Protein folding and misfolding (Q28235199)

Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems

Europe PubMed Central

title

Protein folding and misfolding (English)

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1

Christopher M Dobson

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language of work or name

English

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publication date

18 December 2003

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published in

Nature

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volume

426

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issue

6968

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page(s)

884-90

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cites work

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From Levinthal to pathways to funnels

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Understanding protein folding via free-energy surfaces from theory and experiment

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Matching speed and stability

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Absolute comparison of simulated and experimental protein-folding dynamics

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Folding at the speed limit

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The complete folding pathway of a protein from nanoseconds to microseconds

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Contact order, transition state placement and the refolding rates of single domain proteins.

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Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

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Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism

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Three key residues form a critical contact network in a protein folding transition state

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The topomer search model: A simple, quantitative theory of two-state protein folding kinetics

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A surprising simplicity to protein folding.

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Kinetic role of early intermediates in protein folding

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Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding

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Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse

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Folding of a nascent peptide on the ribosome

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The Hsp70 and Hsp60 chaperone machines

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Molecular chaperones in the cytosol: from nascent chain to folded protein

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Macromolecular crowding: an important but neglected aspect of the intracellular environment

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Enzymes that catalyse the restructuring of proteins

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Quality control in the secretory pathway

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Clusterin is a secreted mammalian chaperone

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Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.

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Impairment of the ubiquitin-proteasome system by protein aggregation

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Defective protein folding as a basis of human disease

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The structural basis of protein folding and its links with human disease

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Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions

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Rescuing the function of mutant p53.

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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

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Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Prion diseases and the BSE crisis

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Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils

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Chaperone overload is a possible contributor to 'civilization diseases'.

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Identifiers

DOI

10.1038/NATURE02261

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

936924

1044990439

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936924

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference