Skip to main content
Portland Press Open Access logoLink to Portland Press Open Access
. 2020 Jul 29;64(5):845. doi: 10.1042/EBC20200013_COR

Correction: Base excision repair and its implications to cancer therapy

PMCID: PMC7588662  PMID: 32725152

Grundy, G.J. and Parsons, J.L. (2020) Base excision repair and its implications to cancer therapy. Essays Biochem. https://doi.org/10.1042/EBC20200013

During the production process errors were introduced into Table 1. The correct version of Table 1 appears here.

Table 1. DNA glycosylases: substrates, inhibitors and synthetic lethal partners.

DNA Glycosylase Substrate Inhibitor Synthetic lethal partner
Monofunctional
UNG
Uracil DNA glycosylase Uracil APOBEC3B
SMUG1
Single-strand selective monofunctional uracil DNA glycosylase Uracil, 5-formyluracil, 5-hydroxyuracil and 5-hydroxymethyluracil
TDG
G/T Mismatch specific thymine DNA glycosylase 5-Formylcytosine and 5-carboxylcytosine in CpG. G:T and U:T mismatches
MBD4
methyl-CpG binding domain protein 4 G:T mismatches within methylated and unmethylated CpG sites. Uracil or 5-fluorouracil in G:U mismatches
MPG
N-methylpurine DNA glycosylase 3-methyladenine, and 7-methylguanine
MUTYH
Adenine DNA glycosylase 7,8-Dihydro-8-oxoguanine (8-oxoG):adenine
Bifunctional
NTH1
Endonuclease III-like protein 1 Oxidised pyrimidines, thymine glycol
OGG1
8-oxoguanine DNA glycosylase 1 8-OxoG, formamidopyrimidine (Fapy)G O8 MMR deficiency
SU0268
TH5487
Endonuclease VIII-like
NEIL1 Thymine glycol, Fapy, 5-hydroxyuracil 2TX FANCG
NEIL2 5-Hydroxyuracil
NEIL3 Spiroiminodihydantoin and guanidinohydantoin

Articles from Essays in Biochemistry are provided here courtesy of Portland Press Ltd

RESOURCES