(Q77793860)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

title

Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

3

1 reference

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8 December 2019

John Carver

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

author name string

Stephen Poon

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

Teresa M Treweek

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

Simon B Easterbrook-Smith

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

publication date

1 February 2002

1 reference

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8 December 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

volume

513

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

issue

2-3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

page(s)

259-266

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

Do molecular chaperones have to be proteins?

8 December 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Moledular chaperones ten years. Introduction

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Protein aggregation: folding aggregates, inclusion bodies and amyloid

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Clusterin is a secreted mammalian chaperone

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin

7 January 2021

2 references

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

7 January 2021

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

inferred from DOI database lookup

7 January 2021

based on heuristic

Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Kinetics of disulfide bond reduction in alpha-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

The molten globule state of alpha-lactalbumin.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

On the interaction of alpha-crystallin with unfolded proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Effects of Clusterin Overexpression on TNFα- and TGFβ-Mediated Death of L929 Cells†

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

The mode of chaperoning of dithiothreitol-denatured alpha-lactalbumin by alpha-crystallin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

pH-Dependent Changes in the in Vitro Ligand-Binding Properties and Structure of Human Clusterin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

On the substrate specificity of alpha-crystallin as a molecular chaperone

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Structural alterations of alpha-crystallin during its chaperone action

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

Small heat shock proteins inhibit in vitro A beta(1-42) amyloidogenesis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902326-8

10.1016/S0014-5793(02)02326-8

7 January 2021

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11904161%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

1 reference