Activation of the abundant nuclear factor poly(ADP-ribose) polymerase-1 by Helicobacter pylori (Q24648738)

2

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Batcha Tamilselvam

3

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Vijay R Gupta

4

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Lin-Feng Chen

5

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Valérie Schreiber

6

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Serge Desnoyers

7

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Steven R Blanke

Proceedings of the National Academy of Sciences of the United States of America

8

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language of work or name

English

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publication date

24 November 2009

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published in

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volume

106

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issue

47

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page(s)

19998-20003

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describes a project that uses

ImageJ

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2785281/fullTextXML

inferred from PubMed Central ID database lookup

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Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

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Parthanatos, a messenger of death

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The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases.

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Modification of a mammalian cell protein in the presence of [32P-adenylate]NAD: evidence for ADP ribosylation activity associated with Helicobacter pylori

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Helicobacter pylori induces apoptosis of T- and B-cell lines and translocates mitochondrial apoptosis-inducing factor to nucleus

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The abundant nuclear enzyme PARP participates in the life cycle of simian virus 40 and is stimulated by minor capsid protein VP3.

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Helicobacter pyloriInfection

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Purification and characterization of native conventional kinesin, HSET, and CENP-E from mitotic hela cells

21 January 2018

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DNA-independent PARP-1 activation by phosphorylated ERK2 increases Elk1 activity: a link to histone acetylation

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Single amino acid substitution enhances bacterial expression of PARP-4D214A

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12 December 2020

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

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12 December 2020

Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular

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12 December 2020

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12 December 2020

The family of bacterial ADP-ribosylating exotoxins

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7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1073/PNAS.0906753106

1 reference

ADS bibcode

2009PNAS..10619998N

0 references

1 reference

1 reference

PubMed publication ID

19897724

1 reference