Rationalization of the effects of mutations on peptide and protein aggregation rates. (Q34222395)

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6 November 2019

title

Rationalization of the effects of mutations on peptide and protein aggregation rates (English)

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6 November 2019

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2

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6 November 2019

Niccolo Taddei

series ordinal

3

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6 November 2019

4

Giampietro Ramponi

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6 November 2019

author name string

Fabrizio Chiti

series ordinal

1

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6 November 2019

Christopher M Dobson

series ordinal

5

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6 November 2019

language of work or name

English

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publication date

1 August 2003

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6 November 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12917692%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

volume

424

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6 November 2019

issue

6950

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6 November 2019

page(s)

805-808

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https://scigraph.springernature.com/pub.10.1038/nature01891

6 November 2019

exact match

0 references

cites work

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

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Amyloid fibrillogenesis: themes and variations

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Construction and deconstruction of bacterial inclusion bodies

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Protein misfolding, evolution and disease

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The structure of amyloid fibrils by electron microscopy and X-ray diffraction

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Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein.

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Prevention of transthyretin amyloid disease by changing protein misfolding energetics.

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Kinetic partitioning of protein folding and aggregation.

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Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases

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7 January 2021

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7 January 2021

A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly.

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7 January 2021

Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation

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7 January 2021

S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin

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7 January 2021

The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C).

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7 January 2021

Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy

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7 January 2021

Pathogenic effects of D23N Iowa mutant amyloid beta -protein

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7 January 2021

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation

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https://api.crossref.org/works/10.1038%2FNATURE01891

7 January 2021

Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence

1 reference

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7 January 2021

Tau polymerization: role of the amino terminus

1 reference

https://api.crossref.org/works/10.1038%2FNATURE01891

7 January 2021

In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants

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7 January 2021

Accelerated filament formation from tau protein with specific FTDP-17 missense mutations.

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7 January 2021

Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis

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7 January 2021

X-ray diffraction and far-UV CD studies of filaments formed by a leucine-rich repeat peptide: structural similarity to the amyloid fibrils of prions and Alzheimer's disease beta-protein.

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7 January 2021

Induction of beta-sheet structure in amyloidogenic peptides by neutralization of aspartate: a model for amyloid nucleation.

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7 January 2021

Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone

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7 January 2021

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

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https://api.crossref.org/works/10.1038%2FNATURE01891

7 January 2021

Identifiers

DOI

10.1038/NATURE01891

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12917692%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

6 November 2019

0 references

1 reference