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The results indicated that S100A1 enhanced the ovarian cancer cell proliferation and migration.
found that S100B (show S100B Proteins) plays a crucial role in blocking the interaction site between RAGE (show AGER Proteins) V domain and S100A1. A cell proliferation assay WST (show EEF1A2 Proteins)-1 also supported our results. This report could potentially be useful for new protein development for cancer treatment
Study provides evidence that mir-363 and its target S100A1 are under the regulatory function of FOXD2-AS1 aggravating nasopharyngeal carcinoma carcinogenesis.
X-ray crystal structure of human calcium-bound S100A1 has been reported.
a molecular mechanism for the potential regulation of TRPM1 (show TRPM1 Proteins) by S100A1
Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 (show STIP1 Proteins) are key players in this pathway; the stoichiometry of S100A1/STIP1 (show STIP1 Proteins) interaction appears to be three S100A1 dimers plus one STIP1 (show STIP1 Proteins) monomer; each S100A1-STIP1 (show STIP1 Proteins)-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 (show STIP1 Proteins) = stress-induced-phosphoprotein 1 (show STIP1 Proteins)) [REVIEW]
Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (show STIP1 Proteins) (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 (show STIP1 Proteins) TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1.
Results identified amino acids motif in S100A1 for protein binding to 2-oxohistidine which appears to be an evolutionarily conserved capacity from bacteria to human.
a correlation between S100B (show S100B Proteins) + A1-positive Human Articular Chondrocytes in monolayer culture and their neochondrogenesis capacity in pellet culture, is reported.
CaM and S100A1 can concurrently bind to and functionally modulate RyR1 and RyR2, but this does not involve direct competition at the RyR CaM binding site.
identified S100A1, but not calmodulin (show KRIT1 Proteins) or other S100 proteins, as a potent molecular chaperone (show HSP90AA1 Proteins) and a new member of the Hsp70 (show HSP70 Proteins)/Hsp90 (show HSP90 Proteins) multichaperone complex (S100A1)
Results suggest that S100A1 can act as a linker between the calcium and redox signalling pathways.
beta-mercaptoethanol modification of apo (show C9orf3 Proteins)-S100A1 makes its structure more similar to that of holo-S100A1, so that it becomes much better adjusted for calcium coordination.
Data (including data from studies using knockout mice) suggest that S100A1 (S-100 calcium-binding protein (show GUCA1B Proteins) A1 (show BCL2A1 Proteins), alpha chain (show FCGRT Proteins)) is involved in protein kinase A- (RIIalpha and RIIbeta (show PRKAR2B Proteins))-dependent signaling resulting in nuclear redistribution/influx of HDAC4 (histone deacetylase 4 (show HDAC5 Proteins)) in skeletal muscle fibers.
S100A1-KO exhibited increased right ventricular (RV) weight and elevated RV pressure in the absence of altered left ventricular filling pressures, increase in wall thickness of muscularized pulmonary arteries and a reduction in microvascular perfusion.
S100A1 and S100B (show S100B Proteins) are dispensable for endochondral ossification during skeletal development.
S100A1 ablationalso reduced plaque associated and increased non-plaque associated PO4-Akt and PO4-GSK3beta staining.
Patients with acute myocardial infarction (MI) showed significantly increased S100A1 serum levels. Experimental MI in mice induced comparable S100A1 release. S100A1 signaling in cardiac fibroblasts occurs through endosomal TLR4 (show TLR4 Proteins)/MyD88 (show MYD88 Proteins).
hypoxia-induced MiR (show MLXIP Proteins)-138 is an essential mediator of EC dysfunction via its ability to target the 3'UTR of S100A1.
Report downregulation of S100A1 expression in critical limb ischemia impairs postischemic angiogenesis via compromised proangiogenic endothelial cell function and nitric oxide synthase regulation.
S100A1 and calmodulin bind to an overlapping domain on the ryanodine receptor (show RYR3 Proteins) type 1 to tune the Ca2 (show CA2 Proteins)+ release process, and thereby regulate skeletal muscle function. (Review)
The RyR1 (show RYR1 Proteins)-L3625D mutation removed both an early activating effect of S100A1 and calmodulin and delayed the suppression of RyR1 (show RYR1 Proteins) Ca2 (show CA2 Proteins)+ release, providing new insights into calmodulin and S100A1 regulation of skeletal muscle excitation-contraction coupling.
Data suggest that the absence of S100A1 suppresses physiological AP-induced Ca(2 (show CA2 Proteins)+) release flux, resulting in impaired contractile activation and force production in skeletal muscle.
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of this protein has been implicated in cardiomyopathies.
S-100 protein alpha chain
, S-100 protein subunit alpha
, S100 alpha
, S100 calcium-binding protein A1
, S100 protein, alpha polypeptide
, protein S100-A1
, S100 calcium binding protein A1
, Protein S100-A1