scholarly journals Interaction with the DNA Repair Protein Thymine DNA Glycosylase Regulates Histone Acetylation by p300

Biochemistry ◽  
2016 ◽  
Vol 55 (49) ◽  
pp. 6766-6775 ◽  
Author(s):  
Ryan A. Henry ◽  
Pietro Mancuso ◽  
Yin-Ming Kuo ◽  
Rossella Tricarico ◽  
Marc Tini ◽  
...  
Keyword(s):  
Dna Repair ◽  
Histone Acetylation ◽  
Dna Glycosylase ◽  
Thymine Dna Glycosylase ◽  
Repair Protein ◽  
Dna Repair Protein

scholarly journals Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily

1996 ◽  
Vol 6 (8) ◽  
pp. 968-980 ◽  
Author(s):  
Huw M. Nash ◽  
Steven D. Bruner ◽  
Orlando D. Schärer ◽  
Tomohiko Kawate ◽  
Theresa A. Addona ◽  
...  
Keyword(s):  
Dna Repair ◽  
Dna Glycosylase ◽  
Protein Superfamily ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Base Excision ◽  
Base Excision Dna Repair

Altered expression of the DNA repair protein, N -methylpurine-DNA glycosylase (MPG), in breast cancer

FEBS Letters ◽  
1998 ◽  
Vol 431 (1) ◽  
pp. 12-18 ◽  
Author(s):  
Sonia R Cerda ◽  
Patrick W Turk ◽  
Ann D Thor ◽  
Sigmund A Weitzman
Keyword(s):  
Breast Cancer ◽  
Dna Repair ◽  
Dna Glycosylase ◽  
Altered Expression ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Methylpurine Dna Glycosylase

scholarly journals A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M

2005 ◽  
Vol 37 (9) ◽  
pp. 958-963 ◽  
Author(s):  
Amom Ruhikanta Meetei ◽  
Annette L Medhurst ◽  
Chen Ling ◽  
Yutong Xue ◽  
Thiyam Ramsing Singh ◽  
...  
Keyword(s):  
Dna Repair ◽  
Fanconi Anemia ◽  
Complementation Group ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Human Ortholog

Chemoproteomics-Enabled Discovery of a Potent and Selective Inhibitor of the DNA Repair Protein MGMT

2016 ◽  
Vol 55 (8) ◽  
pp. 2911-2915 ◽  
Author(s):  
Chao Wang ◽  
Daniel Abegg ◽  
Dominic G. Hoch ◽  
Alexander Adibekian
Keyword(s):  
Dna Repair ◽  
Selective Inhibitor ◽  
Repair Protein ◽  
Dna Repair Protein

Partial characterization of the DNA repair protein complex, containing the ERCC1, ERCC4, ERCC11 and XPF correcting activities

1995 ◽  
Vol 337 (1) ◽  
pp. 25-39 ◽  
Author(s):  
A.J. van Vuuren ◽  
E. Appeldoorn ◽  
H. Odijk ◽  
S. Humbert ◽  
V. Moncollin ◽  
...  
Keyword(s):  
Dna Repair ◽  
Protein Complex ◽  
Partial Characterization ◽  
Repair Protein ◽  
Dna Repair Protein

scholarly journals ROS induces NETosis by oxidizing DNA and initiating DNA repair

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Dhia Azzouz ◽  
Meraj A. Khan ◽  
Nades Palaniyar
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Polymerase Activity ◽  
Neutrophil Activation ◽  
Neutrophil Extracellular Trap ◽  
Nuclear Antigen ◽  
Chromatin Decondensation ◽  
Genome Wide ◽  
Repair Protein ◽  
Dna Repair Protein

AbstractReactive oxygen species (ROS) are essential for neutrophil extracellular trap (NET) formation or NETosis. Nevertheless, how ROS induces NETosis is unknown. Neutrophil activation induces excess ROS production and a meaningless genome-wide transcription to facilitate chromatin decondensation. Here we show that the induction of NADPH oxidase-dependent NETosis leads to extensive DNA damage, and the subsequent translocation of proliferating cell nuclear antigen (PCNA), a key DNA repair protein, stored in the cytoplasm into the nucleus. During the activation of NETosis (e.g., by phorbol myristate acetate, Escherichia coli LPS, Staphylococcus aureus (RN4220), or Pseudomonas aeruginosa), preventing the DNA-repair-complex assembly leading to nick formation that decondenses chromatin causes the suppression of NETosis (e.g., by inhibitors to, or knockdown of, Apurinic endonuclease APE1, poly ADP ribose polymerase PARP, and DNA ligase). The remaining repair steps involving polymerase activity and PCNA interactions with DNA polymerases β/δ do not suppress agonist-induced NETosis. Therefore, excess ROS produced during neutrophil activation induces NETosis by inducing extensive DNA damage (e.g., oxidising guanine to 8-oxoguanine), and the subsequent DNA repair pathway, leading to chromatin decondensation.

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