DNA helicases: ‘inching forward’
Current Opinion in Structural Biology, ISSN: 0959-440X, Vol: 10, Issue: 1, Page: 124-128
2000
- 100Citations
- 61Captures
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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.
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Metrics Details
- Citations100
- Citation Indexes100
- 100
- CrossRef74
- Captures61
- Readers61
- 61
Review Description
Recently determined crystal structures of PcrA helicase complexed with a DNA substrate have revealed details of the helicase mechanism. PcrA and UvrD helicases have been shown to be functional as monomers, challenging previous suggestions that all helicases are required to be oligomeric. Crystal structures of the hexameric helicases RepA and T7 gene 4 explain the formation of hexameric assemblies from identical monomers with RecA-like folds, but their molecular mechanism remains elusive.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0959440X99000597; http://dx.doi.org/10.1016/s0959-440x(99)00059-7; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033951183&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10679457; https://linkinghub.elsevier.com/retrieve/pii/S0959440X99000597; http://linkinghub.elsevier.com/retrieve/pii/S0959440X99000597; http://api.elsevier.com/content/article/PII:S0959440X99000597?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0959440X99000597?httpAccept=text/plain; http://dx.doi.org/10.1016/s0959-440x%2899%2900059-7; https://dx.doi.org/10.1016/s0959-440x%2899%2900059-7
Elsevier BV
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