ADP-ribosylation of histones by ARTD1: an additional module of the histone code? (Q37855198)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21420964 AND SRC:MED&resulttype=core&format=json

26 January 2020

review article

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title

ADP-ribosylation of histones by ARTD1: an additional module of the histone code? (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21420964 AND SRC:MED&resulttype=core&format=json

26 January 2020

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21420964 AND SRC:MED&resulttype=core&format=json

26 January 2020

author name string

Michael O Hottiger

series ordinal

1

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24 August 2017

language of work or name

English

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publication date

21 March 2011

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21420964 AND SRC:MED&resulttype=core&format=json

26 January 2020

number of pages

5

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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26 January 2020

volume

585

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21420964 AND SRC:MED&resulttype=core&format=json

26 January 2020

issue

11

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26 January 2020

page(s)

1595-1599

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

26 January 2020

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PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

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Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation.

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Natural occurrence of poly(ADP-ribosyl) histones in rat liver

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