Peptidase activities of the multicatalytic protease in rat liver after voluntary and intragastric ethanol administration. (Q47720313)

5 February 2018

title

Peptidase activities of the multicatalytic protease in rat liver after voluntary and intragastric ethanol administration. (English)

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5 February 2018

author name string

Donohue TM Jr

1

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5 February 2018

Zetterman RK

2

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5 February 2018

Zhang-Gouillon ZQ

3

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5 February 2018

French SW

4

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5 February 2018

language of work or name

English

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publication date

1 August 1998

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5 February 2018

published in

Hepatology

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5 February 2018

volume

28

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5 February 2018

page(s)

486-491

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5 February 2018

issue

2

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5 February 2018

Inflammation, free radicals, and antioxidants

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Glycosylation enhances malondialdehyde binding to proteins

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4-hydroxynonenal inhibits Na(+)-K(+)-ATPase

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Zonal distribution of protein-acetaldehyde adducts in the liver of rats fed alcohol for long periods

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Acetaldehyde and malondialdehyde react together to generate distinct protein adducts in the liver during long-term ethanol administration

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Covalent binding of acetaldehyde selectively inhibits the catalytic activity of lysine-dependent enzymes

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Selective protein degradation: a journey's end within the proteasome

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Ubiquitin in health and disease.

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Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome.

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Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome.

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The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

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Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1

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Identifiers

DOI

10.1002/HEP.510280228

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5 February 2018

PubMed ID

9696015

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5 February 2018