Ca(2+) homeostasis endoplasmic reticulum protein (CHERP) was first identified as an endoplasmic reticulum protein that regulates intracellular Ca(2+) mobilization in human cells, but recent proteomics data suggest an association between CHERP and spliceosomes.
Marchant et al., Minneapolis, United States. In J Biol Chem, 2013
Ca(2+) homeostasis endoplasmic reticulum protein (CHERP) is a ubiquitously expressed protein that has been proposed as a regulator of both major families of endoplasmic reticulum Ca(2+) channels, inositol 1,4,5-trisphosphate receptors (IP(3)Rs) and ryanodine receptors (RyRs), with resulting effects on mitotic cycling.
Grce et al., Zagreb, Croatia. In Gynecol Oncol, 2009
Sequencing of 11 DIPS amplicons revealed HPV DNA from 6 samples (54.5%) to be integrated in cellular genes (VMP1, PVRL1, CHERP, CEACAM5, AHR, MRF-2) and also 6 (54.5%) within the common fragile sites (CFS).
Miller-Karas et al., Santa Fe, United States. In Int J Emerg Ment Health, 2008
The article has two goals: First, to present a rationale for the use of a biologically-based model of mental health, the Trauma Resiliency Model (TRM), in post-disaster settings and, second, to present evaluation results of TRM training, mental health training focused on the biology of threat and fear with corresponding treatment skills provided as part of the China Earthquake Relief Project (CHERP).
Feinstein et al., Farmington, United States. In Biochem J, 2000
The cDNA predicts a 100 kDa protein, designated Ca(2+) homoeostasis endoplasmic reticulum protein (CHERP), with two putative transmembrane domains, multiple consensus phosphorylation sites, a polyglutamine tract of 12 repeats and regions of imperfect tryptophan and histadine octa- and nona-peptide repeats.