Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities (Q27679375)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23917065%20AND%20SRC:MED&resulttype=core&format=json

6 March 2020

title

Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities (English)

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6 March 2020

1 reference

4

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6 March 2020

Pierre Lafite

7

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6 March 2020

author name string

Eva Barkauskaite

1

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6 March 2020

Amy Brassington

2

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6 March 2020

Edwin S Tan

3

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6 March 2020

Mark S Dunstan

5

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6 March 2020

Benito Banos

6

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6 March 2020

Marijan Ahel

8

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6 March 2020

Timothy J Mitchison

9

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6 March 2020

Ivan Ahel

10

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6 March 2020

David Leys

11

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6 March 2020

language of work or name

English

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publication date

1 January 2013

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6 March 2020

published in

Nature Communications

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6 March 2020

volume

4

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6 March 2020

page(s)

2164

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Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported

6 March 2020

copyright license

start time

6 August 2013

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease

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Structures of the Human Poly (ADP-Ribose) Glycohydrolase Catalytic Domain Confirm Catalytic Mechanism and Explain Inhibition by ADP-HPD Derivatives

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Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase

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Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element

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The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

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Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions

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Regulation of chromatin structure by poly(ADP-ribosyl)ation

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Large-scale preparation and characterization of poly(ADP-ribose) and defined length polymers

29 September 2017

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New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs

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The role of ADP-ribosylation in regulating DNA double-strand break repair

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Poly(ADP-ribose) makes a date with death

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ART2, a T cell surface mono-ADP-ribosyltransferase, generates extracellular poly(ADP-ribose).

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

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PubMed

https://pubmed.ncbi.nlm.nih.gov/23917065

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

ADP-ribosyl protein lyase. Purification, properties, and identification of the product

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PubMed

https://pubmed.ncbi.nlm.nih.gov/23917065

inferred from PubMed ID database lookup

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based on heuristic

Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS3164

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NCOMMS3164

2 references

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Dimensions Publication ID

6 March 2020

ADS bibcode

2013NatCo...4.2164B

0 references

1010588773

0 references

1 reference

2 references

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6 March 2020

2 references

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