Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins.
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Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperoneN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneityMechanism of Protein Kinetic Stabilization by Engineered Disulfide CrosslinksA multiparametric computational algorithm for comprehensive assessment of genetic mutations in mucopolysaccharidosis type IIIA (Sanfilippo syndrome)From conformational chaos to robust regulation: the structure and function of the multi-enzyme RNA degradosomeOn the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses.The evolution of protein structures and structural ensembles under functional constraint.Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric statesNonnative interactions in coupled folding and binding processes of intrinsically disordered proteins.An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.Functional interactions as a survival strategy against abnormal aggregationInduced fit, conformational selection and independent dynamic segments: an extended view of binding eventsTranslationally optimal codons associate with aggregation-prone sites in proteins.Evolutionary capacitance and control of protein stability in protein-protein interaction networks.Slow protein evolutionary rates are dictated by surface-core association.Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicityLocal slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo.Optimization of Codon Translation Rates via tRNA Modifications Maintains Proteome Integrity.Strong Enrichment of Aromatic Residues in Binding Sites from a Charge-neutralized Hyperthermostable Sso7d Scaffold Library.Biochemical nature of Russell Bodies.Cellular crowding imposes global constraints on the chemistry and evolution of proteomes.Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Cellular strategies for regulating functional and nonfunctional protein aggregation.Non-random distribution of homo-repeats: links with biological functions and human diseases.NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.Computational design of self-assembling cyclic protein homo-oligomers.Strategies for protein synthetic biology.Evolutionary selection for protein aggregation.Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.Autoimmune Responses to Soluble Aggregates of Amyloidogenic Proteins Involved in Neurodegenerative Diseases: Overlapping Aggregation Prone and Autoimmunogenic regions.Understanding and predicting protein misfolding and aggregation: Insights from proteomics.Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.Distinct stress conditions result in aggregation of proteins with similar properties.Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.Disulfide bonding in neurodegenerative misfolding diseases.Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold.Rational design of viscosity reducing mutants of a monoclonal antibody: hydrophobic versus electrostatic inter-molecular interactions.
P2860
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P2860
Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 05 June 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Physicochemical principles tha ...... ional association of proteins.
@en
Physicochemical principles tha ...... ional association of proteins.
@nl
type
label
Physicochemical principles tha ...... ional association of proteins.
@en
Physicochemical principles tha ...... ional association of proteins.
@nl
prefLabel
Physicochemical principles tha ...... ional association of proteins.
@en
Physicochemical principles tha ...... ional association of proteins.
@nl
P2860
P50
P356
P1476
Physicochemical principles tha ...... ional association of proteins.
@en
P2093
Sebastian Pechmann
P2860
P304
10159-10164
P356
10.1073/PNAS.0812414106
P407
P577
2009-06-05T00:00:00Z