A closed conformation for the Pol λ catalytic cycle
Nature Structural and Molecular Biology, ISSN: 1545-9993, Vol: 12, Issue: 1, Page: 97-98
2005
- 139Citations
- 41Captures
- 1Mentions
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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
- Citations139
- Citation Indexes139
- 139
- CrossRef121
- Captures41
- Readers41
- 41
- Mentions1
- References1
- 1
Article Description
Pol λ is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol λ representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol λ does not undergo large subdomain movements during catalysis, and they provide a clear characterization of the geometry and stereochemistry of the in-line nucleotidyl transfer reaction.
Bibliographic Details
Springer Science and Business Media LLC
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