Characterization of the third member of the MCAT family of cationic amino acid transporters. Identification of a domain that determines the transport properties of the MCAT proteins.
Open Access
- 1 October 1993
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (28) , 20796-20800
- https://doi.org/10.1016/s0021-9258(19)36854-1
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Identification of a low affinity, high capacity transporter of cationic amino acids in mouse liver.Journal of Biological Chemistry, 1993
- Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteriaProtein Science, 1993
- Replacement of intracellular C-terminal domain of GLUT1 glucose transporter with that of GLUT2 increases Vmax and Km of transport activity.Journal of Biological Chemistry, 1992
- Transport of cationic amino acids by the mouse ecotropic retrovirus receptorNature, 1991
- C-terminal truncated glucose transporter is locked into an inward-facing form without transport activityNature, 1990
- A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infectionCell, 1989
- A comprehensive set of sequence analysis programs for the VAXNucleic Acids Research, 1984
- Efficientin vitrosynthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoterNucleic Acids Research, 1984
- The two-way flux of cationic amino acids across the plasma membrane of mammalian cells is largely explained by a single transport system.Journal of Biological Chemistry, 1982