The most recent information on PIN1 is here. Click here for the function of PIN1. Edit this page in Wiki Genes - PIN1 or see Wiki Gene. The linchpin? Pin1 meets p73. Paper-10299849. Calif. hospital nixes DOD bed request. Paper-3891413. PIN 1 was the most common grade, PIN 3 the least. Paper-7898191. PIN1 was shown to be overexpressed in more than 50% of HCC. Paper-10255803. We have examined the interaction between Pin1 and Cdc25 in detail. Paper-1364274. These data indicate Pin1 is a key mediator of GM-CSF production. Paper-11524493. RESULTS: Excepting clozapine and DOD 647, all drugs induced dystonia. Paper-1955909. Expression of Pin1 and Ki67 in cervical cancer and their significance. Paper-12109749. The results showed that Pin1 directly regulated cyclin D1 levels. Paper-12153195. Pin1 promoter polymorphisms in hepatocellular carcinoma patients. Paper-13292139. An alternative model for Pin1 regulation of APP processing is also proposed. Paper-12353862. Pin1 acts catalytically to promote a conformational change in Cdc25. Paper-8982525. Pin1 modulates the structure and function of human RNA polymerase II. Paper-10157291. We present evidence that Pin1 modulates interactions between SRC-3 and CBP/p300. Paper-11103946. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Paper-9224584. This interaction requires the WW domain of Pin1 and SMRT phosphorylation. Paper-13024200. Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1. Paper-12514419. The role of PIN1 in beta-catenin upregulation in HCC was investigated. Paper-10255803. We consider two molecules, the 27th immunoglobulin domain of titin and protein PIN1. Paper-13241235. Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1. Paper-12048950. Cdk2 and Pin1 negatively regulate the transcriptional corepressor SMRT. Paper-13024200. Vibrational energies and the infrared spectra for DOD and HOD/DOH are also presented. Paper-12263509. Overexpression of Pin1 increases cellular cyclin D1 protein and activates its promoter. Paper-9008575. These results suggest a possible role for Pin1 in the regulation of NFAT in T cells. Paper-8963868. Phosphorylated APP is a Pin1 substrate, which binds to its phosphor-Thr668-Pro motif. Paper-12435164. Pin1 contributes to cervical tumorigenesis by regulating cyclin D1 expression. Paper-12153195. We report that Pin1 is overexpressed in OSCC and its level correlates with cyclin D1 level. Paper-9751019. On transfection study, the mutant Pin1 showed an increased expression of beta-catenin. Paper-12174882. Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation. Paper-9915551. We found that Pin1 is required for efficient loading of p53 on target promoters upon stress. Paper-12566525. Are RB proteins a potential substrate of Pin1 in the regulation of the cell cycle? Paper-11099145. We also showed that in neuronal cells, Pin1 upregulates the expression of cyclin D1. Paper-9297470. Pin1 thus plays a significant role in regulating RNAP II CTD structure and function. Paper-10157291. The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9. Paper-9073217. We also show that RNA polymerase II large subunit interacts with Pin1 in HeLa cells. Paper-2007176. In addition, Pin1 and SRC-3 activate nuclear-receptor-regulated transcription synergistically. Paper-11103946. Pin1 is also a critical regulator of the tumor suppressor p53 during DNA damage response. Paper-10015486. Manipulation of Pin1 levels affects the stability of beta-catenin in vitro. Paper-9058220. After a median follow-up of 20 months 14 (38%) patients are NED, 10 (27%) are AWD and 13 (35%) DOD. Paper-11995164. Interestingly, a significant correlation was found between Pin1 and beta-catenin protein expression. Paper-10752086. In cervical cancer, the overexpression of Pin1 was positively correlated with that of Ki67 (P < 0.05). Paper-12109749. Here, we show that Pin1 modulates oxidative stress- induced NF-H phosphorylation. Paper-13005692. Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. Paper-8963868. These are the E2F family, the ASPP family, Y-box-binding protein YB1, and the prolyl isomerase Pin1. Paper-12108799. Pin1 expression was observed in PTC by immunostaining and was confirmed by reverse transcriptase-PCR. Paper-10224596. This is the first report of Pin1 overexpression in clinical samples of non-small cell lung cancer (NSCLC). Paper-13149429. There was no mutation of beta-catenin gene in tissues with high PIN1 expression level (chi2=58.12, P<0.05). Paper-12477969. Together, our results suggest that KRMP1 is a mitotic target regulated by Pin1 and vice versa. Paper-8960481. IGF-1 induces Pin1 expression in promoting cell cycle S-phase entry. Paper-9354285. Pin1 overexpression in colorectal cancer and its correlation with aberrant beta-catenin expression. Paper-10752086. Conversely, Pin1 may restore the tubulin polymerization function of these hyperphosphorylated Tau. Paper-9297470. Pin1 and Pin2 RNAs were detected early and transiently in both compatible and incompatible interactions. Paper-9931027. Pin1 cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. Paper-9892679. Pin1 cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. Paper-9751019. In this report, we found that Pin1 could interact with Nek6, one of the human NIMA-related kinases (Neks). Paper-11388326. Moreover, recent studies demonstrate that APP is a target for Pin1 and thus, in Abeta production. Paper-12204648. Pin1 stabilizes Emi1 during G2 phase by preventing its association with SCF(betatrcp). Paper-12392717. Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1. Paper-8960481. We show that Pin1 requires these phosphorylation events to act negatively on FOXO4 transcriptional activity. Paper-12947886. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Paper-9155675. These results demonstrate a new role of Pin1 in regulating p53 function during DNA damage. Paper-9282066. Finally, cell death induced by ectopic Pin1 was largely blocked by expression of dominant negative c-Jun. Paper-12901982. Pin1 is a peptidyl-prolyl cis/trans isomerase ( PPIase) essential for cell cycle regulation. Paper-9777423. The proliferation index was significantly higher in PIN 3 and cancers as compared to BPH, PIN 1, and PIN 2 tissues. Paper-6873188. Pin1 promotes cyclin D1 over-expression directly or through the stabilization of beta-catenin. Paper-12070340. The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability. Paper-10825870. The induction of Pin1 by IGF-1 is mediated via the phosphatidylinositol 3-kinase as well as the MAP kinase pathways. Paper-9354285. Pin1 promotes cell death in NGF-dependent neurons through a mechanism requiring c-Jun activity. Paper-12901982. Forward stepwise discriminant analysis showed similarities between NH and PIN 1 and between PIN 2 and carcinoma. Paper-6655420. Pin1 is overexpressed in oral squamous cell carcinoma and its levels correlate with cyclin D1 overexpression. Paper-9751019. However, the analysis of the relationship between Pin1 and other cyclin genes has not been demonstrated in human OSCC. Paper-9892679. Human immunodeficiency virus type 1 replication and regulation of APOBEC3G by peptidyl prolyl isomerase Pin1. Paper-12954102. We show that the peptidyl-prolyl isomerase Pin1 interacts with SMRT both in vitro and in mammalian cells. Paper-13024200. At a median follow-up of 27 months, outcome in this high-risk patient population was 22 NED, 3 AWD, 12 DOD, 2 DOC. Paper-10115777. Pin1 regulates SMRT protein stability, thereby affecting SMRT-dependent transcriptional repression. Paper-13024200. The peptidyl-prolyl isomerase Pin1 is strikingly overexpressed in human cancers and is a novel regulator of beta-catenin. Paper-12174882. The prolyl isomerase Pin1 orchestrates p53 acetylation and dissociation from the apoptosis inhibitor iASPP. Paper-12566525. Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage. Paper-10775381. Recently we have devised a novel methodology in which exogenous Pin1 is used as a TEM probe for its target proteins. Paper-8674634. These results suggest a novel mechanism by which Pin1 promotes cell death involving activation of c-Jun. Paper-12901982. Among 29 pair cases of HCC and non-carcinoma tissues, the expression of PIN1 gene was detected by immunochemical staining. Paper-12477969. The effect of Pin1 on beta-catenin expression was further examined in wild- and mutant-type Pin1-transfected HEK 293T cells. Paper-12174882. To investigate its potential oncogenicity, we over-expressed PIN1 in a non-transformed human liver cell line MIHA. Paper-12197033. Furthermore, the WW domains of human YAP and Pin1 were demonstrated to have a similar transcription-promoting activity. Paper-1860099. Furthermore, we found that Cyclin D1 expression and RB phosphorylation are dramatically decreased in Pin1(-/-) MEF cells. Paper-9354285. RESULTS: Normal colonic epithelium either failed to express or showed focal and weak expression of Pin1 and beta-catenin. Paper-10752086. Interestingly, Pin1 acts on FOXO through stimulation of the activity of the deubiquitinating enzyme HAUSP/ USP7. Paper-12947886. The NFAT- Pin1 interaction is mediated through the WW domain of Pin1 and the serine-proline-rich domains of NFAT. Paper-8963868. PIN1 gene overexpression and beta-catenin gene mutation/expression in hepatocellular carcinoma and their significance. Paper-12477969. In conclusion, Pin1 expression is correlated with cyclinD1 expression and may be a useful prognostic factor for esophageal SCC. Paper-12138331. Furthermore, PIN1 is an E2F target gene essential for the Neu/Ras-induced transformation of mammary epithelial cells. Paper-10015486. The PIN1L cDNA is 89% identical at the nucleotide level to the PIN1 transcript, but contains a shift in the reading frame. Paper-1228591. The expressions of Pin1 and cyclinD1 were examined immunohistochemically in surgical specimens from 119 esophageal SCC patients. Paper-12138331. Pin1 overexpression enhanced SRC-3 cellular turnover, and depletion of Pin1 stabilized SRC-3. Paper-11103946. High Pin1 expression was also correlated with the over-expressions of both beta-catenin (P=0.0225) and cyclin D1 (P=0.0137). Paper-12070340. Consequently, Pin1 stimulates the DNA- binding activity and transactivation function of p53. Paper-9224584. The human parvulin homologue Pin1 is a mitotic regulator essential for the G2/M transition of the eukaryotic cell cycle. Paper-8325326. We show that Pin1 binds to Emi1 and prevents its association with betatrcp in an isomerization-dependent pathway. Paper-12392717. Furthermore, the interaction of Pin1 with p53 is dependent on the phosphorylation that is induced by DNA damage. Paper-9224584. Furthermore, Pin1 binds c-Jun that is phosphorylated on Ser63/73-Pro motifs by activated JNK or oncogenic Ras. Paper-9008575. Pin1 was overexpressed in 5 of 6 esophageal SCC-derived cell lines compared with immortalized esophageal keratinocytes. Paper-12138331. Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients. Paper-11388326. Regulation of the transcriptional activity of c- Fos by ERK. A novel role for the prolyl isomerase PIN1. Paper-10974435. Overexpression of Pin1 and beta-catenin protein was found in 23 (18.54%) and 50 (40.3%) of 124 colorectal cancers, respectively. Paper-10752086. However, an inhibitor of Pin1, 5-hydroxy-1,4-naphthoquinone ( juglone), blocked transcription by RNA polymerase II. Paper-8733403. The pThr site of hNIFK recognized by Ki67 FHA is pThr234-Pro235, a motif also recognized by the proline isomerase Pin1. Paper-10209624. Thus, Pin1 likely acts as a general regulator of mitotic proteins that have been phosphorylated by Cdc2 and other mitotic kinases. Paper-1364274. A Suppressive Role of the Prolyl Isomerase Pin1 in Cellular Apoptosis Mediated by the Death- associated Protein Daxx. Paper-12637285. A recent study shows that a peptidyl-prolyl isomerase, Pin1, specifically regulates the degradation of amyloid precursor protein ( APP). Paper-12353862. The human PIN1 peptidyl-prolyl cis/trans isomerase gene maps to human chromosome 19p13 and the closely related PIN1L gene to 1p31. Paper-1228591. Furthermore, Pin1 regulates the stability of p53 and its transcriptional activity toward the p21 promoter. Paper-9282066. Here we describe the identification and characterization of the binding between BNIP-H and Pin1, a peptidyl-prolyl cis/trans isomerase. Paper-12884140. A further level of control has now been unveiled by showing that also the p53 sibling p73 requires Pin1 for its apoptotic activity. Paper-11429314. We show here that the peptidyl prolyl cis-trans isomerase Pin1 interacts specifically with the phosphorylated form of NFAT. Paper-8963868. CTPS1 interacted with a GST- peptidyl prolyl isomerase, Pin1 fusion ( GST- Pin1) in a Ser 575 (S575) phosphorylation-dependent manner. Paper-12870315. Consistent with these observations, Pin1 overexpression enhances the protein half-life and insolubility of alpha-synuclein. Paper-10844724. Recently, a role for Pin1 has emerged also in the DNA damage response, through modulation of p53 functions upon genotoxic stress. Paper-11429314. High expression levels of Pin1 correlated with high levels of p53 or MDM2 protein, but did not show a correlation with cyclin D1. Paper-13149429. Here, we investigated the role of Pin1 in association with cyclinD1 in esophageal SCC progression and its clinicopathological significance. Paper-12138331. Here we report that Pin1 is strikingly overexpressed in human breast cancers, and that its levels correlate with cyclin D1 levels in tumors. Paper-9008575. The degradation of cyclin E is a consequence of its phosphorylation and subsequent isomerization by the peptidyl-prolyl isomerase Pin1. Paper-13493712. Therefore, oxidative inactivation of ENO1, GLUL and PIN1 may alter these cellular processes and lead to the development of AD from MCI. Paper-11830705. Here we show that the prolyl isomerase Pin1 functions as a positive regulator of neuronal death through a c-Jun-dependent mechanism. Paper-12901982. We examined the relationships between Pin1 expression and clinicopathological factors, prognosis, and beta-catenin/ cyclin D1 expression. Paper-12070340. Prolyl-isomerase Pin1 accumulates in lewy bodies of parkinson disease and facilitates formation of alpha-synuclein inclusions. Paper-10844724. These results indicate that nerve growth factor may stimulate the interaction of BNIP-H with Pin1 by releasing its intramolecular inhibition. Paper-12884140. Instead, phosphorylated rab4 is in a complex with the peptidyl-prolyl isomerase Pin1 during mitosis, but not during interphase. Paper-8438340. Our results establish Che-1 as a new Pin1 and HDM2 target and confirm its important role in the cellular response to DNA damage. Paper-13321927. Flotillin-1-positive granular bodies were also found in neurones containing Pin1-positive vesicles but were not colocalized with them. Paper-10084834. In tumors bearing wild-type p53, expression of Pin1 and iASPP are inversely correlated, supporting the clinical relevance of these interactions. Paper-12566525. Thus, Pin1 is up-regulated in human tumors and cooperates with Ras signaling in increasing c-Jun transcriptional activity towards cyclin D1. Paper-9008575. The differential display screen revealed that Pin1 increases the transcription of several target genes, including cyclin D1 and c-myc genes. Paper-9751019. But Pin1 also modulates the activity of numerous other proteins, and a strong candidate for such regulation has been RNA polymerase II (RNAP II). Paper-10502526. Here we demonstrate that PIN1 expression is mediated by the transcription factor E2F and enhanced by c-Neu and Ha-Ras via E2F. Paper-9504863. Here, we identify Pin1 as a new regulator of Emi1 that induces Emi1 stabilization by preventing its association with SCF(betatrcp). Paper-12392717. Pin1 immunoreactivity appeared as cytoplasmic granules affecting hippocampal subfields to a different extent (CA2>subiculum>CA1>CA3/ CA4). Paper-9173310. Importantly, our findings elucidate the selection for mutations in the Pin1 target Thr81/Pro82 motif within the PPR of p53 in human cancer. Paper-10775381. This study aimed to determine whether Pin1 plays a role in colorectal tumorigenesis through the upregulation of beta-catenin and cyclin D1. Paper-12070340. Pin1 is a peptidyl-prolyl isomerase consisting of a WW domain and a catalytic isomerase ( PPIase) domain connected by a flexible linker. Paper-13153441. Analysis of Pin1 activity in AD brain and separately as oxidized pure Pin1 demonstrated that oxidation of Pin1 led to loss of activity. Paper-12110153. We have previously reported that Pin1 is overexpressed in oral squamous cell carcinoma (OSCC) and its level correlates with Cyclin D1 expression. Paper-9892679. Aberrant expression of beta-catenin, Pin1 and cylin D1 in salivary adenoid cystic carcinoma: relation to tumor proliferation and metastasis. Paper-12153197. Furthermore, expression of Pin1 disrupted the BNIP-H/ glutaminase complex formation in PC12 cells under nerve growth factor-stimulation. Paper-12884140. Pin1 was overexpressed in 51 cases of SACC (78%), and high levels of Pin1 expression correlated with cyclin D1 positive expression (p = 0.02). Paper-12153197. The peptidyl prolyl cis-trans isomerase Pin1 and the Inhibitor of Apoptosis Protein ( IAP) Survivin are two major proteins involved in cancer. Paper-12495575. Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. Paper-9008575. We further found that the expression levels of Pin1 inversely correlate with the degree of Daxx nuclear accumulation in human glioblastoma tissues. Paper-12637285. Reintroducing a recombinant adenovirus encoding Pin1 into Pin1(-/-) MEF cells restores the expression of cyclin D1 and RB phosphorylation. Paper-9354285. Moreover, Pin1 directly bound to cyclin D1 phosphorylated on Thr-286-Pro increased cyclin D1 in the nucleus and stabilized cyclin D1. Paper-9155675. In addition, Pin1 is recruited to chromatin by p53 and stimulates binding of the p300 acetyltransferase and consequent p53 acetylation. Paper-12566525. Pin1 expression was correlated with poor prognosis in esophageal SCC patients (P=0.0044), and found to be an independent prognostic factor (P=0.0277). Paper-12138331. Our results provide genetic evidence for an essential role of Pin1 in maintaining cell proliferation and regulating cyclin D1 function. Paper-9155675. The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils. Paper-11524493. The Pin1 WW domain functioned as a phosphoserine- or phosphothreonine-binding module, with properties similar to those of SRC homology 2 domains. Paper-1751743. Pin1 functions downstream of HER2, positioning it as an important modulator of the crosstalk between ER and growth factor signaling. Paper-13713086. Cyclin D1 overexpression in thyroid tumours from a radio-contaminated area and its correlation with Pin1 and aberrant beta-catenin expression. Paper-10224596. Specifically, we compare Pin1 side-chain motions in the presence and absence of a known phosphopeptide substrate derived from the mitotic phosphatase Cdc25. Paper-13153441. While CyP and FKBP inhibitors have been explored fairly thoroughly, inhibitors of the relatively new Pin1 cell cycle regulator are in their infancy. Paper-11326013. A recent paper shows that the peptidyl-prolyl isomerase Pin1 conformationally alters p73, promoting its acetylation by p300 in a c-Abl dependent manner. Paper-10299849. Pin1 has been identified as the molecular partner of tau and amyloid precursor protein ( APP), the key factors of Alzheimer's disease (AD). Paper-12726339. Given previous findings with p53, Pin1 may represent a common mediator linking proapoptotic cooperative activity of the p53 family members. Paper-10299849. Pin1 is enriched at the mitochondrial membrane in neurons, where it forms a physical complex with the neuron-specific JNK scaffold protein JIP3. Paper-11339708. Given the crucial roles of Ras signaling and cyclin D1 overexpression in oncogenesis, our results suggest that overexpression of Pin1 may promote tumor growth. Paper-9008575. Drug-induced Pin1 accumulation could probably facilitate this transition and in parallel contribute to apoptosis via the p53/ p73-dependent mechanism. Paper-13003987. Designed peptidyl-prolyl isomerase ( PPIase) inhibitors of Pin1, cyclophilin (CyP), and FK506 binding protein ( FKBP) are reviewed. Paper-11326013. Activation of JNK signaling induces the dissociation of Pin1 from JIP3 and concomitantly promotes Pin1 binding to phosphorylated BIMEL. Paper-11339708. The prolyl isomerase Pin1 has a central role in transducing phosphorylation of p53 into conformational changes that affect p53 stability and function. Paper-12566525. Overexpression of KRMP1 caused COS-7 cells to arrest at G(2)-M, and co-expression of Pin1 reversed this effect, indicating their physiological interaction. Paper-8960481. AIM: To investigate clinical significance of Pin1 and beta-catenin expression in colorectal cancers and to demonstrate the relationship of their expression. Paper-10752086. Importantly, these early transformed properties are effectively suppressed by Pin1 deletion, which can be fully rescued by overexpression of cyclin D1. Paper-10515208. We demonstrated the association between the intracellular form of Notch1 (NIC) and Pin1 by analyzing Pin1/ p53 double-knockout mice. Paper-12726339. All cases with PIN1 overexpression also showed beta-catenin accumulation, with 68% of cases showing concomitant beta-catenin and cyclin D1 accumulation. Paper-10255803. Cyclin D1 levels were significantly reduced in many tissues in Pin1-deficient mice, including retina and breast epithelial cells from pregnant mice. Paper-9155675. The interaction between FKBP12 and AICD might hint at a possible role FKBP12 plays, probably in a fashion similar to Pin1, in the amyloidogenesis of APP. Paper-12262935. The cases of PIN were subdivided into PIN 1 and PIN 2 based on the degree of proliferation and the anaplasia of the secretory cells lining the ducts and acini. Paper-6655420. Expression status of Pin1 and cyclins in oral squamous cell carcinoma: Pin1 correlates with Cyclin D1 mRNA expression and clinical significance of cyclins. Paper-9892679. Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage. Paper-9282066. CONCLUSIONS: These results suggest that Pin1 plays an important role in colorectal tumorigenesis, presumably by increasing beta-catenin and cyclin D1 expressions. Paper-12070340. Many Pin1 substrates are antigens of the phosphodependent monoclonal antibody MPM-2, which reacts with a subset of proteins phosphorylated at the G2/M transition. Paper-10288329. Accordingly, tumor-associated mutations at Pin1- binding residues within the p53 proline-rich domain hamper acetylation of p53 by p300. Paper-12566525. However, the relationships between Pin1 expression and clinicopathologic features in patients with esophageal squamous cell carcinoma ( SCC) have not been explored. Paper-12138331. Thus the enhanced resistance to cell death exhibited by phosphorylation defective mutant Bcl2 might be attributed to its inability to associate with Pin1. Paper-9603389. SMRT phosphorylation at multiple sites is required for Pin1 interaction, and these sites can be phosphorylated by Cdk2, which interacts with SMRT. Paper-13024200. In vivo, dominant-negative (DN) Pin1 and Pin1 small interfering RNA inhibited epidermal growth factor- induced NF-H phosphorylation. Paper-13005692. In addition, Pin1, a member of another PPIase family, has been suggested to be involved in the amyloidogenic APP processing and Abeta production. Paper-12262935. Consistent with this result, increased expression of Pin1 in transfected LNCaP PCa cells strongly accelerated tumor growth in vivo in immunodeficient mice. Paper-10827857. The WW domain of Pin1 acts as a phosphoserine/ threonine-binding module binding a defined subset of mitosis-specific phosphoproteins, such as Cdc25 and tau. Paper-11594352. Our study unravels the pathway by which Pin1 activates p53 in response to DNA damage and explains how Pin1 protects p53 from Mdm2. Paper-10775381. Pin1 catalytically modifies the conformation of Cdc25 at stoichiometries less than 0.0005, and mutants of Pin1 in the prolyl isomerase domain are not active. Paper-8982525. The protease-coupled Pin1 assay showed that all three compounds inhibited the Pin1 peptidyl-prolyl isomerase ( PPIase) enzymatic activity. Paper-10848025. The H(2)O(2) and heat shock induced perikaryal phospho- NF-H accumulations, and neuronal apoptosis was rescued by inhibition of Pin1 in cortical neurons. Paper-13005692. So it was postulated that the increase of PIN1 gene expression could promote hepatocellular carcinogenesis via a way different from beta-catenin gene mutation. Paper-12477969. Pin1 regulated the association of the AU-rich element- binding proteins AUF1 and hnRNP C with GM-CSF mRNA, accelerating or slowing decay, respectively. Paper-11524493. Peptidyl-prolyl isomerase 1 ( Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 ( SRC-3/ AIB1). Paper-11103946. Knockdown of Pin1 by transfected Pin1 short interference RNA and DN-Pin1 rescues the effect of stress- induced NF-H phosphorylation. Paper-13005692. We report that Pin1 mRNA correlates with Cyclin D1 mRNA expression and the expression of many cyclin genes is associated with lymph node metastasis in OSCC. Paper-9892679. The PIN1At fold could be superimposed on that of the catalytic domain of hPIN1 and had a 19 residue flexible loop located between strand beta1 and helix alpha1. Paper-9493769. Moreover, in Pin1 knockout mice, mammary epithelial cells fail to undergo massive proliferation during pregnancy, as is the case in cyclin D1 null mice. Paper-9504863. Furthermore, beta-catenin levels are decreased in Pin1-deficient mice but are increased and correlated with Pin1 overexpression in human breast cancer. Paper-9058220. The protective effect of Pin1 knockdown was significantly greater than that caused by loss of Bim and nearly identical to that caused by a dominant negative form of c-Jun. Paper-12901982. The Pin1- mediated p53 activation requires the WW domain, a phosphorylated Ser/Thr-Pro motif interaction module, and the isomerase activity of Pin1. Paper-9224584. A number of previous studies have shown that Pin1 is co-localized with phosphorylated tau in AD brain, and shows an inverse relationship to the expression of tau. Paper-12204648. We propose that S- and M-phase entries are mediated by the accumulation of cyclin A and cyclin B through a Pin1-dependent stabilization of Emi1 during G2. Paper-12392717. Accordingly, Pin 1 was shown to associate with Btk through binding to Ser-21 and -115, respectively, both of which lie in a classical Pin1-binding pocket. Paper-12048950. As a result, p53 and p21 barely increased after DNA damage in Pin1 knock-out embryonic fibroblasts or in neoplastic cells depleted of Pin1. Paper-9282066. After phosphorylation of p53 at Ser46 triggered by cytotoxic stimuli, Pin1 also mediates p53's dissociation from the apoptosis inhibitor iASPP, promoting cell death. Paper-12566525. A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1. Paper-2007176. The negative regulatory effect of Pin1 was observed both in cell lines and in Pin(-/-) mice and was found to be dependent on a functionally intact Btk. Paper-12048950. PCa patients assigned to the high Pin1 score group demonstrated PSA relapse more frequently than those assigned to the low Pin1 score group (p<0.0001). Paper-11821820. Pin1 may thus regulate transcriptional and post-transcriptional events by catalyzing phosphorylation-dependent conformational changes of the large RNA polymerase II subunit. Paper-2007176. Interestingly, many of these Pin1-deficient phenotypes such as retinal hypoplasia and mammary gland impairment are also the characteristic of cyclin D1-deficient mice. Paper-9155675. We have previously shown that monoubiquitination is involved in controlling nuclear translocation in response to cellular stress, and indeed, Pin1 prevents nuclear FOXO4 accumulation. Paper-12947886. Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/ Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons. Paper-12884140. Here we found that DNA damage enhanced the interaction between Pin1 and p53, which depended on the WW domain in Pin1 and Ser(33/46)-Pro motifs in p53. Paper-9282066. Consistent with this, oxidative stress induces binding of Pin1 to FOXO, thereby attenuating its monoubiquitination, a yet uncharacterized mode of substrate modulation by Pin1. Paper-12947886. Immunohistochemical analysis of brain tissue from PD patients revealed that Pin1 localizes to 50-60% of the LBs that show an intense halo pattern resembling that of alpha-synuclein. Paper-10844724. We report in our current study that the peptidyl-prolyl isomerase Pin1 is highly overexpressed in malignant human gliomas and inhibits Daxx-mediated cellular apoptosis. Paper-12637285. The expression levels of Pin1 and cyclinD1 in 6 esophageal SCC-derived cell lines were compared with those in an immortalized human esophageal cell line by western blotting. Paper-12138331. Our results indicate that the peptidylprolyl isomerase Pin1 interacts with Btk in a cell cycle-dependent manner, regulating the Btk expression level. Paper-12048950. Thus, Pin1 is identified as a novel negative FOXO regulator, interconnecting FOXO phosphorylation and monoubiquitination in response to cellular stress to regulate p27(kip1). Paper-12947886. We identified DYRK and Pin1 as novel CRMP4 binding proteins with DYRK interacting preferentially with dephospho-CRMP4 and Pin1 with phospho-CRMP4. Paper-12736552. Cellular phosphorylation of Dab2 by cdc2 promotes the association of Dab2 with Pin1, a peptidylprolyl isomerase that regulates the rate of Dab2 dephosphorylation. Paper-9781882. An intriguing player in this process is the prolyl isomerase Pin1, which induces a conformational change in p53, and more recently identified, also in p73, in response to DNA damage. Paper-11429226. An additional 40-kDa protein was observed with the pro-alpha-inhibin antisera, PIN 1 and 2, and a protein of more than 97 kDa was seen with the PIN 2 antiserum.(ABSTRACT TRUNCATED AT 400 WORDS) Paper-370155. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Paper-1248489. Thus, Pin1 is an E2F target gene that is essential for the Neu/Ras- induced transformation of mammary epithelial cells through activation of cyclin D1. Paper-9504863. Mean PSAD was calculated to be 0.1 for BPH patients; 0.09 for PIN-1 patients; 0.1 for PIN-2 patients; 0.51 for organ-confined prostatic carcinoma (CaP) patients and 1.7 for advanced CaP patients. Paper-636609. By using the peptidylprolyl isomerase, Pin1, as a probe for proline-directed phosphorylation, we show that ERK1/2-dependent phosphorylation of Bim(EL) occurs at (S/T)P motifs. Paper-10278916. In a separate paper, we have shown that Pin1 is a phosphorylation-dependent PPIase that can recognize specifically the phosphorylated Ser/Thr-Pro bonds present in mitotic phosphoproteins. Paper-1364274. Moreover, Pin1-deficient cells are defective in p53 activation and timely accumulation of p53 protein, and exhibit an impaired checkpoint control in response to DNA damage. Paper-9224584. The frequency of disruption of the basal cell layer increased with increasing grades of PIN, with disruption present in 0.7% of cases of PIN 1, 15% of cases of PIN 2, and 56% of cases of PIN 3. Paper-5560052. After DNA damage accumulated, the kinase ATM promoted Bcl-6 phosphorylation, leading to its interaction with the isomerase Pin1 and its degradation by the ubiquitin-proteasome system. Paper-12498277. We have previously shown that Pin1 is overexpressed in breast tumors and positively regulates cyclin D1 by transcriptional activation and posttranslational stabilization. Paper-9504863. Higher Pin1 expression in primary PCa is correlated with disease recurrence, and this study found that Pin1 expression was markedly increased in metastatic PCa. Paper-10827857. We further studied Pin1 and Nek6 mRNA level in 40 pairs of hepatocellular carcinoma cases, finding significant correlations between Nek6 and Pin1 mRNA expression levels in these samples. Paper-11388326. Here we report that DNA damage specifically induces p53 phosphorylation on Ser/Thr-Pro motifs, which facilitates its interaction with Pin1, a member of peptidyl-prolyl isomerase. Paper-9224584. Further, we propose a role for Pin1-dependent induction of p53 conformational change as a mechanism responsible for the enhanced interaction between p53 and Chk2 following DNA damage. Paper-10775381. The tumor suppressor p53 and the prolyl isomerase Pin1 are both highly connected proteins, lying at the crossroads between many signaling pathways that control cell proliferation and transformation. Paper-11429314. Disruption of the parvulin family peptidyl prolyl isomerase ( PPIase) Pin1 gene delays reentry into the cell cycle when quiescent primary mouse embryo fibroblasts are stimulated with serum. Paper-9915551. Deletional mutagenesis revealed two cryptic binding sites within the C-terminus of BNIP-H such that single point mutants affecting the WW domain of Pin1 completely abolished their binding. Paper-12884140. The pathway involves Ras-activated kinases, the Pin1 prolyl isomerase, the PP2A phosphatase and a series of c-Myc phosphorylation and dephosphorylation events that control its stability. Paper-11426378. Following evaluation of the slides, data were also analyzed by combining several of the groups into three categories: (a) benign/ PIN1; (b) PIN2/ PIN3/PIN cannot rule out cancer; and (c) PIN plus cancer. Paper-286570. In this study we show that Pin1 associates with phosphorylated neurofilament-H (p- NF-H) in neurons and is colocalized in ALS-affected spinal cord neuronal inclusions. Paper-13402762. These results implicate Pin1 as a possible modulator of stress- induced NF-H phosphorylation as seen in neurodegenerative disorders like AD and amyotrophic lateral sclerosis. Paper-13005692. JNK3, a brain-specific JNK isoform, is activated under oxidative and heat stresses, and inhibition of Pin1 by Pin1 short interference RNA and DN-Pin1 inhibits this pathway. Paper-13005692. Downregulating Pin1 prior to NGF withdrawal suppressed the accumulation of phosphorylated c-Jun, inhibited the release of cytochrome c, and significantly delayed cell death. Paper-12901982. The association of NHERF-1 with Pin1 facilitated dephosphorylation of NHERF-1, as shown in experiments in which cellular Pin1 activity was blocked by the selective inhibitor juglone. Paper-9088448. To mimic the pathology of neurodegeneration, we studied glutamate-stressed neurons that displayed increased p- NF-H in perikaryal accumulations that colocalized with Pin1 and led to cell death. Paper-13402762. We demonstrate in our current study, however, that the prolyl-isomerase Pin1 localizes to the LBs in PD brain tissue and thereby enhances the formation of alpha-synuclein immunoreactive inclusions. Paper-10844724. Western blotting with the PIN-1 antibody confirmed the presence of immunoreactive proteins of 57,000 and 29,000 mol wt in the follicular fluids of both normal cycle and IVF follicles. Paper-8197826. Repetition of each synthesis with the Fmoc strategy on a newly developed DOD resin for peptide amides using the DCC/HOBt chemistry gave superior results in terms of the yield and purity of the crude peptides. Paper-7160957. Activation of beta-catenin signaling in prostate cancer by peptidyl-prolyl isomerase Pin1- mediated abrogation of the androgen receptor- beta-catenin interaction. Paper-10827857. Furthermore, KRMP1 interacted with the mitotic peptidyl-prolyl isomerase Pin1 in vivo, and an in vitro interaction was detected between the tail domain of KRMP1 and the WW domain of Pin1. Paper-8960481. Furthermore, Pin1 binds to the phosphorylated Ser(178)-Pro motif in the Daxx protein, and Pin1 overexpression results in the rapid degradation of Daxx via the ubiquitin-proteasome pathway. Paper-12637285. In the histological areas examined a decreasing production of neutral mucin was found as follows: normal prostatic tissue (70%), prostatic carcinoma (55%), PIN 1 (50%), PIN 2 (30%) and PIN 3 (15%). Paper-7587390. However, in contrast to results in cells with intact PTEN and active GSK-3beta, Pin1 expression in LNCaP PCa cells, which are PTEN deficient, did not increase beta-catenin. Paper-10827857. The expression of the peptidyl-proplyl-isomerase PIN1 gene, the mutation in exon 3 of beta-catenin and its correspondent abnormal expression and their roles in the hepatocellular carcinogeneisis were investigated. Paper-12477969. Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase ( PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). Paper-1248489. The hyperphosphorylated/desensitized Raf-1 is subsequently dephosphorylated and returned to a signaling-competent state through interactions with the protein phosphatase PP2A and the prolyl isomerase Pin1. Paper-10806287. We conclude that protein oxidation plays a significant role in the development of AD from MCI and that the oxidative inactivation of ENO1, GLUL, PKM2 and PIN1 is involved in the progression of AD from MCI. Paper-11830705. In this respect, here we examine two CK2-interacting proteins, namely Pin1 and CKIP-1 that have been shown to participate in the modulation of CK2 specificity or the subcellular localisation of CK2, respectively. Paper-11522354. We now identify Pin1, a cis-trans isomerase, as an essential component of the ribonucleoprotein complex responsible for GM-CSF mRNA stabilization, cytokine secretion and the survival of activated eosinophils. Paper-11524493. We demonstrate by NMR studies and molecular dynamics simulations that the first turn of the hYAP, FBP28, and PIN1 WW domains is structurally dynamic and solvent exposed in the native and folding transition states. Paper-12505774. We would like to put forward the hypothesis that Pin1 is involved in RB proteins phosphorylation and E2F release, suggesting an additional post-translational level of control on this family of molecules. Paper-11099145. These results showed that PIN1 overexpression leading to beta-catenin accumulation might be a critical event in hepatocarcinogenesis, and that PIN1 is a potential target for therapeutic intervention in HCC. Paper-10255803. Outcome measures and results: The results were analyzed in terms of morbidity and oncological outcome; patients were recorded as NED (no existing disease), AWD (alive with disease), and DOD (died of disease). Paper-12589803. We also show that Emi1- Pin1 binding is present in vivo in XL2 cells during G2 phase and that this association protects Emi1 from being degraded during this phase of the cell cycle. Paper-12392717. It is suggested that Pin1 may contribute to cervical tumorigenesis by regulating cyclin D1 expression and Pin1 may serve as a promising molecular target for diagnostics and therapeutics in cervical cancer. Paper-12153195. BACKGROUND: Pin1 isomerizes the bonds of molecules important for numerous oncogenic and cell-signaling pathways, including Bcl-2, p53, c-Jun, beta-catenin, NF-kappaB, cyclin D1, c-Myc and Raf-1. Paper-13149429. Using several types of assays we could not find any evidence of an effect of Pin1, the human homolog of ESS1, on transcription by RNA polymerase II in vitro or on the expression of a reporter gene in vivo. Paper-8733403. 31P NMR spectra of lipid membrane in the presence of pin1, at various temperatures, showed that pin1 induces various lipid phase behaviors depending on the acyl chain length and charge of phospholipids. Paper-11173197. These results indicate that Pin1- mediated prolyl-isomerization plays a pivotal role in a post-translational modification pathway for alpha-synuclein aggregation and in the resultant Lewy body formations in PD. Paper-10844724. These results indicate that Pin1 is a regulator of Cyclin D1 expression in OSCC and might have a role in oncogenesis; and the expression of many cyclin genes will be an indicator of lymph node metastasis in OSCC. Paper-9892679. Ectopic Pin1 promoted caspase-dependent death of NGF-maintained neurons that was associated with an accumulation of Ser(63)- phosphorylated c-Jun in neuronal nuclei and was partially dependent on Bax. Paper-12901982. We conclude that this basic cluster formed by Arg21 and Arg22, both located in the beta1/ alpha1 loop, is homologous to that found in the hPIN1 crystal structure (Arg68 and Arg69), which also is involved in sulfate ion binding. Paper-9493769. Furthermore, binding of Pin1 to NFAT inhibits the calcineurin-mediated dephosphorylation of NFAT in vitro, and overexpression of Pin1 in T cells inhibits calcium-dependent activation of NFAT in vivo. Paper-8963868. BNIP-H interacted with Pin1 after nerve growth factor-stimulation and they co-localized in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Paper-12884140. Pin1 is a novel essential peptidyl-prolyl isomerase ( PPIase) that inhibits entry into mitosis and is also required for proper progression through mitosis, but its substrate(s) and function(s) remain to be determined. Paper-1364274. Furthermore, we found that in response to apoptotic stimuli Che-1 interacts with the peptidyl-prolyl isomerase Pin1 and that conformational changes generated by Pin1 are required for Che-1/ HDM2 interaction. Paper-13321927. Cdk9 dependent phosphorylation of Rpb1 and hSpt5 followed by Pin1 interaction might thus contribute to the regulation of transcription, pre-mRNA maturation, and the dynamics of these proteins in interphase and mitosis. Paper-9073217. We demonstrate here that peptidyl-prolyl isomerase 1 ( Pin1), which catalyzes the isomerization of phosphorylated Ser/Thr-Pro peptide bonds to induce conformational changes of its target proteins, interacts selectively with phosphorylated SRC-3. Paper-11103946. Thus, these data suggest that the mitogenic function of IGF-1 is at least partially linked to the induction of Pin1, which in turn stimulates cyclin D1 expression and RB phosphorylation, therefore contributing to G0/G1-S transition. Paper-9354285. METHODS: Protein expression levels of Pin1 in tumor and normal lung specimens were analyzed for expression of Pin1, cyclin D1, p53 and MDM2 using immunohistochemistry and compared to several clinicopathological characteristics. Paper-13149429. In an in vitro kinase assay, the addition of Pin1 substantially increased phosphorylation of NF-H KSP repeats by proline-directed kinases, Erk1/2, Cdk5/ p35, and JNK3 in a concentration-dependent manner. Paper-13005692. Furthermore, in the context of Cdc4alpha and cyclin E, mutational data suggest that Pin1 isomerizes a noncanonical proline-proline bond, with the possibility that Cdc4alpha may serve as a cofactor for altering the specificity of Pin1. Paper-12057148. This study aimed to elucidate whether Pin1 was involved in cyclin D1 overexpression and aberrant beta-catenin in thyroid tumourigenesis by examining 14 follicular adenomas (FAa) and 14 papillary thyroid carcinomas (PTCs). Paper-10224596. Here, Pin1 distribution in AD, and its colocalization with pThr231 tau in AD, FTDP-17 (P301L), Pick's disease (PiD), and PSP was investigated using TG-3, a monoclonal antibody to conformationally altered pThr231 tau. Paper-10168595. We first demonstrate that the interaction of Pin1 with chromatin is greatly elevated in G2/ M phase and that this correlates with the presence on chromosomes of several mitotic phosphoproteins, especially topoisomerase ( Topo) IIalpha. Paper-13208959. There was a strong correlation between cyclin D1 and Pin1/ cytoplasmic/membrane beta-catenin expression (p < 0.001), and between Pin1 and cytoplasmic (p < 0.001)/membrane (p = 0.002) beta-catenin expression in thyroid tumours. Paper-10224596. In this study, whether Pin1 is involved in cervical oncogenesis by regulating cyclin D1 was explored and the potential of Pin1-targeted gene silencing in inhibiting cellular growth and tumorigenicity in cervical cancer was investigated. Paper-12153195. Our results suggest that Pin1 functions as a transcriptional coactivator of nuclear receptors by modulating SRC-3 coactivator protein-protein complex formation and ultimately by also promoting the turnover of the activated SRC-3 oncoprotein. Paper-11103946. The expression of Pin1, beta-catenin and cyclin D1 were examined in the specimens of 65 patients with SACC by immunohistochemistry, protein and mRNA expressions were detected by western blotting and RT-PCR in four SACC cell lines. Paper-12153197. Pin1 not only binds the mitotic form of Cdc25 on the phosphorylation sites important for its activity in vitro and in vivo, but it also inhibits its activity, offering one explanation for the ability of Pin1 to inhibit mitotic entry. Paper-1364274. Cdk2- mediated phosphorylation of SMRT is required for Pin1 binding and decreases SMRT stability, whereas mutation of these phosphorylation sites abrogates Pin1 binding and stabilizes SMRT. Paper-13024200. CONCLUSION: Overexpression of Pin1 and beta-catenin may be closely related with the development and/or progression of colorectal carcinoma and further supports that Pin1 overexpression might contribute to the upregulation of beta-catenin. Paper-10752086. In contrast, inhibition of Pin1 suppresses Neu- and Ras-induced transformed phenotypes, which can be fully rescued by overexpression of a constitutively active cyclin D1 mutant that is refractory to the Pin1 inhibition. Paper-9504863. RESULTS: GC was characterized by overregulated v-raf, v-erb-a, BCL2-associated- athanogene, immediate-early-response-3, Polo-like kinase, CDK-2, cyclin-C, Pin1 genes, and downregulated ADP-ribosyltransferase, sialophorin and DCC. Paper-13398110. By utilizing a cellular model of alpha-synuclein aggregation, we also demonstrate that, whereas Pin1 overexpression facilitates the formation of alpha-synuclein inclusions, dominant-negative Pin1 expression significantly suppresses this process. Paper-10844724. The peptidyl-proplyl-isomerase, PIN1, upregulates beta-catenin by inhibiting its interaction with APC. beta-catenin accumulation occurs in about 70% of hepatocellular carcinoma ( HCC), of which only 20% are due to beta-catenin mutations. Paper-10255803. Although we could not be able to differentiate BPH from PIN-1 and PIN-2 by using PSAD alone (p > 0.05), there were statistically significant differences between BPH versus localized CaP, PIN-2 versus localized CaP and localized CaP versus advanced CaP (p < 0.05). Paper-636609. Instead, Pin1 expression markedly inhibited the beta-catenin interaction with AR, and Pin1 abrogated the ability of AR to antagonize beta-catenin/ Tcf4 binding and transcriptional activity. Paper-10827857. Finally, decreases in SMRT stability occur in response to the activation of Her2/Neu/ErbB2, and this receptor functions upstream of both Pin1 and Cdk2 in the signaling cascade that regulates SMRT stability and cellular response to tamoxifen. Paper-13024200. Here, we characterize novel FOXO4 phosphorylation sites after increased cellular oxidative stress and identify the isomerase Pin1, a protein frequently found to be overexpressed in cancer, as a critical regulator of p27(kip1) through FOXO4 inhibition. Paper-12947886. Pin1 is a peptidyl-prolyl cis/trans isomerase that stabilizes beta-catenin by inhibiting its binding to the adenomatous polyposis coli gene product and subsequent glycogen synthase kinase 3beta (GSK-3beta)-dependent degradation. Paper-10827857. Finally, we show that Pin1 binds synphilin-1, an alpha-synuclein partner, via its Ser-211-Pro and Ser-215-Pro motifs, and enhances its interaction with alpha-synuclein, thus likely facilitating the formation of alpha-synuclein inclusions. Paper-10844724. The relationships among these signaling cascades, which involve the amyloid precursor protein ( APP), cyclin-dependent kinases (cdks), and the cell cycle protein Pin1, have not yet been fully elucidated, but details of the individual pathways are beginning to emerge. Paper-12114548. Cyclin D1 is a target molecule transcriptionally activated by aberrant beta-catenin in Wnt signalling, while prolyl isomerase Pin1 promotes cyclin D1 overexpression directly or through accumulation of beta-catenin in cancer cells. Paper-10224596. On the basis of these findings, we demonstrated that these types of small molecules were able to effectively disrupt the phosphoprotein-protein interaction in a phosphorylated CTD peptide and the Pin1 WW domain, a phosphoprotein binding domain, at a micromolar level. Paper-11393905. These include the neuronal Munc-18 interacting proteins (Mints)/X11s, members of the reticulon family ( RTN-3 and RTN-4/ Nogo-B), the Nogo-66 receptor ( NgR), the peptidyl-prolyl isomerase Pin1 and the Rho family GTPases and their effectors. Paper-12435164. Here we show that the peptidyl-prolyl isomerase Pin1 influences the phosphorylation status of the CTD in vitro by inhibiting the CTD phosphatase FCP1 and stimulating CTD phosphorylation by cdc2/ cyclin B. Paper-10157291. The WW domain of the human PIN1 and p13(SUC1), a subunit of the cyclin-dependent kinase complex, were previously shown to be involved in the regulation of the cyclin-dependent kinase complex activity at the entry into mitosis, by an unresolved molecular mechanism. Paper-8697047. We show that Pin1 catalytically generates a conformational change on the mitotic phosphatase Cdc25, as assayed by limited protease digestion, differential reactivity to a phosphoserine-proline-directed monoclonal antibody (MPM-2), and by changes in Cdc25 enzymatic activity. Paper-8982525. ES1 treatment induced the rapid agglomeration of the auxin translocators PIN2 and AUX1 and the brassinosteroid receptor BRI1 into distinct endomembrane compartments termed "endosidin bodies"; however, the markers PIN1, PIN7, and other PM proteins were unaffected. Paper-12839915. Primers were designed to discriminate between the two transcripts, and PCR on DNA from hamster/human somatic cell hybrids retaining chromosomes 1 or 19 was used to map the human PIN1 gene to chromosome 19, and PIN1L, a closely related gene, to chromosome 1. Paper-1228591. Here, we found that Pin1 binds c- Fos through specific pS/T-P sites within the c- Fos TAD, and that this interaction results in an enhanced transcriptional response of c- Fos to polypeptide growth factors that stimulate ERK. Paper-10974435. Using a quantitative trait linkage disequilibrium test, we found significant associations between UBL5 genetic variants and waist-to-hip ratio (p = 0.027), and the circulating concentrations of insulin (p = 0.018) and total cholesterol (p = 0.023) in fasted individuals. Paper-12268034. We have here shown that the peptidylprolyl cis/trans isomerase ( PPIase) Pin1 is a negative regulator of Btk, controlling its expression level by reducing its half-life, whereas the catalytic activity of Btk was unaffected. Paper-12048950. These results together indicate that Pin1- mediated prolyl isomerization plays an important role in the negative regulation of Daxx and thereby inhibits the oxidative stress-induced cellular apoptotic response, particularly in malignant tumor cells where Pin1 is often overexpressed. Paper-12637285. Pin1 expression in LNCaP cells enhanced beta-catenin/ Tcf4 transcriptional activity, as assessed using Tcf4-regulated reporter genes, and increased expression of endogenous Tcf4 and c-myc. Paper-10827857. Results: Low dose of Taxol that cause apoptosis (25 nM) enhanced Rb protein phosphorylation, decreased the expression of cyclin-dependent kinase inhibitors small er, Cyrillic27(KIP1) and p21(WAF1) , and potentiated the accumulation of phosphorylated p53 and of the prolyl isomerase Pin1. Paper-13003987. Thus, isomerization of lys-ser-pro repeat residues that are abundant in NF-H tail domains by Pin1 can regulate NF-H phosphorylation, which suggests that Pin1 inhibition may be an attractive therapeutic target to reduce pathological accumulations of p- NF-H. Paper-13402762. Here, we report that Pin1(-/-) MEF cells display a delayed cell cycle S-phase entry in response to IGF stimulation and that IGF-1 induces Pin1 protein expression which correlates with the induction of cyclin D1 and RB phosphorylation in human breast cancer cells. Paper-9354285. This aberrant response leading to neurofibrillary degeneration may be triggered by the sequential combination of three partners: the complex Cdk5/ p25 induces both apoptosis and the "abnormal mitotic Tau phosphorylation". These mitotic epitopes may allow for the nuclear depletion of Pin1. Paper-10114694. Since neurofibrillary degeneration is likely to be a third way to die, molecular mechanisms leading to changes in Tau phosphorylation including activation of kinases such as cdk5 or other regulators such as Pin1 could be important drug targets as they are possibly involved in early stages of neurodegeneration. Paper-10114694. Chemical complementation by flavonoids correlates with an asymmetric distribution of the PIN1 protein. pin2 complementation probably does not result from inhibition of auxin efflux, as supply of the auxin transport inhibitor N-1-naphthylphthalamic acid failed to restore pin2 gravitropism. Paper-13067150. Human parvulin (hParvulin; Par14/ EPVH) belongs to the third family of peptidylprolyl cis-trans isomerases that exhibit an enzymatic activity of interconverting the cis-trans conformation of the prolyl peptide bond, and shows sequence similarity to the regulator enzyme for cell cycle transitions, human Pin1. Paper-9180231. No direct interaction between the PIN1 WW domain or its catalytic proline cis/trans-isomerase domain and p13(SUC1) was detected, but our study showed that in vitro the WW domain of the human PIN1 antagonizes the binding of the p13(SUC1) to the CDC25 phosphopeptide, by binding to the same phosphoepitope. Paper-8697047. METHODS: The role of Pin1 and beta-catenin protein in colorectal tumorigenesis and their clinicopathologic significance were analyzed by immunohistochemistry, and the correlation between Pin1 and beta-catenin protein expressions was also studied in 124 patients with colorectal cancer who were surgically treated. Paper-10752086. These results indicate that Pin1 positively regulates cyclin D1 function at the transcriptional level, as demonstrated previously, and also through posttranslational stabilization, which together explain why Pin1 loss-of- function phenotypes in the mouse resemble cyclin D1-null phenotypes. Paper-9155675. In order to investigate the expression levels of Pin1 mRNA and protein in cervical cancer and its association with Ki67 and their clinical significance, amplification of Pin1 gene was examined by RT-PCR, and the expression of both Pin1 and Ki67 protein was detected by immunohistochemistry in cervical cancer tissues. Paper-12109749. Because of the diverse functions of Pin1, and the discovery that this protein is one of the oxidized proteins common to both MCI and AD brain, the question arises as to whether Pin1 is one of the driving forces for the initiation or progression of AD pathogenesis, finally leading to neurodegeneration and neuronal apoptosis. Paper-12204648. Similar levels of pro-alpha-inhibin immunoreactivity ( PIN-1 RIA; N-terminus alpha-inhibin precursor) were detected in hFF collected from women with normal menstrual cycles during the follicular phase and from multiple follicles from a woman undergoing ovarian hyperstimulation during an in vitro fertilization ( IVF) protocol. Paper-8197826. SCF(hCdc4alpha) binds a complex containing cyclin E, Cdk2, and the prolyl cis/trans isomerase Pin1 and promotes the activity of Pin1 without directly ubiquitylating cyclin E. However, due to the action of this SCF(hCdc4alpha)-Pin1 complex, cyclin E becomes an efficient ubiquitylation substrate of SCF(hCdc4gamma). Paper-12057148. In this regard, it has been recently observed that the prolyl isomerase Pin1 can interact with proteins phosphorylated on serine or threonine residues that precede prolines (pS/T-P), such as the transcription factors p53 and c-Jun, thereby controlling their activity by promoting the cis-trans isomerization of these pS/T-P bonds. Paper-10974435. The X-ray crystal structure of Pin1 bound to a doubly phosphorylated peptide (Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser) representing a heptad repeat of the RNA polymerase II large subunit's C-terminal domain (CTD), reveals the residues involved in the recognition of a single P.Ser side chain, the rings of two prolines, and the backbone of the CTD peptide. Paper-8365095. Our findings suggest that c- Fos represents a novel target for the isomerizing activity of Pin1 and support a role for Pin1 in the mechanism by which c-Jun and c- Fos can cooperate to regulate AP-1-dependent gene transcription upon phosphorylation by mitogen- activated kinase ( MAPK) family members. Paper-10974435. These findings demonstrate that AR can suppress beta-catenin signaling, that the AR- beta-catenin interaction can be regulated by Pin1, and that abrogation of this interaction can enhance beta-catenin/ Tcf4 signaling and contribute to aggressive biological behavior in PCa. Paper-10827857. The strongly decreased affinity of Pin1 for ligand at increasing ionic strength implicates that the potential of bidentate binding of a substrate protein by the PPIase and the WW domain of Pin1 may be required to deploy improved efficiency and specificity of Pin1 under conditions of physiological ionic strength. Paper-11987582. The aims of this study were to investigate the expression levels of beta-catenin, Pin1 and cyclin D1 in salivary adenoid cystic carcinomas (SACC ) and to evaluate its clinical importance, furthermore, to elucidate whether beta-catenin expression was aberrant in SACC and whether Pin1 was involved in aberrant beta-catenin and cyclin D1 expression. Paper-12153197. In the model dicot plant Arabidopsis thaliana, the trafficking and localization of auxin efflux facilitators such as PIN-FORMED1 ( PIN1) are mediated by GNOM, a guanine-nucleotide exchange factor ( GEF) for the ADP-ribosylation factor ( ARF) family of small GTPases, but molecular regulators of the auxin influx facilitators remain unknown. Paper-12305716. These synonyms are used for gene PIN1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1): UBL5, Rotamase Pin1, PPIase Pin1, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, DOD, dod. These accession numbers are used for gene PIN1: Q53X75 (UNIPROT__AC), Q49AR7 (UNIPROT__AC), AAV38138 (NCBI_GENBANK__AC), AAH02899 (NCBI_GENBANK__AC). PIN1 is a homologue of Y110A2AL.13 (hypothetical protein) from Caenorhabditis elegans. PIN1 is a homologue of PIN1AT (PIN1AT (PEPTIDYLPROLYL CIS/TRANS ISOMERASE, NIMA-INTERACTING 1); peptidyl...) from Arabidopsis thaliana. PIN1 is a homologue of PIN1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1) from Bos taurus. PIN1 is a homologue of PIN1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1) from Pan troglodytes. PIN1 is a homologue of PIN1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1) from Canis lupus familiaris. PIN1 is a homologue of Pin1 (protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1) from Mus musculus. PIN1 is a homologue of Pin1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1) from Rattus norvegicus. PIN1 is a homologue of pin1 (peptidyl-prolyl cis-trans isomerase Pin1) from Schizosaccharomyces pombe. PIN1 is a homologue of Os04g0118500 (Os04g0118500) from Oryza sativa Japonica Group. PIN1 is a homologue of NCU08554 (peptidyl-prolyl cis-trans isomerase ssp-1) from Neurospora crassa OR74A. PIN1 is a homologue of MGG_07389 (hypothetical protein) from Magnaporthe grisea 70-15. PIN1 is a homologue of KLLA0E16610g (hypothetical protein) from Kluyveromyces lactis NRRL Y-1140. PIN1 is a homologue of ESS1 (Ess1p) from Saccharomyces cerevisiae. PIN1 is a homologue of dod (dodo) from Drosophila melanogaster. PIN1 is a homologue of AGOS_ACL120W (ACL120Wp) from Ashbya gossypii ATCC 10895. PIN1 is a homologue of AgaP_AGAP004321 (AGAP004321-PA) from Anopheles gambiae str. PEST. Important links ! iHOP - Information Hyperlinked over Proteins . Concept & Implementation by Robert Hoffmann.