The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Structure and Mechanism of a Na + -Independent Amino Acid Transporter
Open accessAbstract
APC Transporter Structure: Amino acid, polyamine, and organocation (APC) transporters that move a range of organic molecules across the cell membrane are important in many cellular processes. Shaffer et al. (p. 1010 ; published online 16 July) report the crystal structure of apoApcT, a proton-dependent APC transporter. The structure shows similarity to the sodium-coupled amino acid transporter LeuT and has an amino group from a lysine in an equivalent position to a sodium ion in LeuT. This suggests common principles between proton- and sodium-coupled transporters.
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Metadata
- Authors
- Shaffer, P. L., Goehring, A., Shankaranarayanan, A., & Gouaux, E.
- Venue
- Science
- Published
- 2009-08-21
- Volume
- 325
- Issue
- 5943
- Pages
- 1010-1014
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2074274532
- Cited by
- 309
- References
- 30
- FWCI
- 14.62
- Type
- journal article
- Language
- en
- Open access
- green
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- Shaffer, P. L., Goehring, A., Shankaranarayanan, A., & Gouaux, E. (2009). Structure and Mechanism of a Na + -Independent Amino Acid Transporter. Science. https://doi.org/10.1126/science.1176088
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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.
