Functional sites in F-ATPases: Location and interactions
Journal of Bioenergetics and Biomembranes, ISSN: 0145-479X, Vol: 24, Issue: 5, Page: 469-477
1992
- 44Citations
- 2Captures
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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
- Citations44
- Citation Indexes44
- 44
- CrossRef41
- Captures2
- Readers2
Article Description
This review focuses on the location and interaction of three functional sites in F-ATPases. These are catalytic sites which are located in β subunits, noncatalytic nucleotide-binding sites which are located at interfaces of α and β subunits and modulate the hydrolytic activity of the enzyme, and a site that binds inhibitory amphipathic cations which is at an interface of α and β subunits. The latter site may participate in transmission of conformational signals between catalytic sites in F and the proton-conducting apparatus of F in the intact ATP synthases. © 1992 Plenum Publishing Corporation.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0026613084&origin=inward; http://dx.doi.org/10.1007/bf00762364; http://www.ncbi.nlm.nih.gov/pubmed/1429541; http://link.springer.com/10.1007/BF00762364; http://www.springerlink.com/index/pdf/10.1007/BF00762364; http://www.springerlink.com/index/10.1007/BF00762364; https://dx.doi.org/10.1007/bf00762364; https://link.springer.com/article/10.1007/BF00762364
Springer Nature
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