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Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. Additionally we are shipping Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Antibodies (218) and Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Kits (8) and many more products for this protein.
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Pin1 serves as a positive regulatory molecule of proplatelet formation of megakaryocytes by enhancing the function of phosphorylated tau.
Direct delivery of recombinant Pin1 via fibroin nanoparticle encapsulated cationic lipid complex successfully rescued osteoblast differentiation of pin-1 deficient cells.
Pin1 plays important role in the cell cycle progression and increase oval cells proliferation which may be crucial in chronic liver injury.
in vivo functional analyses of Pin1 in the GFAP (show GFAP Proteins)-tTA;TRE (show TREH Proteins)-SmoA1 mouse model of Hedgehog (show SHH Proteins)-driven medulloblastoma demonstrate that the loss of Pin1 impairs tumor development and dramatically increases survival.
Data, including data from studies conducted with knockout mice, suggest that Pin1 (prolyl isomerase 1) expression in pancreatic beta-cells is markedly elevated in obesity from diet high in fat/sucrose; Pin1 appears to be involved in proliferation of beta-cells and in regulation of secretion of insulin (show INS Proteins); Pin1 interacts with Sik2 (salt-inducible kinase 2 (show SIK2 Proteins)) to regulate calcium signaling.
Pin1 knockout in lupus-prone MRL lpr mi (show TLR7 Proteins)ce pre (show TLR9 Proteins)vents expres (show IRAK1 Proteins)sion o (show IRF7 Proteins)f lupus phenotype.
By interacting with PSD-95 (show DLG4 Proteins), Pin1 dampens PSD-95 (show DLG4 Proteins) ability to complex with NMDARs, thus negatively affecting NMDAR (show GRIN1 Proteins) signaling and spine morphology.
Oral administration of brown algae polyphenol, a Pin1 inhibitor, reduced fat buildup in mice.
The findings provide evidence for a putative novel role of PIN1 in the development of the nociceptive system and indicate phosphorylation-mediated conformational changes as a mechanism for regulating the PRRXL1 (show DRGX Proteins) role in the process.
Data show that peptidyl-prolyl isomerase (Pin1) inhibition inhibits high glucose (HG)-induced cardiac fibroblasts (CFs) proliferation and migration.
Pin1 is an essential factor regulating CPEB degradation
Pin1 binding is required for the inactivation of XeWee1B at M phase, presumably causing isomerization of the phospho-TP motif and thereby impairing the function of the Wee (show WEE1 Proteins)-box
High PIN1 expression is associated with stomach neoplasms.
Pin1 is a novel regulator of ATF1 (show AFT1 Proteins) at Thr184.
The dynamic basis for signal propagation in Pin1 N-terminal binding domain WW has been described.
The endoplasmic reticulum (ER) stress decreased Pin1 expression through p53 (show TP53 Proteins) activation, and this mechanism may be associated with ER stress-induced cell death. These data reported here support the importance of Pin1 as a potential target molecule mediating tumor development.
our data suggested that miR (show MLXIP Proteins)-874-3p plays a tumour suppressive role in HCC (show FAM126A Proteins) through down-regulation of PIN1.
in in silico gene expression analysis of human T-ALL samples we observed a significant correlation between Pin1 and Notch3 (show NOTCH3 Proteins) expression levels, which may further suggest a key role of the newly identified Notch3 (show NOTCH3 Proteins)-Pin1 axis in T-cell Acute Lymphoblastic Leukemia (T-ALL) aggressiveness and progression. Thus, combined suppression of Pin1 and Notch3 (show NOTCH3 Proteins) proteins may be exploited as an additional target therapy for T-ALL
The study demonstrates the oncogenic role of PIN1 in NPC (show NPC1 Proteins) tumorigenesis, and shows that its overexpression can enhance tumor cell growth via the upregulation of cyclinD1.
Pin1 expression was decreased remarkably in temporal lobe epilepsy patients compared to controls.
Data, including data from studies conducted with knockout mice, suggest that PIN1 (prolyl isomerase 1) expression in pancreatic beta-cells is markedly elevated in obesity from diet high in fat/sucrose; PIN1 appears to be involved in proliferation of beta-cells and in regulation of secretion of insulin (show INS Proteins); PIN1 interacts with Sik2 (salt-inducible kinase 2 (show SIK2 Proteins)) to regulate calcium signaling.
Knockdown of PIN1 potently blocks TLR-7 (show TLR7 Proteins)/TLR-9 (show TLR9 Proteins)/Pin1/IRAK-1 (show IRAK1 Proteins)/IRF-7 (show IRF7 Proteins) signaling in vitro.
The data provide the first evidence that Pin 1 expression in the granulosa cells but not the theca cells changes during follicular development, and that FSH (show BRD2 Proteins) stimulate the expression of the Pin 1 gene.
Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. This gene encodes one of the PPIases, which specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. The conformational regulation catalyzed by this PPIase has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, induction and maintenance of pluripotency, germ cell development, neuronal differentiation, and survival. This enzyme also plays a key role in the pathogenesis of Alzheimer's disease and many cancers. Multiple alternatively spliced transcript variants have been found for this gene.
peptidylprolyl cis/trans isomerase, NIMA-interacting 1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1, pseudogene 1
, prolyl isomerase Pin1 b
, prolyl isomerase Pin1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1 b
, protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1 a
, peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
, PPIase Pin1
, protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1
, rotamase Pin1
, peptidyl-prolyl cis-trans isomerase Pin1