(Q45195856)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15611128%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

title

Investigating the effects of mutations on protein aggregation in the cell (English)

1 reference

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6 January 2020

1 reference

1

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6 January 2020

Massimo Stefani

3

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6 January 2020

author name string

Sara Zoffoli

2

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6 January 2020

Fabrizio Chiti

5

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6 January 2020

Christopher M Dobson

4

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6 January 2020

language of work or name

English

0 references

publication date

16 December 2004

1 reference

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Journal of Biological Chemistry

6 January 2020

published in

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6 January 2020

volume

280

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6 January 2020

page(s)

10607-10613

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6 January 2020

issue

11

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Folding proteins in fatal ways

6 January 2020

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

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Protein folding and misfolding

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

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De novo amyloid proteins from designed combinatorial libraries

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Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology

21 January 2018

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Conformational constraints for amyloid fibrillation: the importance of being unfolded

21 January 2018

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Amyloid fibrillogenesis: themes and variations

21 January 2018

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A role for destabilizing amino acid replacements in light-chain amyloidosis

21 January 2018

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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

21 January 2018

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Mutational analysis of the propensity for amyloid formation by a globular protein

21 January 2018

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

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Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity

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A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation

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

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Protein engineering as a strategy to avoid formation of amyloid fibrils

21 January 2018

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

21 January 2018

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Kinetic partitioning of protein folding and aggregation.

21 January 2018

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

21 January 2018

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De novo designed peptide-based amyloid fibrils

21 January 2018

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Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides

21 January 2018

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

21 January 2018

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Rational design of potent human transthyretin amyloid disease inhibitors

21 January 2018

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Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation

21 January 2018

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Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization

21 January 2018

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Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question.

21 January 2018

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21 January 2018

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Protein degradation and protection against misfolded or damaged proteins

21 January 2018

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Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

21 January 2018

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Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils.

21 January 2018

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Expression, purification, and characterization of acylphosphatase muscular isoenzyme as fusion protein with glutathione S-transferase.

21 January 2018

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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

21 January 2018

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21 January 2018

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Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

21 January 2018

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Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.

21 January 2018

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21 January 2018

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21 January 2018

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Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding.

21 January 2018

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Genetic screens and directed evolution for protein solubility

21 January 2018

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Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants

21 January 2018

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Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M412951200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15611128%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

1 reference