S
Shenyuan L. Zhang
Researcher at University of California, Irvine
Publications - 16
Citations - 6270
Shenyuan L. Zhang is an academic researcher from University of California, Irvine. The author has contributed to research in topics: ORAI1 & STIM2. The author has an hindex of 15, co-authored 16 publications receiving 6002 citations. Previous affiliations of Shenyuan L. Zhang include University of California, Berkeley & Texas A&M Health Science Center.
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Journal ArticleDOI
STIM1, an essential and conserved component of store-operated Ca2+ channel function
Jack Roos,Paul J. Digregorio,Andriy V. Yeromin,Kari Lynn Ohlsen,Maria I. Lioudyno,Shenyuan L. Zhang,Olga Safrina,J. Ashot Kozak,Steven L. Wagner,Michael D. Cahalan,Gonul Velicelebi,Kenneth A. Stauderman +11 more
TL;DR: It is proposed that STIM1, a ubiquitously expressed protein that is conserved from Drosophila to mammalian cells, plays an essential role in SOC influx and may be a common component of SOC and CRAC channels.
Journal ArticleDOI
STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane
Shenyuan L. Zhang,Ying Yu,Jack Roos,J. Ashot Kozak,Thomas J. Deerinck,Mark H. Ellisman,Kenneth A. Stauderman,Michael D. Cahalan +7 more
TL;DR: It is proposed that STIM1 functions as the missing link between Ca2+ store depletion and SOC influx, serving as aCa2+ sensor that translocates upon store depletion to the plasma membrane to activate CRAC channels.
Journal ArticleDOI
Genome-wide RNAi screen of Ca(2+) influx identifies genes that regulate Ca(2+) release-activated Ca(2+) channel activity.
Shenyuan L. Zhang,Andriy V. Yeromin,Xiang Zhang,Ying Yu,Olga Safrina,Aubin Penna,Jack Roos,Kenneth A. Stauderman,Michael D. Cahalan +8 more
TL;DR: Using an unbiased genome-wide RNA interference screen in Drosophila S2 cells, 75 hits are identified that strongly inhibited Ca(2+) influx upon store emptying by thapsigargin, including Stim and olf186-F, a member of a highly conserved family of four-transmembrane spanning proteins with homologs from Caenorhabditis elegans to human.
Journal ArticleDOI
Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai
Andriy V. Yeromin,Shenyuan L. Zhang,Shenyuan L. Zhang,Weihua Jiang,Weihua Jiang,Ying Yu,Ying Yu,Olga Safrina,Olga Safrina,Michael D. Cahalan,Michael D. Cahalan +10 more
TL;DR: By site-directed mutagenesis, it is shown that a point mutation from glutamate to aspartate at position 180 in the conserved S1–S2 loop of Orai transforms the ion selectivity properties of CRAC current from being Ca2+-selective with inward rectification to being selective for monovalent cations and outwardly rectifying.
Journal ArticleDOI
The CRAC channel consists of a tetramer formed by Stim-induced dimerization of Orai dimers
Aubin Penna,Angelo Demuro,Andriy V. Yeromin,Shenyuan L. Zhang,Olga Safrina,Ian Parker,Michael D. Cahalan +6 more
TL;DR: It is shown that Orai is predominantly a dimer in the plasma membrane under resting conditions, which represents a new mechanism in which assembly and activation of the functional ion channel are mediated by the same triggering molecule.