Probing the instabilities in the dynamics of helical fragments from mouse PrPC. - Wikidata - awgldk - TriplyDB

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

http://www.wikidata.org/entity/Q37593382

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Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires Crystal structure of human prion protein bound to a therapeutic antibody Prion Fibrillization Is Mediated by a Native Structural Element That Comprises Helices H2 and H3 Unique Structural Characteristics of the Rabbit Prion Protein Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations The dominant-negative effect of the Q218K variant of the prion protein does not require protein X.Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.Association thermodynamics and conformational stability of beta-sheet amyloid beta(17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralization Structural and dynamic properties of the human prion protein.Principles governing oligomer formation in amyloidogenic peptides.Influence of pH on the human prion protein: insights into the early steps of misfolding.Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions: a replica exchange molecular dynamics study.The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPSc Role of water in protein aggregation and amyloid polymorphism.Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange Strand swapping regulates the iron-sulfur cluster in the diabetes drug target mitoNEET Mutations as trapdoors to two competing native conformations of the Rop-dimer Effects of disulfide bond formation and protein helicity on the aggregation of activating transcription factor 5 Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.NMR structure and CD titration with metal cations of human prion alpha2-helix-related peptides.Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition Mouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism.The reconstitution of mammalian prion infectivity de novo.Hydration effects on the HET-s prion and amyloid-beta fibrillous aggregates, studied with three-dimensional molecular theory of solvation Factors governing helix formation in peptides confined to carbon nanotubes.Direct single-molecule observation of a protein living in two opposed native structures.The consequences of pathogenic mutations to the human prion protein.Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysis Prion proteins with pathogenic and protective mutations show similar structure and dynamics.Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins.Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements Left handed beta helix models for mammalian prion fibrils.Structural and hydration properties of the partially unfolded states of the prion protein.Massive conformation change in the prion protein: Using dual-basin structure-based models to find misfolding pathways.Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.β-sheet-like formation during the mechanical unfolding of prion protein.

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Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

http://www.wikidata.org/entity/Q37593382

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on 19 October 2004

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@en

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@nl

type

label

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@en

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@nl

prefLabel

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@en

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@nl

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PNAS.0404235101

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

P1476

Probing the instabilities in the dynamics of helical fragments from mouse PrPC.

@en

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D Thirumalai

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

Ruxandra I Dima

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P2860

NMR solution structure of the human prion protein

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus

NMR structure of the mouse prion protein domain PrP(121-231)

VMD: visual molecular dynamics

ASTRAL compendium enhancements.

Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

Development and current status of the CHARMM force field for nucleic acids.

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15335-15340

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10.1073/PNAS.0404235101

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