Role of the fourth transmembrane domain in proton-coupled folate transporter function as assessed by the substituted cysteine accessibility method
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Title
Role of the fourth transmembrane domain in proton-coupled folate transporter function as assessed by the substituted cysteine accessibility method
Authors
Keywords
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Journal
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
Volume 304, Issue 12, Pages C1159-C1167
Publisher
American Physiological Society
Online
2013-04-04
DOI
10.1152/ajpcell.00353.2012
References
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Note: Only part of the references are listed.- Identification of a functionally critical GXXG motif and its relationship to the folate binding site of the proton-coupled folate transporter (PCFT-SLC46A1)
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- Functional roles of the A335 and G338 residues of the proton-coupled folate transporter (PCFT-SLC46A1) mutated in hereditary folate malabsorption
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- Mechanisms of Membrane Transport of Folates into Cells and Across Epithelia
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- Identification and Functional Impact of Homo-oligomers of the Human Proton-coupled Folate Transporter
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- Random Mutagenesis of the Proton-coupled Folate Transporter (SLC46A1), Clustering of Mutations, and the Bases for Associated Losses of Function
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- Therapeutic Targeting of a Novel 6-Substituted Pyrrolo [2,3-d]pyrimidine Thienoyl Antifolate to Human Solid Tumors Based on Selective Uptake by the Proton-Coupled Folate Transporter
- (2011) S. Kugel Desmoulin et al. MOLECULAR PHARMACOLOGY
- Properties of the Arg376 residue of the proton-coupled folate transporter (PCFT-SLC46A1) and a glutamine mutant causing hereditary folate malabsorption
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- Transmembrane Segment 11 Appears to Line the Purine Permeation Pathway of thePlasmodium falciparumEquilibrative Nucleoside Transporter 1 (PfENT1)
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- Targeting the Proton-Coupled Folate Transporter for Selective Delivery of 6-Substituted Pyrrolo[2,3-d]Pyrimidine Antifolate Inhibitors of De Novo Purine Biosynthesis in the Chemotherapy of Solid Tumors
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