scispace - formally typeset
M

Michael D. Cahalan

Researcher at University of California, Irvine

Publications -  223
Citations -  28728

Michael D. Cahalan is an academic researcher from University of California, Irvine. The author has contributed to research in topics: T cell & Voltage-dependent calcium channel. The author has an hindex of 84, co-authored 218 publications receiving 27117 citations. Previous affiliations of Michael D. Cahalan include University of Washington & University of California, Berkeley.

Papers
More filters
Journal ArticleDOI

STIM1, an essential and conserved component of store-operated Ca2+ channel function

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

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

Two-photon imaging of lymphocyte motility and antigen response in intact lymph node.

TL;DR: Using two-photon laser microscopy to image the dynamic behavior of individual living lymphocytes deep within intact lymph nodes reveals lymphocyte behaviors that are fundamental to the initiation of the immune response.
Journal ArticleDOI

Genome-wide RNAi screen of Ca(2+) influx identifies genes that regulate Ca(2+) release-activated Ca(2+) channel activity.

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

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.