| Full text | |
| Author(s): Show less - |
Cesar-Razquin, Adrian
[1]
;
Snijder, Berend
[1]
;
Frappier-Brinton, Tristan
[2]
;
Isserlin, Ruth
[3]
;
Gyimesi, Gergely
[4, 5]
;
Bai, Xiaoyun
[6]
;
Reithmeier, Reinhart A.
[6]
;
Hepworth, David
[7]
;
Hediger, Matthias A.
[4, 5]
;
Edwards, Aled M.
[2]
;
Superti-Furga, Giulio
[1, 8]
Total Authors: 11
|
| Affiliation: | [1] Austrian Acad Sci, CeMM Res Ctr Mol Med, A-1090 Vienna - Austria
[2] Univ Toronto, Struct Genom Consortium, Toronto, ON M5G 1L7 - Canada
[3] Univ Toronto, Donnelly Ctr, Toronto, ON M5S 3E1 - Canada
[4] Univ Bern, NCCR TransCure, Inst Biochem & Mol Med, CH-3012 Bern - Switzerland
[5] Univ Bern, NCCR TransCure, Swiss Natl Ctr Competence Res, CH-3012 Bern - Switzerland
[6] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8 - Canada
[7] Pfizer Worldwide Res & Dev, Worldwide Med Chem, Cambridge, MA 02139 - USA
[8] Med Univ Vienna, Ctr Physiol & Pharmacol, A-1090 Vienna - Austria
Total Affiliations: 8
|
| Document type: | Review article |
| Source: | Cell; v. 162, n. 3, p. 478-487, JUL 30 2015. |
| Web of Science Citations: | 133 |
| Abstract | |
Solute carrier (SLC) membrane transport proteins control essential physiological functions, including nutrient uptake, ion transport, and waste removal. SLCs interact with several important drugs, and a quarter of the more than 400 SLC genes are associated with human diseases. Yet, compared to other gene families of similar stature, SLCs are relatively understudied. The time is right for a systematic attack on SLC structure, specificity, and function, taking into account kinship and expression, as well as the dependencies that arise from the common metabolic space. (AU) | |