Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice (Q34231667)

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3 January 2020

title

Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice (English)

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3 January 2020

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4

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Ron M. Peshock

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author name string

Namakkal S Rajasekaran

1

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Patrice Connell

2

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Elisabeth S Christians

3

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Ryan P Taylor

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András Orosz

6

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Xiu Q Zhang

7

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Tamara J Stevenson

8

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Jane A Leopold

10

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William H Barry

11

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Shannon J Odelberg

13

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Ivor J Benjamin

14

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Joseph Loscalzo

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language of work or name

English

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publication date

1 August 2007

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volume

130

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issue

3

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3 January 2020

page(s)

427-439

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Aldosterone impairs vascular reactivity by decreasing glucose-6-phosphate dehydrogenase activity

3 January 2020

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The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.

6 July 2018

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Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function

6 July 2018

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6 July 2018

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12 December 2020

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12 December 2020

10.1016/J.CELL.2007.06.044

Identifiers

DOI

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3 January 2020

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3 January 2020

PubMed publication ID

17693254

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