umuDC-dnaQ interaction and its implications for cell cycle regulation and SOS mutagenesis in Escherichia coli
Journal of Bacteriology, ISSN: 0021-9193, Vol: 183, Issue: 3, Page: 1085-1089
2001
- 27Citations
- 24Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations27
- Citation Indexes27
- 27
- CrossRef22
- Captures24
- Readers24
- 24
Article Description
The Escherichia coli SOS-regulated umuDC gene products participate in a DNA damage checkpoint control and in translesion DNA synthesis. Specific interactions involving the UmuD and UmuD' proteins, both encoded by the umuD gene, and components of the replicative DNA polymerase, Pol III, appear to be important for regulating these two biological activities of the umuDC gene products. Here we show that overproduction of the ε proofreading subunit of Pol III suppresses the cold sensitivity normally associated with overexpression of the umuDC gene products. Our results suggest that this suppression is attributable to specific interactions between UmuD or UmuD' and the C-terminal domain of ε.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035148764&origin=inward; http://dx.doi.org/10.1128/jb.183.3.1085-1089.2001; http://www.ncbi.nlm.nih.gov/pubmed/11208808; http://jb.asm.org/cgi/doi/10.1128/JB.183.3.1085-1089.2001; https://syndication.highwire.org/content/doi/10.1128/JB.183.3.1085-1089.2001; https://journals.asm.org/doi/10.1128/JB.183.3.1085-1089.2001; https://dx.doi.org/10.1128/jb.183.3.1085-1089.2001
American Society for Microbiology
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