Interconversion between two unrelated protein folds in the lymphotactin native state - Wikidata - awgldk - TriplyDB

Interconversion between two unrelated protein folds in the lymphotactin native state

Interconversion between two unrelated protein folds in the lymphotactin native state

http://www.wikidata.org/entity/Q27650152

about

Native-state interconversion of a metamorphic protein requires global unfolding ARNT PAS-B has a fragile native state structure with an alternative -sheet register nearby in sequence space The Structure of a Bacterial DUF199/WhiA Protein: Domestication of an Invasive Endonuclease A minimal sequence code for switching protein structure and function Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family Metamorphic proteins mediate evolutionary transitions of structure An Alternative Conformation of the T-Cell Receptor α Constant Region An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor Structure and dynamics of a primordial catalytic fold generated by in vitro evolution Disease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact Structure Mutational Tipping Points for Switching Protein Folds and Functions Structural insight into the evolution of a new chemokine family from zebrafish A Model of GAG/MIP-2/CXCR2 Interfaces and Its Functional Effects Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase Multiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidase Lessons from making the Structural Classification of Proteins (SCOP) and their implications for protein structure modelling Fast-folding proteins under stress A designed point mutant in Fis1 disrupts dimerization and mitochondrial fission Transient helical structure during PI3K and Fyn SH3 domain folding.Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape Interdomain contacts control folding of transcription factor RfaH.Transformation: the next level of regulation.Virtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.Protein dynamism and evolvability.Benchmarking Inverse Statistical Approaches for Protein Structure and Design with Exactly Solvable Models.Dynamic interchanging native states of lymphotactin examined by SNAPP-MS Structural gymnastics of multifunctional metamorphic proteins.Evolutionary bridges to new protein folds: design of C-terminal Cro protein chameleon sequences.Effects of point mutations on protein structure are nonexponentially distributed.Moonlighting is mainstream: paradigm adjustment required.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.A polymetamorphic protein.Chemokine CXCL7 Heterodimers: Structural Insights, CXCR2 Receptor Function, and Glycosaminoglycan Interactions Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.Fast protein folding kinetics A nuclear magnetic resonance based approach to accurate functional annotation of putative enzymes in the methanogen Methanosarcina acetivorans.Proteins that switch folds Bootstrapping new protein folds Smooth functional transition along a mutational pathway with an abrupt protein fold switch.Biophysics of protein evolution and evolutionary protein biophysics

P2860

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P2860

Interconversion between two unrelated protein folds in the lymphotactin native state

http://www.wikidata.org/entity/Q27650152

description

2008 nî lūn-bûn

@nan

2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Interconversion between two unrelated protein folds in the lymphotactin native state

@ast

Interconversion between two unrelated protein folds in the lymphotactin native state

@en

Interconversion between two unrelated protein folds in the lymphotactin native state

@nl

type

label

Interconversion between two unrelated protein folds in the lymphotactin native state

@ast

Interconversion between two unrelated protein folds in the lymphotactin native state

@en

Interconversion between two unrelated protein folds in the lymphotactin native state

@nl

prefLabel

Interconversion between two unrelated protein folds in the lymphotactin native state

@ast

Interconversion between two unrelated protein folds in the lymphotactin native state

@en

Interconversion between two unrelated protein folds in the lymphotactin native state

@nl

P1433

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P356

PNAS.0709518105

P1433

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

P1476

Interconversion between two unrelated protein folds in the lymphotactin native state

@en

P2093

Brian F Volkman

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

E Sonay Elgin

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

Francis C Peterson

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

Michael A Kron

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

Robbyn L Tuinstra

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

Snjezana Kutlesa

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

P2860

Intrinsically unstructured proteins and their functions

Identification of viral macrophage inflammatory protein (vMIP)-II as a ligand for GPR5/XCR1

Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions

A backbone-based theory of protein folding

Monomeric solution structure of the prototypical 'C' chemokine lymphotactin

An Engineered Second Disulfide Bond Restricts Lymphotactin/XCL1 to a Chemokine-like Conformation with XCR1 Agonist Activity †

Refinement of protein structures in explicit solvent

The Xplor-NIH NMR molecular structure determination package

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

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5057-62

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scholarly article

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1665870

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10.1073/PNAS.0709518105

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P407

P433

13

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P478

105

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P577

2008-04-01T00:00:00Z

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P5875

5488857

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P698

18364395

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P921

protein folding

P932

2278211

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