Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Marie E. Sweet"'
Autor:
Marie E Sweet, Xihui Zhang, Hediye Erdjument-Bromage, Vikas Dubey, Himanshu Khandelia, Thomas A Neubert, Bjørn P Pedersen, David L Stokes
Publikováno v:
eLife, Vol 9 (2020)
KdpFABC is an ATP-dependent K+ pump that ensures bacterial survival in K+-deficient environments. Whereas transcriptional activation of kdpFABC expression is well studied, a mechanism for down-regulation when K+ levels are restored has not been descr
Externí odkaz:
https://doaj.org/article/74c658c8288544649c85982d6776c5e1
Autor:
Casper Larsen, Michael Schlame, David L. Stokes, Marie E. Sweet, Bjørn Panyella Pedersen, Xihui Zhang
Publikováno v:
Proc Natl Acad Sci U S A
Sweet, M E, Larsen, C, Zhang, X, Schlame, M, Pedersen, B P & Stokes, D L 2021, ' Structural basis for potassium transport in prokaryotes by KdpFABC ', Proceedings of the National Academy of Sciences of the United States of America, vol. 118, no. 29, e2105195118 . https://doi.org/10.1073/pnas.2105195118
Sweet, M E, Larsen, C, Zhang, X, Schlame, M, Pedersen, B P & Stokes, D L 2021, ' Structural basis for potassium transport in prokaryotes by KdpFABC ', Proceedings of the National Academy of Sciences of the United States of America, vol. 118, no. 29, e2105195118 . https://doi.org/10.1073/pnas.2105195118
KdpFABC is an oligomeric K+ transport complex in prokaryotes that maintains ionic homeostasis under stress conditions. The complex comprises a channel-like subunit (KdpA) from the superfamily of K+ transporters and a pump-like subunit (KdpB) from the
Autor:
Xihui Zhang, Marie E. Sweet, David L. Stokes, Bjørn Panyella Pedersen, Michael Schlame, Casper Larsen
KdpFABC is an oligomeric K+ transport complex in prokaryotes that maintains ionic homeostasis under stress conditions. The complex comprises a channel-like subunit (KdpA) from the Superfamily of K+ Transporters and a pump-like subunit (KdpB) from the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d87b28c9f1f7f11dc95df6197a40941
https://doi.org/10.1101/2021.01.09.426067
https://doi.org/10.1101/2021.01.09.426067
Autor:
Marie E. Sweet, David L. Stokes, Vikas Dubey, Bjørn Panyella Pedersen, Hediye Erdjument-Bromage, Thomas A. Neubert, Himanshu Khandelia, Xihui Zhang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64da16f5840bce3aa45e2566745e9959
https://doi.org/10.7554/elife.55480.sa2
https://doi.org/10.7554/elife.55480.sa2
Autor:
Vikas Dubey, Thomas A. Neubert, Marie E. Sweet, Xihui Zhang, Himanshu Khandelia, Bjørn Panyella Pedersen, David L. Stokes, Hediye Erdjument-Bromage
Publikováno v:
eLife
Sweet, M E, Zhang, X, Erdjument-Bromage, H, Dubey, V, Khandelia, H, Neubert, T A, Pedersen, B P & Stokes, D L 2020, ' Serine phosphorylation regulates the P-type potassium pump KdpFABC ', eLife, vol. 9, e55480 . https://doi.org/10.7554/eLife.55480
eLife, Vol 9 (2020)
Sweet, M E, Zhang, X, Erdjument-Bromage, H, Dubey, V, Khandelia, H, Neubert, T A, Pedersen, B P & Stokes, D L 2020, ' Serine phosphorylation regulates the P-type potassium pump KdpFABC ', eLife, vol. 9, e55480 . https://doi.org/10.7554/ELIFE.55480
Sweet, M E, Zhang, X, Erdjument-Bromage, H, Dubey, V, Khandelia, H, Neubert, T A, Pedersen, B P & Stokes, D L 2020, ' Serine phosphorylation regulates the P-type potassium pump KdpFABC ', eLife, vol. 9, e55480 . https://doi.org/10.7554/eLife.55480
eLife, Vol 9 (2020)
Sweet, M E, Zhang, X, Erdjument-Bromage, H, Dubey, V, Khandelia, H, Neubert, T A, Pedersen, B P & Stokes, D L 2020, ' Serine phosphorylation regulates the P-type potassium pump KdpFABC ', eLife, vol. 9, e55480 . https://doi.org/10.7554/ELIFE.55480
KdpFABC is an ATP-dependent K+pump that ensures bacterial survival in K+-deficient environments. Whereas transcriptional activation of kdpFABC expression is well studied, a mechanism for down regulation when K+levels are restored has not been describ
Publikováno v:
Journal of the Korean Ceramic Society. 53:521-528
Kinetic Monte Carlo (KMC) and graph searches show that proton conduction limiting barriers and trajectories in BaZr 0.875 Y 0.125 O₃ are affected by the presence of other protons. At 1000 K, KMC limiting conduction barriers increase from 0.39 eV to
Publikováno v:
Biophysical Journal. 118:18a
Publikováno v:
Biophysical Journal. 114:189a