The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1
Open accessAbstract
Dissecting DNA Repair: Covalent modification of proteins can be a crucial regulatory event. Poly(ADP-ribose) polymerase 1 (PARP-1) (ADP, adenosine diphosphate) synthesizes poly(ADP-ribose), which is attached to and regulates proteins involved in DNA repair. Langelier et al. (p. 728 ; see the Perspective by Gagné et al. ) use x-ray crystallography and biochemical analysis to demonstrate how PARP-1 detects DNA damage and how the interaction with DNA is coupled to poly(ADP-ribosyl)ation activity.
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Cited by
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
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“Moreover, while PARP-2 and PARP-3 share the allosteric activation mechanismwith PARP-1, they require 5′ phosphorylation at the DNA breaks for activation, unlike PARP-1 (Langelier et al. 2014).”
BackgroundPARP and PARG inhibitors in cancer treatment
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Metadata
- Authors
- Langelier, M.-F., Planck, J. L., Roy, S., & Pascal, J. M.
- Venue
- Science
- Published
- 2012-05-11
- Volume
- 336
- Issue
- 6082
- Pages
- 728-732
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2073660843
- Cited by
- 665
- References
- 45
- FWCI
- 14.17
- Type
- journal article
- Language
- en
- Open access
- green
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- Langelier, M.-F., Planck, J. L., Roy, S., & Pascal, J. M. (2012). Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1. Science. https://doi.org/10.1126/science.1216338
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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