(Q28247808)

English

Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation

scientific article (publication date: 7 November 2014)

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scholarly article

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Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation (English)

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molecular chaperones

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7

object named as

Christopher M Dobson

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Rasha M Hussein

object named as

Rasha Hussein

3

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object named as

Reem M Hashem

5

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Harm H Kampinga

object named as

Harm H Kampinga

4

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Sara Snogerup Linse

object named as

Sara Linse

9

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author name string

Cecilia Månsson

1

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Paolo Arosio

2

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Wilbert C Boelens

6

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Tuomas P J Knowles

8

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Cecilia Emanuelsson

10

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language of work or name

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publication date

7 November 2014

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Journal of Biological Chemistry

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289

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45

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31066-76

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The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides

1 reference

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

1 reference

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20 March 2017

Protein misfolding, functional amyloid, and human disease

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20 March 2017

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6 April 2017

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

1 reference

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Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease

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Quantitation of protein

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Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones

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

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Charge dependent retardation of amyloid β aggregation by hydrophilic proteins

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1 reference

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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

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Assembly chaperones: a perspective

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1 reference

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12 December 2020

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