Substituted Cysteine Accessibility Reveals a Novel Transmembrane 2–3 Reentrant Loop and Functional Role for Transmembrane Domain 2 in the Human Proton-coupled Folate Transporter
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Title
Substituted Cysteine Accessibility Reveals a Novel Transmembrane 2–3 Reentrant Loop and Functional Role for Transmembrane Domain 2 in the Human Proton-coupled Folate Transporter
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 36, Pages 25287-25295
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2014-07-23
DOI
10.1074/jbc.m114.578252
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Note: Only part of the references are listed.- Role of the fourth transmembrane domain in proton-coupled folate transporter function as assessed by the substituted cysteine accessibility method
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- 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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- (2010) Rongbao Zhao et al. BIOCHEMISTRY
- Functional roles of aspartate residues of the proton-coupled folate transporter (PCFT-SLC46A1); a D156Y mutation causing hereditary folate malabsorption
- (2010) D. S. Shin et al. BLOOD
- 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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- Hereditary folate malabsorption: A positively charged amino acid at position 113 of the proton-coupled folate transporter (PCFT/SLC46A1) is required for folic acid binding
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- Reversible severe combined immunodeficiency phenotype secondary to a mutation of the proton-coupled folate transporter
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