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Translesion Synthesis of 2′-Deoxyguanosine Lesions by Eukaryotic DNA Polymerases
[Image: see text] With the discovery of translesion synthesis DNA polymerases, great strides have been made in the last two decades in understanding the mode of replication of various DNA lesions in prokaryotes and eukaryotes. A database search indicated that approximately 2000 articles on this topi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5241707/ https://www.ncbi.nlm.nih.gov/pubmed/27760288 http://dx.doi.org/10.1021/acs.chemrestox.6b00285 |
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author | Basu, Ashis K. Pande, Paritosh Bose, Arindam |
author_facet | Basu, Ashis K. Pande, Paritosh Bose, Arindam |
author_sort | Basu, Ashis K. |
collection | PubMed |
description | [Image: see text] With the discovery of translesion synthesis DNA polymerases, great strides have been made in the last two decades in understanding the mode of replication of various DNA lesions in prokaryotes and eukaryotes. A database search indicated that approximately 2000 articles on this topic have been published in this period. This includes research involving genetic and structural studies as well as in vitro experiments using purified DNA polymerases and accessory proteins. It is a daunting task to comprehend this exciting and rapidly emerging area of research. Even so, as the majority of DNA damage occurs at 2′-deoxyguanosine residues, this perspective attempts to summarize a subset of this field, focusing on the most relevant eukaryotic DNA polymerases responsible for their bypass. |
format | Online Article Text |
id | pubmed-5241707 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-52417072017-01-19 Translesion Synthesis of 2′-Deoxyguanosine Lesions by Eukaryotic DNA Polymerases Basu, Ashis K. Pande, Paritosh Bose, Arindam Chem Res Toxicol [Image: see text] With the discovery of translesion synthesis DNA polymerases, great strides have been made in the last two decades in understanding the mode of replication of various DNA lesions in prokaryotes and eukaryotes. A database search indicated that approximately 2000 articles on this topic have been published in this period. This includes research involving genetic and structural studies as well as in vitro experiments using purified DNA polymerases and accessory proteins. It is a daunting task to comprehend this exciting and rapidly emerging area of research. Even so, as the majority of DNA damage occurs at 2′-deoxyguanosine residues, this perspective attempts to summarize a subset of this field, focusing on the most relevant eukaryotic DNA polymerases responsible for their bypass. American Chemical Society 2016-10-19 2017-01-17 /pmc/articles/PMC5241707/ /pubmed/27760288 http://dx.doi.org/10.1021/acs.chemrestox.6b00285 Text en Copyright © 2016 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Basu, Ashis K. Pande, Paritosh Bose, Arindam Translesion Synthesis of 2′-Deoxyguanosine Lesions by Eukaryotic DNA Polymerases |
title | Translesion Synthesis
of 2′-Deoxyguanosine
Lesions by Eukaryotic DNA Polymerases |
title_full | Translesion Synthesis
of 2′-Deoxyguanosine
Lesions by Eukaryotic DNA Polymerases |
title_fullStr | Translesion Synthesis
of 2′-Deoxyguanosine
Lesions by Eukaryotic DNA Polymerases |
title_full_unstemmed | Translesion Synthesis
of 2′-Deoxyguanosine
Lesions by Eukaryotic DNA Polymerases |
title_short | Translesion Synthesis
of 2′-Deoxyguanosine
Lesions by Eukaryotic DNA Polymerases |
title_sort | translesion synthesis
of 2′-deoxyguanosine
lesions by eukaryotic dna polymerases |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5241707/ https://www.ncbi.nlm.nih.gov/pubmed/27760288 http://dx.doi.org/10.1021/acs.chemrestox.6b00285 |
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