(Q30165168)

9 June 2017

title

Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils (English)

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9 June 2017

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Salvador Ventura

1

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author name string

Emmanuel Lacroix

series ordinal

2

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9 June 2017

Luis Serrano

series ordinal

3

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9 June 2017

language of work or name

English

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publication date

1 October 2002

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Journal of Molecular Biology

9 June 2017

published in

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9 June 2017

volume

322

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9 June 2017

issue

5

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9 June 2017

page(s)

1147-1158

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https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900783-0

9 June 2017

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From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

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Amyloid fibril formation by an SH3 domain

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Protein misfolding, evolution and disease

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Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy

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The folding kinetics and thermodynamics of the Fyn-SH3 domain.

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Folding dynamics of the src SH3 domain

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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition.

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A thermodynamic analysis of a family of small globular proteins: SH3 domains

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Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain

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The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis

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Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5

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Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques

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Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain

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Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly

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The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.

7 January 2021

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates

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Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation

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An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

7 January 2021

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Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro

7 January 2021

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Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases

7 January 2021

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Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.

7 January 2021

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Protein design based on folding models

7 January 2021

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The SH3-fold family: experimental evidence and prediction of variations in the folding pathways

7 January 2021

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Application of a self-consistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy

7 January 2021

1 reference

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Pairwise calculation of protein solvent-accessible surface areas

7 January 2021

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Solvation energy in protein folding and binding

7 January 2021

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Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.

7 January 2021

1 reference

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Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis

7 January 2021

1 reference

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10.1016/S0022-2836(02)00783-0

7 January 2021

Identifiers

DOI

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9 June 2017

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