Cargando…
A Zinc Linchpin Motif in the MUTYH Glycosylase Interdomain Connector Is Required for Efficient Repair of DNA Damage
[Image: see text] Mammalian MutY glycosylases have a unique architecture that features an interdomain connector (IDC) that joins the catalytic N-terminal domain and 8-oxoguanine (OG) recognition C-terminal domain. The IDC has been shown to be a hub for interactions with protein partners involved in...
Autores principales: | Engstrom, Lisa M., Brinkmeyer, Megan K., Ha, Yang, Raetz, Alan G., Hedman, Britt, Hodgson, Keith O., Solomon, Edward I., David, Sheila S. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4063174/ https://www.ncbi.nlm.nih.gov/pubmed/24841533 http://dx.doi.org/10.1021/ja502942d |
Ejemplares similares
-
MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNA
por: Markkanen, Enni, et al.
Publicado: (2013) -
Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer
por: Nakamura, Teruya, et al.
Publicado: (2021) -
Association of a New Germline Variant in the MUTYH DNA Glycosylase Gene with Colorectal Adenoma Transformation into Malignancy
por: Mahasneh, Amjad, et al.
Publicado: (2019) -
MUTYH, an adenine DNA glycosylase, mediates p53 tumor suppression via PARP-dependent cell death
por: Oka, S, et al.
Publicado: (2014) -
MUTYH, an adenine DNA glycosylase, mediates p53 tumor suppression via PARP-dependent cell death
por: Oka, S, et al.
Publicado: (2015)