Single homopolypeptide chains collapse into mechanically rigid conformations. - Test2 - elhamkhani - TriplyDB

Single homopolypeptide chains collapse into mechanically rigid conformations.

Single homopolypeptide chains collapse into mechanically rigid conformations.

http://www.wikidata.org/entity/Q37293354

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Fibrillogenesis of huntingtin and other glutamine containing proteins Disease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact Structure Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10 Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes Common features at the start of the neurodegeneration cascade Trinucleotide repeats: a structural perspective Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansion Describing sequence-ensemble relationships for intrinsically disordered proteins.Net charge per residue modulates conformational ensembles of intrinsically disordered proteins Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool.Are long-range structural correlations behind the aggregration phenomena of polyglutamine diseases?Single molecule force spectroscopy using polyproteins.Aggregation kinetics of interrupted polyglutamine peptides Design of symmetric TIM barrel proteins from first principles.Sequence-dependent stability test of a left-handed β-helix motif.Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.Structural Characterization of λ-Repressor Folding from All-Atom Molecular Dynamics Simulations Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions Conformation sensors that distinguish monomeric proteins from oligomers in live cells.Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein Analysis of the REJ Module of Polycystin-1 Using Molecular Modeling and Force-Spectroscopy Techniques Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation.A platform to view huntingtin exon 1 aggregation flux in the cell reveals divergent influences from chaperones hsp40 and hsp70.C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins.Understanding biology by stretching proteins: recent progress.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils.Emerging β-Sheet Rich Conformations in Supercompact Huntingtin Exon-1 Mutant Structures.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Atomic force microscopy studies of bioprocess engineering surfaces - imaging, interactions and mechanical properties mediating bacterial adhesion.Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin.A strategy for analyzing bond strength and interaction kinetics between Pleckstrin homology domains and PI(4,5)P2 phospholipids using force distance spectroscopy and surface plasmon resonance.Complex unfolding kinetics of single-domain proteins in the presence of force Protease power strokes force proteins to unfold.Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent Effect of αB-crystallin on protein aggregation in Drosophila.Transitions of tethered chain molecules under tension.Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering.

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P2860

Single homopolypeptide chains collapse into mechanically rigid conformations.

http://www.wikidata.org/entity/Q37293354

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 19 June 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Single homopolypeptide chains collapse into mechanically rigid conformations.

@en

Single homopolypeptide chains collapse into mechanically rigid conformations.

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Single homopolypeptide chains collapse into mechanically rigid conformations.

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type

label

Single homopolypeptide chains collapse into mechanically rigid conformations.

@en

Single homopolypeptide chains collapse into mechanically rigid conformations.

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Single homopolypeptide chains collapse into mechanically rigid conformations.

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prefLabel

Single homopolypeptide chains collapse into mechanically rigid conformations.

@en

Single homopolypeptide chains collapse into mechanically rigid conformations.

@en-gb

Single homopolypeptide chains collapse into mechanically rigid conformations.

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PNAS.0900678106

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

P1476

Single homopolypeptide chains collapse into mechanically rigid conformations.

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P2093

B J Berne

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

Carmen L Badilla

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

Julio M Fernandez

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

P2860

Molecular origin of polyglutamine aggregation in neurodegenerative diseases.

Entropic elasticity of lambda-phage DNA

How does a protein fold?

Impairment of the ubiquitin-proteasome system by protein aggregation

Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice

Forces of tertiary structural organization in globular proteins.

Contour length and refolding rate of a small protein controlled by engineered disulfide bonds.

Stepwise unfolding of ankyrin repeats in a single protein revealed by atomic force microscopy.

Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

Functional insights from the distribution and role of homopeptide repeat-containing proteins

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12605-12610

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scholarly article

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10.1073/PNAS.0900678106

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31

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106

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2009-06-19T00:00:00Z

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26314278

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19549822

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2722357

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