Prion proteins with pathogenic and protective mutations show similar structure and dynamics.
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Unique Structural Characteristics of the Rabbit Prion ProteinNMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural FeaturesSolution Structure and Dynamics of the I214V Mutant of the Rabbit Prion ProteinUse of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins.Considering protonation as a posttranslational modification regulating protein structure and function.PrP overdrive: does inhibition of α-cleavage contribute to PrP(C) toxicity and prion disease?Separating instability from aggregation propensity in γS-crystallin variants.Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transitionZinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interfacePrediction of the rotational tumbling time for proteins with disordered segments.Protein functional landscapes, dynamics, allostery: a tortuous path towards a universal theoretical framework.Interplay of buried histidine protonation and protein stability in prion misfolding.Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Acid-induced molten globule state of a prion protein: crucial role of Strand 1-Helix 1-Strand 2 segment.Exploring the essential collective dynamics of interacting proteins: application to prion protein dimers.3D-RISM-KH approach for biomolecular modelling at nanoscale: thermodynamics of fibril formation and beyondStructural basis for the complete resistance of the human prion protein mutant G127V to prion disease
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P2860
Prion proteins with pathogenic and protective mutations show similar structure and dynamics.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on September 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Prion proteins with pathogenic ...... imilar structure and dynamics.
@en
Prion proteins with pathogenic ...... imilar structure and dynamics.
@nl
type
label
Prion proteins with pathogenic ...... imilar structure and dynamics.
@en
Prion proteins with pathogenic ...... imilar structure and dynamics.
@nl
prefLabel
Prion proteins with pathogenic ...... imilar structure and dynamics.
@en
Prion proteins with pathogenic ...... imilar structure and dynamics.
@nl
P2860
P50
P356
P1433
P1476
Prion proteins with pathogenic ...... imilar structure and dynamics.
@en
P2093
Ana Serban
Sung-Hun Bae
P2860
P304
P356
10.1021/BI900923B
P407
P577
2009-09-01T00:00:00Z