Peptide binding induces large scale changes in inter-domain mobility in human Pin1. - Wikidata - awgldk - TriplyDB

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

http://www.wikidata.org/entity/Q47986427

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Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1 Structure-function-folding relationship in a WW domain 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 The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination Discovery and binding studies on a series of novel Pin1 ligands.The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex.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).Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase Two pathways mediate interdomain allosteric regulation in pin1 Stereospecific gating of functional motions in Pin1 Roles of Prolyl Isomerases in RNA-Mediated Gene Expression Investigating Dynamic Interdomain Allostery in Pin1 Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human 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.The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.Dynamics driving function: new insights from electron transferring flavoproteins and partner complexes.Folding mechanisms of individual beta-hairpins in a Go model of Pin1 WW domain by all-atom molecular dynamics simulations.Protein Allostery and Conformational Dynamics.Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding.Enzyme-linked enzyme-binding assay for Pin1 WW domain ligands.Non-catalytic participation of the Pin1 peptidyl-prolyl isomerase domain in target binding.Interdomain interactions support interdomain communication in human Pin1 Comparative analysis of enzyme activities and mRNA levels of peptidyl prolyl cis/trans isomerases in various organs of wild type and Pin1-/- mice.Determination of phosphorylation sites for NADP-specific isocitrate dehydrogenase from mycobacterium tuberculosis.The role of the turn in beta-hairpin formation during WW domain folding.Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation.PINA is essential for growth and positively influences NIMA function in Aspergillus nidulans.Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1.A Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1.Regulation of Pin1 peptidyl-prolylcis/transisomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein Pin1 Modulation in Physiological Status and Neurodegeneration. Any Contribution to the Pathogenesis of Type 3 Diabetes?Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1

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P2860

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

http://www.wikidata.org/entity/Q47986427

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

@zh-my

2003年学术文章

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2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@en

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@nl

type

label

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@en

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@nl

prefLabel

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@en

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@nl

P1433

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Journal of Biological Chemistry

P1476

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@en

P2093

Doris M Jacobs

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

Klaus M Fiebig

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Krishna Saxena

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Martin Vogtherr

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Pau Bernado

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P2860

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

NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein

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

Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences

NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1

Structure and dynamics of KH domains from FBP bound to single-stranded DNA

Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana

Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding

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

Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

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26174-26182

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10.1074/JBC.M300796200

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