A family of macrodomain proteins reverses cellular mono-ADP-ribosylation (Q24323450)

Mono-ADP ribosylhydrolase 1

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protein de-ADP-ribosylation

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ADP-ribose 1''-phosphate phosphatase YBR022W

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5

Martin Zacharias

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author name string

Gytis Jankevicius

1

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Markus Hassler

2

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Barbara Golia

3

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Vladimir Rybin

4

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Gyula Timinszky

6

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Andreas G Ladurner

Nature Structural & Molecular Biology

7

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language of work or name

English

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publication date

April 2013

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published in

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volume

20

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page(s)

508-14

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issue

4

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cites work

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

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SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells

20 April 2017

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PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1

20 April 2017

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

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A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation

20 April 2017

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A biochemical genomics approach for identifying genes by the activity of their products.

20 April 2017

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Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases

20 April 2017

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Orphan macrodomain protein (human C6orf130) is an O-acyl-ADP-ribose deacylase: solution structure and catalytic properties

20 April 2017

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

20 April 2017

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

20 April 2017

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The macro domain is an ADP-ribose binding module

20 April 2017

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Substrate-assisted catalysis: molecular basis and biological significance

20 April 2017

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Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains

20 April 2017

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Scaling and assessment of data quality

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MolProbity: all-atom structure validation for macromolecular crystallography

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

20 April 2017

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

20 April 2017

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A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins.

21 January 2018

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PARP1 ADP-ribosylates lysine residues of the core histone tails

21 January 2018

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

21 January 2018

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

21 January 2018

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Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications

21 January 2018

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

21 January 2018

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Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes

21 January 2018

1 reference

Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome

21 January 2018

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Sensing NAD metabolites through macro domains

21 January 2018

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Splicing regulates NAD metabolite binding to histone macroH2A.

21 January 2018

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Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites

21 January 2018

1 reference

Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.

21 January 2018

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Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3.

21 January 2018

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Reverse transfection on cell arrays for high content screening microscopy.

21 January 2018

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A new method for oligo (ADP-ribose) fractionation according to chain length

21 January 2018

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Glycation and glycoxidation of histones by ADP-ribose

31 March 2020

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

31 March 2020

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23474712

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NSMB.2523

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

1240978

1020758140

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1240978

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference