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Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
scientific article published on 18 May 2017
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Europe PubMed Central
PMC publication ID
5499872
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
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20 March 2020
title
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
(English)
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stated in
Europe PubMed Central
PMC publication ID
5499872
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
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20 March 2020
main subject
glycosylation
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author
Ivan Matic
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3
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Europe PubMed Central
PMC publication ID
5499872
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
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20 March 2020
Juan José Bonfiglio
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1
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Europe PubMed Central
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5499872
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20 March 2020
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Thomas Colby
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2
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5499872
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20 March 2020
publication date
1 June 2017
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20 March 2020
published in
Nucleic Acids Research
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Europe PubMed Central
PMC publication ID
5499872
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
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20 March 2020
volume
45
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Europe PubMed Central
PMC publication ID
5499872
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
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20 March 2020
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11
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Europe PubMed Central
PMC publication ID
5499872
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20 March 2020
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6259-6264
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5499872
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retrieved
20 March 2020
copyright license
Creative Commons Attribution-NonCommercial 4.0 International
start time
18 May 2017
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April 2022 Public Data File from Crossref
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0 references
cites work
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
1 reference
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PubMed Central
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25 September 2017
Serine ADP-Ribosylation Depends on HPF1
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25 September 2017
Serine is a new target residue for endogenous ADP-ribosylation on histones.
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Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue.
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25 September 2017
Expanding functions of ADP-ribosylation in the maintenance of genome integrity
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Mass-spectrometric exploration of proteome structure and function
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New directions in poly(ADP-ribose) polymerase biology
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The Promise of Proteomics for the Study of ADP-Ribosylation
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25 September 2017
Quantitative site-specific ADP-ribosylation profiling of DNA-dependent PARPs
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Processing of protein ADP-ribosylation by Nudix hydrolases
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25 September 2017
Molecular perspectives on protein adenylylation
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25 September 2017
Proteomics approaches to identify mono-(ADP-ribosyl)ated and poly(ADP-ribosyl)ated proteins.
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25 September 2017
Family-wide analysis of poly(ADP-ribose) polymerase activity
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25 September 2017
Phosphoproteomic approach to characterize protein mono- and poly(ADP-ribosyl)ation sites from cells.
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Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease
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Vertebrate protein glycosylation: diversity, synthesis and function
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Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse
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A Review of Tandem Mass Spectrometry Characterization of Adenosine Diphosphate-Ribosylated Peptides
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Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets
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Proteomic and phosphoproteomic comparison of human ES and iPS cells
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Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines
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PARP1 ADP-ribosylates lysine residues of the core histone tails
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Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications
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Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry
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25 September 2017
Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
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Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics
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New Quantitative Mass Spectrometry Approaches Reveal Different ADP-ribosylation Phases Dependent On the Levels of Oxidative Stress.
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Nudix hydrolases degrade protein-conjugated ADP-ribose
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Chromatin to Clinic: The Molecular Rationale for PARP1 Inhibitor Function
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Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sites
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Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites
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Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
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Electron transfer dissociation facilitates sequencing of adenosine diphosphate-ribosylated peptides
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Precursor ion scanning and sequencing of arginine-ADP-ribosylated peptide by mass spectrometry.
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19 August 2018
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Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
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Identifiers
DOI
10.1093/NAR/GKX446
1 reference
stated in
Europe PubMed Central
PMC publication ID
5499872
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
retrieved
20 March 2020
PMC publication ID
5499872
1 reference
stated in
Europe PubMed Central
PMC publication ID
5499872
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
retrieved
20 March 2020
PubMed publication ID
28520971
1 reference
stated in
Europe PubMed Central
PMC publication ID
5499872
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28520971%20AND%20SRC:MED&resulttype=core&format=json
retrieved
20 March 2020
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