Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
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Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteinsSolution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulinsStructural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerasesSolution structural analysis of the single-domain parvulin TbPin1Molecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirusG protein-coupled receptor kinase 2 (GRK2) modulation and cell cycle progressionThe Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Prolyl isomerase Pin1 regulates transcription factor LSF (TFCP2) by facilitating dephosphorylation at two serine-proline motifs.Pin1 promotes degradation of Smad proteins and their interaction with phosphorylated tau in Alzheimer's disease.Prolyl isomerases in gene transcriptionSurf the post-translational modification network of p53 regulationNegative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1Regulation of PRDX1 peroxidase activity by Pin1.Expression of peptidyl-prolyl isomerase PIN1 and its role in the pathogenesis of extrahepatic cholangiocarcinoma.Unraveling the role of peptidyl-prolyl isomerases in neurodegeneration.The CTD code of RNA polymerase II: a structural view.MYC degradationThe alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites.Non-catalytic participation of the Pin1 peptidyl-prolyl isomerase domain in target binding.Mechanistic insights into Pin1 peptidyl-prolyl cis-trans isomerization from umbrella sampling simulations.Pin1 inhibition exerts potent activity against acute myeloid leukemia through blocking multiple cancer-driving pathways.
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P2860
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
description
2007 nî lūn-bûn
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2007年の論文
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2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
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2007年論文
@zh-tw
2007年论文
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2007年论文
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2007年论文
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name
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
@en
type
label
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
@en
prefLabel
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
@en
P2860
P1433
P1476
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
@en
P2093
I Landrieu
P2860
P304
P356
10.1111/J.1742-4658.2007.06057.X
P407
P577
2007-09-24T00:00:00Z