Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. - Wikidata - awgldk - TriplyDB

Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes.

Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes.

http://www.wikidata.org/entity/Q34009230

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The prolyl-isomerase Pin1 is a Notch1 target that enhances Notch1 activation in cancer Small family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical research Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism?The prolyl isomerase Pin1 in breast development and cancer Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins Prolyl isomerase Pin1 in cancer Structural Basis for High-Affinity Peptide Inhibition of Human Pin1 The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway The yeast Ess1 prolyl isomerase controls Swi6 and Whi5 nuclear localization.Understanding the role of PIN1 in hepatocellular carcinoma KSHV reactivation and novel implications of protein isomerization on lytic switch control Landscape of Pin1 in the cell cycle Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage Phosphorylation-specific prolyl isomerization: is there an underlying theme?The prolyl isomerase Pin1 acts synergistically with CDK2 to regulate the basal activity of estrogen receptor α in breast cancer Regulation of cardiac hypertrophic signaling by prolyl isomerase Pin1 Pin1 inhibition activates cyclin D and produces neurodegenerative pathology The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease An essential role for Pin1 in Xenopus laevis embryonic development revealed by specific inhibitors.Pin1: a molecular orchestrator in the heart.Redox proteomics in selected neurodegenerative disorders: from its infancy to future applications.Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires.Discovery and binding studies on a series of novel Pin1 ligands.Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces Pin-1 binding in cytoplasm and cell death.Membrane permeable cyclic peptidyl inhibitors against human Peptidylprolyl Isomerase Pin1.Dynamic regulation of Pin1 expression and function during zebrafish development.Identification of Peroxiredoxin 1 as a novel interaction partner for the lifespan regulator protein p66Shc.Pin1 facilitates the phosphorylation-dependent ubiquitination of SF-1 to regulate gonadotropin beta-subunit gene transcription G protein-coupled receptor kinase 2 (GRK2) modulation and cell cycle progression Physiological regulation of Akt activity and stability.Inhibition of the prolyl isomerase Pin1 enhances the ability of sorafenib to induce cell death and inhibit tumor growth in hepatocellular carcinoma.Prolyl isomerase Pin1 acts downstream of miR200c to promote cancer stem-like cell traits in breast cancer Pin1-Targeted Therapy for Systemic Lupus Erythematosus The functional promoter polymorphism (-842G>C) in the PIN1 gene is associated with decreased risk of breast cancer in non-Hispanic white women 55 years and younger.Phosphorylation stabilizes Nanog by promoting its interaction with Pin1 Elevated PIN1 expression by C/EBPalpha-p30 blocks C/EBPalpha-induced granulocytic differentiation through c-Jun in AML 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).The telomerase inhibitor PinX1 is a major haploinsufficient tumor suppressor essential for chromosome stability in mice Prolyl isomerase Pin1 regulates mouse embryonic fibroblast differentiation into adipose cells.The roles of peptidyl-proline isomerases in gene regulation.

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P2860

Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes.

http://www.wikidata.org/entity/Q34009230

description

2002 nî lūn-bûn

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2002 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2002 թվականի հունվարին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@ast

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@en

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@nl

type

label

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@ast

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@en

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@nl

prefLabel

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@ast

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@en

Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

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Loss of Pin1 function in the m ...... ing cyclin D1-null phenotypes.

@en

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Akihide Ryo

http://www.w3.org/2001/XMLSchema#string

Fumihiro Fujimori

http://www.w3.org/2001/XMLSchema#string

Han-Kuei Huang

http://www.w3.org/2001/XMLSchema#string

Kun Ping Lu

http://www.w3.org/2001/XMLSchema#string

Pei-Jung Lu

http://www.w3.org/2001/XMLSchema#string

Roderick Bronson

http://www.w3.org/2001/XMLSchema#string

Takafumi Uchida

http://www.w3.org/2001/XMLSchema#string

Tony Hunter

http://www.w3.org/2001/XMLSchema#string

Yih-Cherng Liou

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P2860

Function of WW domains as phosphoserine- or phosphothreonine-binding modules

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC

The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1

Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1.

Accumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosis

The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins

Structural basis for phosphoserine-proline recognition by group IV WW domains

Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent

The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery.

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1335-1340

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scholarly article

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10.1073/PNAS.032404099

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P433

3

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99

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2002-01-22T00:00:00Z

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11554416

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11805292

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122191

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