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Prolyl isomerase Pin1 regulates YB-1 and promotes tumor cell proliferation
四川大学学报. 自然科学版Peptidyl-prolyl cis/trans isomerase Pin1 has been proven to be closely related to tumor progression. Here， we aimed to explore the signal pathway by which Pin1 regulates the proliferation of tumor cells， immunoprecipitation and protein half-life ...
WANG Jia-Xin +3 more
doaj
파골세포와 근육세포의 세포 융합 과정에서의 Pin1 의 역할
, 2015 학위논문 (박사)-- 서울대학교 대학원 : 치의과학과, 2015. 2. 류현모.Cell-cell fusion is critical for the conception, development, and physiology of multicellular organisms. Although cellular fusogenic proteins and the actin cytoskeleton are implicated in cell-cell fusion, it ...
이슬람라비아
core
Pin1, the master orchestrator of bone cell differentiation
, 2017 Pin1 is an enzyme that specifically recognizes the peptide bond between phosphorylated serine or threonine (pS/pT-P) and proline. This recognition causes a conformational change of its substrate, which further regulates downstream signaling. Pin1−/− mice
R Islam (9875153) +2 more
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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.
Anthony R Means, Means Anthony R
exaly +3 more sources
Landscape of Pin1 in the cell cycle [PDF]
Experimental Biology and Medicine, 2015 Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle ...
Cheng-Han Lin +2 more
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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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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: A New Outlook in Alzheimers Disease
Current Alzheimer Research, 2011Neurodegenerative diseases termed Tauopathies, including Alzheimer disease, are characterized by the presence of intraneuronal neurofibrillary tangles (NFTs), composed by hyperphosphorylated protein Tau. Peptidyl-prolyl cis/trans isomerase Pin1 plays a pivotal role in the regulation of Tau phosphorylation/dephosphorylation state.
LONATI, ELENA RITA +2 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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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
openaire +1 more source