(Q28235199)

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

From computer simulations to human disease: emerging themes in protein folding

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Protein Folding: A Perspective from Theory and Experiment.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Navigating the folding routes

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

From Levinthal to pathways to funnels

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Matching speed and stability

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Absolute comparison of simulated and experimental protein-folding dynamics

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Folding at the speed limit

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

The complete folding pathway of a protein from nanoseconds to microseconds

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Protein folding and unfolding at atomic resolution

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

A surprising simplicity to protein folding.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Kinetic role of early intermediates in protein folding

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

The kinetic pathway of folding of barnase

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Structures and relative free energies of partially folded states of proteins

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Folding of a nascent peptide on the ribosome

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

The Hsp70 and Hsp60 chaperone machines

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https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Enzymes that catalyse the restructuring of proteins

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Quality control in the secretory pathway

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

The unfolded protein response in nutrient sensing and differentiation

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Clusterin is a secreted mammalian chaperone

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Impairment of the ubiquitin-proteasome system by protein aggregation

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Defective protein folding as a basis of human disease

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Rescuing the function of mutant p53.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

https://api.crossref.org/works/10.1038%2FNATURE02261

1 reference

7 January 2021

The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Protein misfolding, evolution and disease

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Rationalization of the effects of mutations on peptide and protein aggregation rates.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Neurodegenerative disease: amyloid pores from pathogenic mutations

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Protein folding and disease: a view from the first Horizon Symposium.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Role of Escherichia coli curli operons in directing amyloid fiber formation

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Amyloid as a natural product

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Kinetic partitioning of protein folding and aggregation.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Sick chaperones and ageing: a perspective

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Prion Diseases and the BSE Crisis

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Toxic proteins in neurodegenerative disease

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02261

7 January 2021

https://api.crossref.org/works/10.1038%2FNATURE02261

1 reference

7 January 2021