Caspase-1 and caspase-8 cleave and inactivate cellular parkin (Q73262534)

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2 November 2019

title

Caspase-1 and caspase-8 cleave and inactivate cellular parkin (English)

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2 November 2019

5

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2 November 2019

Poul Henning Jensen

6

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2 November 2019

author name string

Soren Kahns

1

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2 November 2019

Michael Kalai

2

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2 November 2019

Lene Diness Jakobsen

3

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2 November 2019

Brian F C Clark

4

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2 November 2019

language of work or name

English

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publication date

11 April 2003

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Journal of Biological Chemistry

2 November 2019

number of pages

5

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based on heuristic

inferred from page(s)

published in

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2 November 2019

volume

278

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2 November 2019

issue

26

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2 November 2019

page(s)

23376-23380

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Parkinson's disease. First of two parts

2 November 2019

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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

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Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity

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Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

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Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease

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Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

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An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin

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Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress

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Caspase-mediated parkin cleavage in apoptotic cell death.

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Characterization of seven murine caspase family members.

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Molecular cloning and identification of murine caspase-8.

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A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis

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Target protease specificity of the viral serpin CrmA. Analysis of five caspases

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Inhibition of death receptor signals by cellular FLIP

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Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes

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The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases

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Translation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylation

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Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis

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Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

21 January 2018

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Immunohistochemical and subcellular localization of Parkin protein: absence of protein in autosomal recessive juvenile parkinsonism patients

21 January 2018

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Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodies

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21 January 2018

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Identifiers

DOI

10.1074/JBC.M300495200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12692130%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

1 reference