Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Anoosh Javaherian"'
Autor:
Chris S. Gandhi, Sarah Franklin, Antonios Pantazis, Anoosh Javaherian, Riccardo Olcese, Taleh N. Yusifov
Large-conductance voltage- and Ca^(2+)-dependent K^+ (BK, also known as MaxiK) channels are homo-tetrameric proteins with a broad expression pattern that potently regulate cellular excitability and Ca^(2+) homeostasis. Their activation results from t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8af88de49dcba64c2682ada024594807
https://resolver.caltech.edu/CaltechAUTHORS:20110620-134932876
https://resolver.caltech.edu/CaltechAUTHORS:20110620-134932876
Publikováno v:
Biophysical Journal. 100(3)
The large cytoplasmic C-terminal domain (CTD) of the human BK channel forms a gating ring structure composed by two tandem RCK domains serving as a signal transducer for intracellular Ca2+ and other ligands. However, the mechanism of the gating ring'
Publikováno v:
The Journal of general physiology, vol 136, iss 2
The Journal of General Physiology
The Journal of General Physiology
Large-conductance voltage- and Ca^(2+)-activated K^+ (BK_(Ca)) channels play a fundamental role in cellular function by integrating information from their voltage and Ca2+ sensors to control membrane potential and Ca^(2+) homeostasis. The molecular m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f99fb29e335cf6cb6b4606574736924
https://resolver.caltech.edu/CaltechAUTHORS:20100830-134310107
https://resolver.caltech.edu/CaltechAUTHORS:20100830-134310107
Publikováno v:
Biophysical Journal. 102:687a-688a
The human BK channel gating ring (GR) is the site of action of numerous signaling molecules such as Ca2+ and heme, which ultimately modulate pore open probability. However, the precise nature of these structural rearrangements remains elusive. Recent
Publikováno v:
Biophysical Journal. 102:688a
Phosphoinositides, in particular, phosphatidylinositol 4,5-bisphosphate (PIP2), are known regulators of numerous ion channels and have been implicated in cellular processes such modulation of the actin cytoskeleton, cell migration and vesicle traffic
Autor:
Shangwei Hou, Stefan H. Heinemann, Toshinori Hoshi, Anoosh Javaherian, Chris S. Gandhi, Taleh N. Yusifov, Riccardo Olcese
Publikováno v:
Biophysical Journal. 98:126a
Large-conductance voltage- and Ca2+-activated K+ channels (BKCa) are regulated by signaling molecules acting on two intracellular Regulator of K+ Conductance (RCK) domains which assemble into a gating ring superstructure. The discovery of heme as a B
Publikováno v:
Biophysical Journal. 96:481a
The large-conductance voltage- and Ca2+-activated K+ channels (BK) are activated by membrane depolarizations and intracellular Ca2+. Two consecutive intracellular RCK (Regulators of K+ Conductance) domains, RCK1 and RCK2, are responsible for calcium
Publikováno v:
Biophysical Journal. (3):481a
Recent studies suggest that Ca2+-dependent activation of the large-conductance voltage- and Ca2+-activated K+ (BK) channel is controlled by two RCK (Regulators of K+ Conductance) domains located in the C-terminus, encompassing high affinity Ca2+-site
Publikováno v:
Biophysical Journal. (3):581a
In BK channels, four RCK1 and four RCK2 domains assemble into a cytosolic ligand-sensing superstructure known as the gating ring. While electrophysiological data suggest that both RCK1 and RCK2 contain high affinity Ca2+-sensing sites, recent crystal