Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Glenna Wink"'
Publikováno v:
In Trends in Biotechnology April 2024 42(4):449-463
Autor:
Foight, Glenna Wink, Keating, Amy E.
Publikováno v:
In Journal of Molecular Biology 31 July 2015 427(15):2468-2490
Autor:
Glenna Wink Foight, Per Jr Greisen, Cindy T. Wei, Dustin J. Maly, David Baker, Zhizhi Wang, William Sheffler, T. J. Brunette, Daniel Cunningham-Bryant, Keunwan Park, Katrina M Warner
Publikováno v:
Nature biotechnology
Chemical and optogenetic methods for post-translationally controlling protein function have enabled new discoveries and the engineering of synthetic cellular functions. However, most of these methods only confer single-input, single-output control. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cafa4057abcaab4c5e6bb99e5a24287
https://doi.org/10.1038/s41587-019-0242-8
https://doi.org/10.1038/s41587-019-0242-8
Autor:
Glenna Wink Foight, Daniel Cunningham-Bryant, John C. Rose, Dana E. Loutey, Dustin J. Maly, Emily M. Dieter
Publikováno v:
Journal of the American Chemical Society. 141:3352-3355
Chemical methods that allow the spatial proximity of proteins to be temporally modulated are powerful tools for studying biology and engineering synthetic cellular behaviors. Here, we describe a new chemically-controlled method for rapidly disrupting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::799775c12c4b54d21a5910fec1cf4c84
https://doi.org/10.1021/jacs.8b12382
https://doi.org/10.1021/jacs.8b12382
Autor:
Lauren Carter, Binchen Mao, Joshua C. Vaughan, Enrique Marcos, Matthew J. Bick, Hahnbeom Park, Po-Ssu Huang, Banumathi Sankaran, Min Yen Lee, William Sheffler, Glenna Wink Foight, Barry L. Stoddard, Sergey Ovchinnikov, David Baker, Anastassia A. Vorobieva, Lindsey Doyle, Lauren A. Gagnon, Jiayi Dou
Publikováno v:
Nature, vol 561, iss 7724
Nature
Nature
The regular arrangements of β-strands around a central axis in β-barrels and of α-helices in coiled coils contrast with the irregular tertiary structures of most globular proteins, and have fascinated structural biologists since they were first di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c145c7e626e146f69c1f7eb54d5ef660
https://pubmed.ncbi.nlm.nih.gov/30254342
https://pubmed.ncbi.nlm.nih.gov/30254342
Akademický článek
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Publikováno v:
ACS Chemical Biology
Mcl-1 is overexpressed in many cancers and can confer resistance to cell-death signaling in refractory disease. Molecules that specifically inhibit Mcl-1 hold potential for diagnosing and disrupting Mcl-1-dependent cell survival. We selected three pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6426750137e36430771cbe6c6b6e022
https://doi.org/10.1021/cb500340w
https://doi.org/10.1021/cb500340w
Publikováno v:
Methods in Molecular Biology ISBN: 9781493967964
PMC
PMC
Peptide reagents with high affinity or specificity for their target protein interaction partner are of utility for many important applications. Optimization of peptide binding by screening large libraries is a proven and powerful approach. Libraries
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51dc45c45477be4d7fb7909df5fa64b8
https://europepmc.org/articles/PMC5553629/
https://europepmc.org/articles/PMC5553629/
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 76:861-881
The multiple solvent crystal structures (MSCS) method uses organic solvents to map the surfaces of proteins. It identifies binding sites and allows for a more thorough examination of protein plasticity and hydration than could be achieved by a single
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79fca6b29d3c80f91309eb34043be57d
https://doi.org/10.1002/prot.22393
https://doi.org/10.1002/prot.22393
Publikováno v:
Structure. 15(12):1618-1629
Summary Transformation efficiencies of Ras mutants at residue 61 range over three orders of magnitude, but the in vitro GTPase activity decreases 10-fold for all mutants. We show that Raf impairs the GTPase activity of RasQ61L, suggesting that the Ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de94cb71ed7bf07316863579da08a567