Structural Basis for High-Affinity Peptide Inhibition of Human Pin1 - Test2 - elhamkhani - TriplyDB

Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Regulation of AU-Rich Element RNA Binding Proteins by Phosphorylation and the Prolyl Isomerase Pin1 Prolyl isomerase Pin1 in cancer Epigallocatechin-gallate Suppresses Tumorigenesis by Directly Targeting Pin1 A Reduced-Amide Inhibitor of Pin1 Binds in a Conformation Resembling a Twisted-Amide Transition State Structural and Kinetic Analysis of Prolyl-isomerization/Phosphorylation Cross-Talk in the CTD Code Circular Permutation of a WW Domain: Folding Still Occurs after Excising the Turn of the Folding-Nucleating Hairpin The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination Stereochemical Control in the Still-Wittig Rearrangement Synthesis of Cyclohexyl (Z)-Alkene Inhibitors of Pin1 Interfacial water molecules in SH3 interactions: a revised paradigm for polyproline recognition.Isoform-specific inhibition of cyclophilins Kinetic isotope effects support the twisted amide mechanism of Pin1 peptidyl-prolyl isomerase Discovery and binding studies on a series of novel Pin1 ligands.Detection of protein catalytic residues at high precision using local network properties.Membrane permeable cyclic peptidyl inhibitors against human Peptidylprolyl Isomerase Pin1.Dynamic regulation of Pin1 expression and function during zebrafish development.The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Prolyl isomerase Pin1 acts downstream of miR200c to promote cancer stem-like cell traits in breast cancer Cyclohexyl ketone inhibitors of Pin1 dock in a trans-diaxial cyclohexane conformation.Pin1-mediated Sp1 phosphorylation by CDK1 increases Sp1 stability and decreases its DNA-binding activity during mitosis.Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function Prolyl isomerases in gene transcription Active Pin1 is a key target of all-trans retinoic acid in acute promyelocytic leukemia and breast cancer Roles of Prolyl Isomerases in RNA-Mediated Gene Expression Retinoblastoma tumor-suppressor protein phosphorylation and inactivation depend on direct interaction with Pin1.Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668.Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.Complete protein characterization using top-down mass spectrometry and ultraviolet photodissociation Peptidyl-prolyl cis-trans isomerase Pin1 in ageing, cancer and Alzheimer disease.Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.The role of Pin1 in the development and treatment of cancer.Bio-molecular architects: a scaffold provided by the C-terminal domain of eukaryotic RNA polymerase II Optimization of a β-sheet-cap for long loop closure.Convergent synthesis of alpha-ketoamide inhibitors of Pin1.Proline cis/trans-isomerase Pin1 regulates peroxisome proliferator-activated receptor gamma activity through the direct binding to the activation function-1 domain.A phosphorylated prodrug for the inhibition of Pin1.Crowning proteins: modulating the protein surface properties using crown ethers.Non-catalytic participation of the Pin1 peptidyl-prolyl isomerase domain in target binding.Knockdown of Pin1 leads to reduced angiogenic potential and tumorigenicity in glioblastoma cells

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

http://www.wikidata.org/entity/Q27644848

description

2007 nî lūn-bûn

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2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2007 թվականի մայիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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type

label

Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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prefLabel

Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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ACS Chemical Biology

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

@en

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Dirk Wildemann

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

Gunter Fischer

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Joseph P Noel

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

Kun-Ping Lu

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Marianne E Bowman

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

Mark A Verdecia

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Sebastian Daum

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

Tony Hunter

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Xiao Zhen Zhou

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

Yan Zhang

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P2860

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

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

A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase

Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

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

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases

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320-8

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scholarly article

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10.1021/CB7000044

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5

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2

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Christian Lücke

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2007-05-22T00:00:00Z

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6315091

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17518432

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2692202

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