A Bifunctional NAD
Azides
/ chemical synthesis
Click Chemistry
Cross-Linking Reagents
/ chemical synthesis
Diazomethane
/ analogs & derivatives
HEK293 Cells
Humans
NAD
/ chemical synthesis
Poly (ADP-Ribose) Polymerase-1
/ metabolism
Poly ADP Ribosylation
Protein Processing, Post-Translational
Proteome
/ chemistry
Proteomics
Ultraviolet Rays
Journal
ACS chemical biology
ISSN: 1554-8937
Titre abrégé: ACS Chem Biol
Pays: United States
ID NLM: 101282906
Informations de publication
Date de publication:
19 02 2021
19 02 2021
Historique:
pubmed:
2
2
2021
medline:
29
6
2021
entrez:
1
2
2021
Statut:
ppublish
Résumé
Protein poly-ADP-ribosylation (PARylation) is a heterogeneous and dynamic post-translational modification regulated by various writers, readers, and erasers. It participates in a variety of biological events and is involved in many human diseases. Currently, tools and technologies have yet to be developed for unambiguously defining readers and erasers of individual PARylated proteins or cognate PARylated proteins for known readers and erasers. Here, we report the generation of a bifunctional nicotinamide adenine dinucleotide (NAD
Identifiants
pubmed: 33524253
doi: 10.1021/acschembio.0c00937
pmc: PMC7909001
mid: NIHMS1669996
doi:
Substances chimiques
Azides
0
Cross-Linking Reagents
0
Proteome
0
NAD
0U46U6E8UK
Diazomethane
60A625P70P
PARP1 protein, human
EC 2.4.2.30
Poly (ADP-Ribose) Polymerase-1
EC 2.4.2.30
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
389-396Subventions
Organisme : NIDDK NIH HHS
ID : P30 DK048522
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM137901
Pays : United States
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