ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). (Q35956444)

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English	ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose).	scientific article

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scholarly article

1 reference

Europe PubMed Central

11 August 2017

ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). (English)

1 reference

Europe PubMed Central

11 August 2017

Mathias Ziegler

8

object named as

Mathias Ziegler

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Europe PubMed Central

11 August 2017

7

object named as

Joel Moss

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Europe PubMed Central

11 August 2017

author name string

Marc Niere

1

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Europe PubMed Central

11 August 2017

Masato Mashimo

2

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Europe PubMed Central

11 August 2017

Line Agledal

3

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Europe PubMed Central

11 August 2017

Christian Dölle

4

1 reference

Europe PubMed Central

11 August 2017

Atsushi Kasamatsu

5

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Europe PubMed Central

11 August 2017

Jiro Kato

6

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Europe PubMed Central

11 August 2017

language of work or name

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publication date

20 March 2012

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Europe PubMed Central

11 August 2017

number of pages

15

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Journal of Biological Chemistry

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Europe PubMed Central

11 August 2017

287

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11 August 2017

20

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11 August 2017

16088-16102

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Europe PubMed Central

11 August 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3351285/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

Identification of a regulatory segment of poly(ADP-ribose) glycohydrolase.

1 reference

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1 reference

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Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix

1 reference

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Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death

1 reference

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The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases

1 reference

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1 reference

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Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?

1 reference

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PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery.

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Poly(ADP-ribose): novel functions for an old molecule

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Poly(ADP-ribose) polymerase-1 activation during DNA damage and repair

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Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage

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Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase

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Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?

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Failure to degrade poly(ADP-ribose) causes increased sensitivity to cytotoxicity and early embryonic lethality

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Depletion of the 110-kilodalton isoform of poly(ADP-ribose) glycohydrolase increases sensitivity to genotoxic and endotoxic stress in mice

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The PARP superfamily

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Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments

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Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes

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The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase

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1 reference

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Visualization of subcellular NAD pools and intra-organellar protein localization by poly-ADP-ribose formation

1 reference

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Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo

1 reference

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Identifiers

10.1074/JBC.M112.349183

1 reference

Europe PubMed Central

11 August 2017

1 reference

Europe PubMed Central

11 August 2017

1 reference

Europe PubMed Central

11 August 2017

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