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

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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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26 January 2020

1

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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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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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volume

585

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issue

11

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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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DNA strand breaks alter histone ADP-ribosylation

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Properties of the Complex between Histone H1 and Poly(ADP-ribose) Synthesised in HeLa Cell Nuclei

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Nuclear protein modification and chromatin substructure. 1. Differential poly(adenosine diphosphate) ribosylation of chromosomal proteins in nuclei versus isolated nucleosomes

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Nuclear protein modification and chromatin substructure. 3. Relationship between poly(adenosine diphosphate) ribosylation and different functional forms of chromatin

21 January 2018

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Poly ADP-ribose polymerase: Self-ADP-ribosylation, the stimulation by DNA, and the effects on nucleosome formation and stability

21 January 2018

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PARP1 ADP-ribosylates lysine residues of the core histone tails

21 January 2018

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Large-scale mapping of human protein-protein interactions by mass spectrometry

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PARP-3 and APLF function together to accelerate nonhomologous end-joining

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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.

21 January 2018

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Electron transfer dissociation facilitates sequencing of adenosine diphosphate-ribosylated peptides

21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

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26 January 2020

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