Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Andrea N. Kravats"'
Autor:
Anna Clara Miranda Moura, Isaac K. Asare, Mateo Fernandez Cruz, Antonio Javier Franco Aguado, Kaeleigh Dyan Tuck, Conner C. Campbell, Matthew W. Scheyer, Ikponwmosa Obaseki, Steve Alston, Andrea N. Kravats, Charles R. Sanders, Gary A. Lorigan, Indra D. Sahu
Publikováno v:
Membranes, Vol 14, Iss 2, p 45 (2024)
KCNE3 is a single-pass integral membrane protein that regulates numerous voltage-gated potassium channel functions such as KCNQ1. Previous solution NMR studies suggested a moderate degree of curved α-helical structure in the transmembrane domain (TM
Externí odkaz:
https://doaj.org/article/f8ac973c94f44591a95a61186b1b0d48
Autor:
Isaac K. Asare, Alberto Perez Galende, Andres Bastidas Garcia, Mateo Fernandez Cruz, Anna Clara Miranda Moura, Conner C. Campbell, Matthew Scheyer, John Paul Alao, Steve Alston, Andrea N. Kravats, Charles R. Sanders, Gary A. Lorigan, Indra D. Sahu
Publikováno v:
Membranes, Vol 12, Iss 5, p 469 (2022)
KCNE3 is a potassium channel accessory transmembrane protein that regulates the function of various voltage-gated potassium channels such as KCNQ1. KCNE3 plays an important role in the recycling of potassium ion by binding with KCNQ1. KCNE3 can be fo
Externí odkaz:
https://doaj.org/article/611b6e3967204d6eae590330c9a4c38e
Autor:
Anushka Wickramaratne, Jui-Yun Liao, Shannon M. Doyle, Joel R. Hoskins, Gabrielle Puller, John Paul Alao, Ikponwmosa Obaseki, Madison L. Scott, Jerry C. Dinan, Tapan K. Maity, Lisa M. Jenkins, Andrea N. Kravats, Sue Wickner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48020777afa9fbf2d2b90ba0e8f08690
https://doi.org/10.2139/ssrn.4372926
https://doi.org/10.2139/ssrn.4372926
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 1, p e1004675 (2016)
Clp ATPases are powerful ring shaped nanomachines which participate in the degradation pathway of the protein quality control system, coupling the energy from ATP hydrolysis to threading substrate proteins (SP) through their narrow central pore. Repe
Externí odkaz:
https://doaj.org/article/f00b6315ed2447da90dd9c953c7d4af1
Publikováno v:
Reference Module in Life Sciences ISBN: 9780128096338
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e90e617f668f48bff4fe8f212b6699ab
https://doi.org/10.1016/b978-0-12-822563-9.00061-5
https://doi.org/10.1016/b978-0-12-822563-9.00061-5
Autor:
Yaa S. Amankwah, Preston Collins, Yasmeen Fleifil, Erin Unruh, Kevin J. Ruiz Márquez, Katherine Vitou, Andrea N. Kravats
Publikováno v:
Journal of Molecular Biology. 434:167762
Hsp90 and Hsp70 are highly conserved molecular chaperones that promote the proper folding and activation of substrate proteins that are often referred to as clients. The two chaperones functionally collaborate to fold specific clients in an ATP-depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be779a3b902683d32db6d9273c86a871
https://doi.org/10.1016/j.jmb.2022.167762
https://doi.org/10.1016/j.jmb.2022.167762
Autor:
Aidan M. Sturgill, Michael W. Crowder, Kundi Yang, Ben A. Shurina, Zishuo Cheng, Richard C. Page, Robert A. Bonomo, Walter Fast, Pei W. Thomas, Christopher R. Bethel, Huan Zhang, Steven H. Marshall, John-Paul Alao, Andrea N. Kravats, Caitlyn A. Thomas
Publikováno v:
Antimicrob Agents Chemother
Metallo-β-lactamases (MBLs) are a growing clinical threat because they inactivate nearly all β-lactam-containing antibiotics, and there are no clinically available inhibitors. A significant number of variants have already emerged for each MBL subfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15e989d702cb28a7d29900daa21b2392
https://doi.org/10.1128/aac.01714-20
https://doi.org/10.1128/aac.01714-20
Autor:
Riina Tehver, Andrea N. Kravats, Matthew P Grindle, Ben Carter, John Paul Alao, Katherine Connors
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 2200, p 2200 (2021)
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 2200, p 2200 (2021)
The 70 kDa and 90 kDa heat shock proteins Hsp70 and Hsp90 are two abundant and highly conserved ATP-dependent molecular chaperones that participate in the maintenance of cellular homeostasis. In Escherichia coli, Hsp90 (Hsp90Ec) and Hsp70 (DnaK) dire
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c2e5f447ff346a268a46ec3072f2a55
http://europepmc.org/articles/PMC7926864
http://europepmc.org/articles/PMC7926864
Autor:
Olivier Genest, Shannon M. Doyle, Erin E. Doody, Joel R. Hoskins, Sue Wickner, Andrea N. Kravats
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, 2017, 429 (6), pp.858-872. ⟨10.1016/j.jmb.2016.12.014⟩
Journal of Molecular Biology, Elsevier, 2017, 429 (6), pp.858-872. ⟨10.1016/j.jmb.2016.12.014⟩
Journal of Molecular Biology, 2017, 429 (6), pp.858-872. ⟨10.1016/j.jmb.2016.12.014⟩
Journal of Molecular Biology, Elsevier, 2017, 429 (6), pp.858-872. ⟨10.1016/j.jmb.2016.12.014⟩
International audience; Hsp90 is a widely conserved and ubiquitous molecular chaperone that participates in ATP-dependent protein remodeling in both eukaryotes and prokaryotes. It functions in conjunction with Hsp70 and the Hsp70 cochaperones, an Hsp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6499878587fca924f404ea5fe1b9a061
https://doi.org/10.1016/j.jmb.2016.12.014
https://doi.org/10.1016/j.jmb.2016.12.014
Autor:
Audrey L. Heffner, Joel R. Hoskins, Andrea N. Kravats, Srilakshmi Garikapati, Sue Wickner, Shannon M. Doyle
Publikováno v:
J Mol Biol
Members of the Hsp90 and Hsp70 families of molecular chaperones are imp\ortant for the maintenance of protein homeostasis and cellular recovery following environmental stresses, such as heat and oxidative stress. Moreover, the two chaperones can coll
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7193f56f8081238effbaa379b6ba84db
https://europepmc.org/articles/PMC6599576/
https://europepmc.org/articles/PMC6599576/