Publikováno v:
eLife
eLife, vol 5, iss JANUARY2016
eLife, Vol 5 (2016)
eLife, vol 5, iss JANUARY2016
eLife, Vol 5 (2016)
To form and maintain organized tissues, multicellular organisms orient their mitotic spindles relative to neighboring cells. A molecular complex scaffolded by the GK protein-interaction domain (GKPID) mediates spindle orientation in diverse animal ta
Proteins exist in a delicate balance between the native and unfolded states, where thermodynamic stability may be sacrificed to attain the flexibility required for efficient catalysis, binding, or allosteric control. Partition-defective 6 (Par-6) reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c172bc7b9c704c711b418f430fc273f6
https://europepmc.org/articles/PMC3736553/
https://europepmc.org/articles/PMC3736553/
Autor:
Francis C. Peterson, Kenneth E. Prehoda, Brian F. Volkman, Dustin S. Whitney, John M. Egner, Aaron W. Kittell
Publikováno v:
Biochemistry. 55:2063-2063
Autor:
Christopher A. Johnston, Brian F. Volkman, Chris Q. Doe, Kenneth E. Prehoda, Dustin S. Whitney
New protein functions can require complex sequence changes, but the minimal path is not well understood. The guanylate kinase enzyme (GK enz ), which catalyzes phosphotransfer from ATP to GMP, evolved into the GK domain (GK dom ), a protein-binding d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9356f5de3e7d403f810a5a7b794a8e92
https://europepmc.org/articles/PMC3207680/
https://europepmc.org/articles/PMC3207680/