Thymine DNA glycosylase exhibits negligible affinity for nucleobases that it removes from DNA
Thymine DNA Glycosylase (TDG) performs essential functions in maintaining genetic integrity and epigenetic regulation. Initiating base excision repair, TDG removes thymine from mutagenic G·T mispairs caused by 5-methylcytosine (mC) deamination and other lesions including uracil (U) and 5-hydroxymeth...
Main Authors: | Malik, Shuja S., Coey, Christopher T., Varney, Kristen M., Pozharski, Edwin, Drohat, Alexander C. |
---|---|
Format: | Online |
Language: | English |
Published: |
Oxford University Press
2015
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4627079/ |
Similar Items
-
Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues
by: Coey, Christopher T., et al.
Published: (2016) -
Stoichiometry and affinity for thymine DNA glycosylase binding to specific and nonspecific DNA
by: Morgan, Michael T., et al.
Published: (2011) -
Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging
by: Buechner, Claudia N., et al.
Published: (2015) -
Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
by: Zhang, Liang, et al.
Published: (2012) -
How a mismatch repair enzyme balances the needs for efficient lesion processing and minimal action on undamaged DNA
by: Drohat, Alexander C., et al.
Published: (2012)