The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.
ABC transporters: the power to change
Open accessAbstract
ATP-binding cassette (ABC) transporters constitute a ubiquitous superfamily of integral membrane proteins that are responsible for the ATP-powered translocation of many substrates across membranes. The highly conserved ABC domains of ABC transporters provide the nucleotide-dependent engine that drives transport. By contrast, the transmembrane domains that create the translocation pathway are more variable. Recent structural advances with prokaryotic ABC transporters have provided a qualitative molecular framework for deciphering the transport cycle. An important goal is to develop quantitative models that detail the kinetic and molecular mechanisms by which ABC transporters couple the binding and hydrolysis of ATP to substrate translocation.
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Principles of nanoparticle design for overcoming biological barriers to drug delivery
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The mechanism of eukaryotic translation initiation and principles of its regulation
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The mononuclear molybdenum enzymes
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Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Locher, K. P. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3216 · Cited by 804
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Metadata
- Authors
- Rees, D. C., Johnson, E., & Lewinson, O.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2009-03
- Volume
- 10
- Issue
- 3
- Pages
- 218-227
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2092435069
- Cited by
- 1,450
- References
- 75
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
