Associated Papers
PARG is essential for Polθ-mediated DNA end-joining by removing repressive poly-ADP-ribose marks.
Vekariya U et al.
Nature Communications, 2024
Poly(ADP-ribosylation) of P-TEFb by PARP1 disrupts phase separation to inhibit global transcription after DNA damage.
Fu H et al.
Nature Cell Biology, 2022
An assessment of poly (ADP-ribose) polymerase-1 role in normal and cancer cells.
Kumar M et al.
Biofactors (oxford, England), 2020
DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination.
Ahmed SF et al.
Science Advances, 2020
HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.
Suskiewicz MJ et al.
Nature, 2020
Poly(ADP-ribose) polymerase enzymes and the maintenance of genome integrity.
Eisemann T et al.
Cellular and Molecular Life Sciences : Cmls, 2020
Structural and functional analysis of parameters governing tankyrase-1 interaction with telomeric repeat-binding factor 1 and GDP-mannose 4,6-dehydratase.
Eisemann T et al.
The Journal of Biological Chemistry, 2019
MORC2 regulates DNA damage response through a PARP1-dependent pathway.
Zhang L et al.
Nucleic Acids Research, 2019
31616951 (PubMed )
Supplement: gkz545_supplemental_file.pdf
Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry.
Li P et al.
Methods in Enzymology, 2019
Serine ADP-ribosylation reversal by the hydrolase ARH3.
Fontana P et al.
Elife, 2017
Structural and functional analysis of Oceanobacillus iheyensis macrodomain reveals a network of waters involved in substrate binding and catalysis.
Zapata-Pérez R et al.
Open Biology, 2017
Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.
Barkauskaite E et al.
Nature Communications, 2013
Towards a structural understanding of PARP1 activation and related signalling ADP-ribosyl-transferases.
Hassler M et al.
Current Opinion in Structural Biology, 2012
Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1.
Langelier MF et al.
Science (new York, N.y.), 2012
Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications.
Tao Z et al.
Journal of the American Chemical Society, 2009
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