Results 171 to 180 of about 19,713 (201)
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Translational Research, 2023
Alzheimer's disease (AD) is an immense and growing public health crisis. Despite over 100 years of investigation, the etiology remains elusive and therapy ineffective. Despite current gaps in knowledge, recent studies have identified dysfunction or loss-of-function of Pin1, a unique cis-trans peptidyl prolyl isomerase, as an important step in AD ...
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Alzheimer's disease (AD) is an immense and growing public health crisis. Despite over 100 years of investigation, the etiology remains elusive and therapy ineffective. Despite current gaps in knowledge, recent studies have identified dysfunction or loss-of-function of Pin1, a unique cis-trans peptidyl prolyl isomerase, as an important step in AD ...
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Dissecting Pin1 and phospho‐pRb regulation
Journal of Cellular Physiology, 2012AbstractThe activity of the Retinoblastoma protein, the master regulator of the cell cycle, is finely regulated by phosphorylation. CDKs and cyclins are major players in phosphorylation and it has been recently discovered that the prolyl isomerase Pin1 is an essential protein that orchestrates this process.
Rizzolio, Flavio +10 more
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Journal of Cellular Physiology, 2017
Pin1 is a peptidyl prolyl cis‐trans isomerase that specifically binds to the phosphoserine‐proline or phosphothreonine‐proline motifs of several proteins. We reported that Pin1 plays a critical role in the fate determination of Smad1/5, Runx2, and β‐catenin that are indispensable nuclear proteins for osteoblast differentiation.
Woo-Jin, Kim +7 more
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Pin1 is a peptidyl prolyl cis‐trans isomerase that specifically binds to the phosphoserine‐proline or phosphothreonine‐proline motifs of several proteins. We reported that Pin1 plays a critical role in the fate determination of Smad1/5, Runx2, and β‐catenin that are indispensable nuclear proteins for osteoblast differentiation.
Woo-Jin, Kim +7 more
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PIN1 expression contributes to hepatic carcinogenesis
The Journal of Pathology, 2006AbstractThe phospho‐Ser/Thr‐Pro specific prolyl‐isomerase PIN1 is over‐expressed in more than 50% of hepatocellular carcinomas (HCCs). To investigate its potential oncogenicity, we over‐expressed PIN1 in a non‐transformed human liver cell line MIHA. This resulted in up‐regulation of β‐catenin and cyclin D1, leading to anchorage‐independent growth in ...
Man, K +6 more
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1997
Abstract Pinl, a human protein interacting with the mitotic NIMA kinase isolated from Aspergillus nidulans, contains a catalytic domain characteristic of the highly conserved third family of peptidyl-prolyl cis-trans isomerases that are distinct from either the cyclophilins or the FK506-binding proteins. Pinl is a widely expressed 18 kDa
K P Lu, T Hunter
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Abstract Pinl, a human protein interacting with the mitotic NIMA kinase isolated from Aspergillus nidulans, contains a catalytic domain characteristic of the highly conserved third family of peptidyl-prolyl cis-trans isomerases that are distinct from either the cyclophilins or the FK506-binding proteins. Pinl is a widely expressed 18 kDa
K P Lu, T Hunter
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Pin1 Promoter Polymorphisms in Hepatocellular Carcinoma Patients
Gastroenterology, 2007We analyzed Pin-1 rs2233678 and rs2233679 SNPs in a group of 228 HCC patients and 250 healthy controls with the aim of determining whether they can have a role in the onset of hepatocellular carcinogenesis. For the -842G/C SNP we found no significant differences in allelic and genotype frequencies in HCC patients and controls (Table 1).
SEGAT L, MILANESE M, CROVELLA, SERGIO
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PIN1, the cell cycle and cancer
Nature Reviews Cancer, 2007PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for cell-cycle progression and, based on gain- and loss-of-function studies, is presumed to operate as a molecular timer of this important process.
Elizabeth S, Yeh, Anthony R, Means
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Pin1 as an anticancer drug target
Drug News & Perspectives, 2009Pin1 specifically catalyzes the cis/trans isomerization of phospho-Ser/Thr-Pro bonds and plays an important role in many cellular events through the effects of conformational change on the function of its biological substrates, including cell division cycle 25 C (Cdc25C), c-Jun and p53.
Guoyan G, Xu, Felicia A, Etzkorn
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Pin1: Inhibitors and Mechanism
2010Introduction Peptidyl-prolyl isomerase (PPIase) enzymes are something of an enigma. Part chaperone, part enzyme, they play multiple roles in multiple biological systems. Cyclophilin and FKBP were first discovered in the late 1980’s because they bind to distinct natural products, cyclosporine and FK506 respectively, immunosuppressants which act as ...
Felicia A. Etzkorn +3 more
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Pin1 and Nuclear Receptors: A New Language?
Journal of Cellular Physiology, 2013AbstractPin1 is a unique enzyme that can isomerize specific phospho‐Ser/Thr‐Pro peptide bonds, inducing a conformational change in the target protein. Such activity represents a novel and tightly controlled signaling mechanism regulating a spectrum of protein functions during the normal physiology of the cell and in pathological conditions.
La Montagna, Raffaele +3 more
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