Associated Papers
Catalytically Competent Conformation of the Active Site of Human 8-Oxoguanine-DNA Glycosylase.
Popov AV et al.
Biochemistry. Biokhimiia, 2020
Could 8-oxoguanine DNA glycosylase 1 Ser326Cys polymorphism be a biomarker of susceptibility in cancer?
Karahalil B et al.
Toxicology and Industrial Health, 2014
Variation in base excision repair capacity.
Wilson DM et al.
Mutation Research, 2011
8-Oxoguanine incision activity is impaired in lung tissues of NSCLC patients with the polymorphism of OGG1 and XRCC1 genes.
Janik J et al.
Mutation Research, 2011
OGG1 Ser326Cys polymorphism and susceptibility to esophageal cancer in low and high at-risk populations of northern India.
Upadhyay R et al.
Journal of Gastrointestinal Cancer, 2010
Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase.
Sidorenko VS et al.
The Febs Journal, 2009
The R46Q, R131Q and R154H polymorphs of human DNA glycosylase/beta-lyase hOgg1 severely distort the active site and DNA recognition site but do not cause unfolding.
Anderson PC et al.
Journal of the American Chemical Society, 2009
Oxidized guanine lesions and hOgg1 activity in lung cancer.
Mambo E et al.
Oncogene, 2005
Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA.
Bruner SD et al.
Nature, 2000
Mutations in OGG1, a gene involved in the repair of oxidative DNA damage, are found in human lung and kidney tumours.
Chevillard S et al.
Oncogene, 1998
Molecular dynamics approach to identification of new OGG1 cancer-associated somatic variants with impaired activity.
Popov AV et al.
The Journal of Biological Chemistry, 0
Select a paper to view details