Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch - Test2 - elhamkhani - TriplyDB

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

http://www.wikidata.org/entity/Q27696897

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Phenotypic plasticity in prostate cancer: role of intrinsically disordered proteins Order, Disorder, and Everything in Between NMR Meets Tau: Insights into Its Function and Pathology Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies Signalling to eIF4E in cancer Whi5 phosphorylation embedded in the G1/S network dynamically controls critical cell size and cell fate.Rapid Brownian Motion Primes Ultrafast Reconstruction of Intrinsically Disordered Phe-Gly Repeats Inside the Nuclear Pore Complex.Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast.The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease Quantitative studies of mRNA recruitment to the eukaryotic ribosome Identification of a Novel Regulatory Mechanism of Nutrient Transport Controlled by TORC1-Npr1-Amu1/Par32 Conformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer Model Spatial proximity statistics suggest a regulatory role of protein phosphorylation on compound binding.Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum Conditionally disordered proteins: bringing the environment back into the fold.Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturation Intrinsic Disorder in Transmembrane Proteins: Roles in Signaling and Topology Prediction.The complexity of glycoprotein-derived glycans.Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.A simple model for electrical charge in globular macromolecules and linear polyelectrolytes in solution.New frontiers in translational control of the cancer genome Structural basis for regulation of RNA-binding proteins by phosphorylation.Differential Requirements for eIF4E Dose in Normal Development and Cancer IRBIT Interacts with the Catalytic Core of Phosphatidylinositol Phosphate Kinase Type Iα and IIα through Conserved Catalytic Aspartate Residues.Targeting intrinsically disordered proteins in rational drug discovery.Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1 Examining the Influence of Phosphorylation on Peptide Ion Structure by Ion Mobility Spectrometry-Mass Spectrometry.Low potency toxins reveal dense interaction networks in metabolism.Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Cyclin B Translation Depends on mTOR Activity after Fertilization in Sea Urchin Embryos.Chemical perturbation of an intrinsically disordered region of TFIID distinguishes two modes of transcription initiation.Functional advantages of dynamic protein disorder.Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and Ser250 phosphorylation in the conserved C-terminal regions.Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.Destabilizing an interacting motif strengthens the association of a designed ankyrin repeat protein with tubulin Hypertension: the missing WNKs.Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor Finding Our Way in the Dark Proteome.Exploring the dark foldable proteome by considering hydrophobic amino acids topology.

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P2860

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

http://www.wikidata.org/entity/Q27696897

description

2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

@zh-hk

2015年論文

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2015年論文

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2015年论文

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name

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@ast

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@en

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@nl

type

label

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@ast

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@en

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@nl

prefLabel

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@ast

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@en

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

@nl

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P1476

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

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Alaji Bah

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

Mickaël Krzeminski

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

Ranjith Muhandiram

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

Robert M Vernon

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

Zeba Siddiqui

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

P2860

Intrinsically unstructured proteins and their functions

Translational homeostasis via the mRNA cap-binding protein, eIF4E

The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins

Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Consistent blind protein structure generation from NMR chemical shift data

Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G

Structural polymorphism in the N-terminal oligomerization domain of NPM1

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Regulation of translation initiation in eukaryotes: mechanisms and biological targets

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106-9

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scholarly article

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227450

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10.1038/NATURE13999

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7541

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519

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Julie D Forman-Kay

Nahum Sonenberg

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2015-03-05T00:00:00Z

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1038656204

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25533957

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phosphorylation

protein folding