1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides - Wikidata - wikimedia - TriplyDB

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

http://www.wikidata.org/entity/Q27631268

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Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1 Markov state model reveals folding and functional dynamics in ultra-long MD trajectories Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity.Modeling conformational ensembles of slow functional motions in Pin1-WW Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding Structural Basis for Polyadenosine-RNA Binding by Nab2 Zn Fingers and Its Function in mRNA Nuclear Export Evolutionary information for specifying a protein fold The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease Cell signaling, post-translational protein modifications and NMR spectroscopy Modulating the folding stability and ligand binding affinity of Pin1 WW domain by proline ring puckering.Discovery and binding studies on a series of novel Pin1 ligands.Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial.Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance.High-resolution visualisation of the states and pathways sampled in molecular dynamics simulations The natively disordered loop of Bcl-2 undergoes phosphorylation-dependent conformational change and interacts with Pin1 Two pathways mediate interdomain allosteric regulation in pin1 Characterization of native protein complexes using ultraviolet photodissociation mass spectrometry.New Frontiers in Druggability Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons.Investigating Dynamic Interdomain Allostery in Pin1 Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1 Simple few-state models reveal hidden complexity in protein folding.Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668.Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease.Visualization of Compartmentalized Kinase Activity Dynamics Using Adaptable BimKARs.Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.Dynamics of ligand binding from 13C NMR relaxation dispersion at natural abundance.Effect of Pin1 or microtubule binding on dephosphorylation of FTDP-17 mutant Tau The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.Enzyme-linked enzyme-binding assay for Pin1 WW domain ligands.4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and 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.Interdomain interactions support interdomain communication in human Pin1 Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation.Mitotic-like tau phosphorylation by p25-Cdk5 kinase complex.Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites.Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.

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P2860

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

http://www.wikidata.org/entity/Q27631268

description

2001 nî lūn-bûn

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2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հուլիսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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name

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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type

label

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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prefLabel

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

@en

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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Journal of Biological Chemistry

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

@en

P2093

I Landrieu

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

J M Wieruszeski

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

P Rousselot-Pailley

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

R Wintjens

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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

Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands

Structural basis of cyclin-dependent kinase activation by phosphorylation

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

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

PROCHECK: a program to check the stereochemical quality of protein structures

Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding

Structural analysis of WW domains and design of a WW prototype

Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan

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25150-25156

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10.1074/JBC.M010327200

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27

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276

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11313338

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