Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Ian Scott, Ramsey"'
Autor:
Gisela Rangel-Yescas, Cecilia Cervantes, Miguel A Cervantes-Rocha, Esteban Suárez-Delgado, Anastazia T Banaszak, Ernesto Maldonado, Ian Scott Ramsey, Tamara Rosenbaum, Leon D Islas
Publikováno v:
eLife, Vol 10 (2021)
Voltage-dependent proton-permeable channels are membrane proteins mediating a number of important physiological functions. Here we report the presence of a gene encoding Hv1 voltage-dependent, proton-permeable channels in two species of reef-building
Externí odkaz:
https://doaj.org/article/d43519a4b7d44809a375b212c22eea6b
Publikováno v:
eLife, Vol 5 (2016)
The Hv1 proton channel is evidently unique among voltage sensor domain proteins in mediating an intrinsic ‘aqueous’ H+ conductance (GAQ). Mutation of a highly conserved ‘gating charge’ residue in the S4 helix (R1H) confers a resting-state H+
Externí odkaz:
https://doaj.org/article/10366edcbbec4e47ae3c07806e5c5983
Autor:
León D. Islas, Ernesto Maldonado, Miguel A Cervantes-Rocha, Tamara Rosenbaum, Cecilia Cervantes, Anastazia T. Banaszak, Esteban Suárez-Delgado, Gisela E. Rangel-Yescas, Ian Scott Ramsey
Publikováno v:
eLife, Vol 10 (2021)
Voltage-dependent proton-permeable channels are membrane proteins mediating a number of important physiological functions. Here we report the presence of a gene encoding Hv1 voltage-dependent, proton-permeable channels in two species of reef-building
Autor:
Esteban Suárez-Delgado, Cecilia Cervantes, Anastazia T. Banaszak, León D. Islas, Tamara Rosenbaum, Gisela E. Rangel-Yescas, Ian Scott Ramsey, Ernesto Maldonado, Miguel A Cervantes-Rocha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea472c982d7efecb10f82be4a50b7fde
https://doi.org/10.7554/elife.69248.sa2
https://doi.org/10.7554/elife.69248.sa2
Autor:
Victor De La Rosa, Ian Scott Ramsey
Publikováno v:
Biophysical Journal. 114:2844-2854
The Hv1 proton channel shares striking structural homology with fourth transmembrane helical segment-type voltage-sensor (VS) domains but manifests distinctive functional properties, including a proton-selective “aqueous” conductance and alloster
Publikováno v:
The Journal of General Physiology
Hv1 proteins form a voltage-gated proton channel that is inhibited by extracellular Zn2+. De La Rosa et al find that extracellular Zn2+ is octahedrally coordinated by specific protein atoms and that Zn2+ occupancy modulates voltage sensor activation