Zobrazeno 1 - 10
of 201
pro vyhledávání: '"Eduardo Perozo"'
Autor:
Carus H. Y. Lau, Emelie Flood, Mark J. Hunter, Billy J. Williams-Noonan, Karen M. Corbett, Chai-Ann Ng, James C. Bouwer, Alastair G. Stewart, Eduardo Perozo, Toby W. Allen, Jamie I. Vandenberg
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract The fine tuning of biological electrical signaling is mediated by variations in the rates of opening and closing of gates that control ion flux through different ion channels. Human ether-a-go-go related gene (HERG) potassium channels have u
Externí odkaz:
https://doaj.org/article/972987d550f34a1a8904b0996298240b
Publikováno v:
eLife, Vol 12 (2023)
Prestin responds to transmembrane voltage fluctuations by changing its cross-sectional area, a process underlying the electromotility of outer hair cells and cochlear amplification. Prestin belongs to the SLC26 family of anion transporters yet is the
Externí odkaz:
https://doaj.org/article/171cf7e90fbe4af1886a08282c50d10e
Publikováno v:
eLife, Vol 12 (2023)
The force-from-lipids hypothesis of cellular mechanosensation posits that membrane channels open and close in response to changes in the physical state of the lipid bilayer, induced for example by lateral tension. Here, we investigate the molecular b
Externí odkaz:
https://doaj.org/article/301f810db5204175a4fe5cdde5f99558
Autor:
Ruiming Zhao, Hui Dai, Rodolfo J. Arias, Gerardo A. De Blas, Gerardo Orta, Martín A. Pavarotti, Rong Shen, Eduardo Perozo, Luis S. Mayorga, Alberto Darszon, Steve A. N. Goldstein
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The human voltage-gated proton channel (hHv1) maintains intracellular pH and membrane potential in sperm and neutrophils. Here, the authors show that albumin activates hHv1, by binding to the channel voltage sensor domains to enhance open probability
Externí odkaz:
https://doaj.org/article/c46008eddc1543f7b537b4b7900693ee
Publikováno v:
eLife, Vol 8 (2019)
Prokaryotic mechanosensitive (MS) channels open by sensing the physical state of the membrane. As such, lipid-protein interactions represent the defining molecular process underlying mechanotransduction. Here, we describe cryo-electron microscopy (cr
Externí odkaz:
https://doaj.org/article/9a4e7fb91ebf45fdaac1e110c653e491
Publikováno v:
eLife, Vol 8 (2019)
CorA, a divalent-selective channel in the metal ion transport superfamily, is the major Mg2+-influx pathway in prokaryotes. CorA structures in closed (Mg2+-bound), and open (Mg2+-free) states, together with functional data showed that Mg2+-influx inh
Externí odkaz:
https://doaj.org/article/318c500ab8c041b1b634c006e15cb60e
Autor:
Navid Bavi, D. Marien Cortes, Charles D. Cox, Paul R. Rohde, Weihong Liu, Joachim W. Deitmer, Omid Bavi, Pavel Strop, Adam P. Hill, Douglas Rees, Ben Corry, Eduardo Perozo, Boris Martinac
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
The activation of bacterial mechanosensitive channels is still not fully understood. Here, Bavi et al. show that the N-terminal helix of MscL dynamically couples membrane tension to channel gating, suggesting a conserved mechanism underlying the mech
Externí odkaz:
https://doaj.org/article/2a07ef9b726d4ac8a5718aab20eb0e33
Publikováno v:
eLife, Vol 6 (2017)
C-type inactivation in potassium channels helps fine-tune long-term channel activity through conformational changes at the selectivity filter. Here, through the use of cross-linked constitutively open constructs, we determined the structures of KcsA
Externí odkaz:
https://doaj.org/article/e5d031cc822e4e258af9fb7d50570508
Autor:
Satchal K. Erramilli, Pawel K. Dominik, Dawid Deneka, Piotr Tokarz, Sangwoo S. Kim, Bharat G. Reddy, Blazej M. Skrobek, Olivier Dalmas, Eduardo Perozo, Anthony A. Kossiakoff
Publikováno v:
bioRxiv
CorA, the primary magnesium ion channel in prokaryotes and archaea, is a prototypical homopentameric ion channel that undergoes ion-dependent conformational transitions. CorA adopts five-fold symmetric non-conductive states in the presence of high co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8d9aab3e6e66892dd26d639718c88d2
https://doi.org/10.1101/2023.05.07.539746
https://doi.org/10.1101/2023.05.07.539746