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MFSD2B is a sphingosine 1-phosphate transporter in erythroid cells

Scientific reports, 2018-03, Vol.8 (1), p.4969-11, Article 4969

2018

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The Amino-terminal Domain of the Vacuolar Proton-translocating ATPase a Subunit Controls Targeting and in Vivo Dissociation, and the Carboxyl-terminal Domain Affects Coupling of Proton Transport and ATP Hydrolysis

The Journal of biological chemistry, 2001-12, Vol.276 (50), p.47411-47420

2001

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Arg-735 of the 100-kDa Subunit a of the Yeast V-ATPase is Essential for Proton Translocation

Proceedings of the National Academy of Sciences - PNAS, 2001-10, Vol.98 (22), p.12397-12402

2001

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Interacting Helical Surfaces of the Transmembrane Segments of Subunits a and c′ of the Yeast V-ATPase Defined by Disulfide-mediated Cross-linking

The Journal of biological chemistry, 2003-10, Vol.278 (43), p.41908-41913

2003

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Expression and Function of the Mouse V-ATPase d Subunit Isoforms

The Journal of biological chemistry, 2003-11, Vol.278 (47), p.46396-46402

2003

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Tissue specific expression of the splice variants of the mouse vacuolar proton-translocating ATPase a4 subunit

Biochemical and biophysical research communications, 2007-12, Vol.364 (4), p.1032-1036

2007

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Mutational Analysis of the Non-homologous Region of Subunit A of the Yeast V-ATPase

The Journal of biological chemistry, 2003-04, Vol.278 (15), p.12985-12991

2003

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The First Putative Transmembrane Segment of Subunit c" (Vma16p) of the Yeast V-ATPase Is Not Necessary for Function

The Journal of biological chemistry, 2003-02, Vol.278 (8), p.5821-5827

2003

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Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation

The Journal of biological chemistry, 2001-05, Vol.276 (21), p.17941-17948

2001

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Proton translocation driven by ATP hydrolysis in V-ATPases

FEBS Letters, 2003-06, Vol.545 (1), p.76-85

2003

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Yeast V-ATPase Complexes Containing Different Isoforms of the 100-kDa a-subunit Differ in Coupling Efficiency and in VivoDissociation

The Journal of biological chemistry, 2001-05, Vol.276 (21), p.17941-17948

2001

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Structure, subunit function and regulation of the coated vesicle and yeast vacuolar (H +)-ATPases

Biochimica et biophysica acta, 2002-09, Vol.1555 (1), p.71-74

2002

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Expression and Localization of the Mouse Homologue of the Yeast V-ATPase 21-kDa Subunit c′′ (Vma16p)

The Journal of biological chemistry, 2001-09, Vol.276 (36), p.34122-34130

2001

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Interacting Helical Surfaces of the Transmembrane Segments of Subunits a and câ² of the Yeast V-ATPase Defined by Disulfide-mediated Cross-linking

The Journal of biological chemistry, 2003-10, Vol.278 (43), p.41908

2003

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Expression and Localization of the Mouse Homologue of the Yeast V-ATPase 21-kDa Subunit câ²â² (Vma16p)

The Journal of biological chemistry, 2001-09, Vol.276 (36), p.34122

2001

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MFSD2B is a sphingosine 1-phosphate transporter in erythroid cells

The Amino-terminal Domain of the Vacuolar Proton-translocating ATPase a Subunit Controls Targeting and in Vivo Dissociation, and the Carboxyl-terminal Domain Affects Coupling of Proton Transport and ATP Hydrolysis

Arg-735 of the 100-kDa Subunit a of the Yeast V-ATPase is Essential for Proton Translocation

Interacting Helical Surfaces of the Transmembrane Segments of Subunits a and c′ of the Yeast V-ATPase Defined by Disulfide-mediated Cross-linking

Expression and Function of the Mouse V-ATPase d Subunit Isoforms

Tissue specific expression of the splice variants of the mouse vacuolar proton-translocating ATPase a4 subunit

Mutational Analysis of the Non-homologous Region of Subunit A of the Yeast V-ATPase

The First Putative Transmembrane Segment of Subunit c" (Vma16p) of the Yeast V-ATPase Is Not Necessary for Function

Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation

Proton translocation driven by ATP hydrolysis in V-ATPases

Yeast V-ATPase Complexes Containing Different Isoforms of the 100-kDa a-subunit Differ in Coupling Efficiency and in VivoDissociation

Structure, subunit function and regulation of the coated vesicle and yeast vacuolar (H +)-ATPases

Expression and Localization of the Mouse Homologue of the Yeast V-ATPase 21-kDa Subunit c′′ (Vma16p)

Interacting Helical Surfaces of the Transmembrane Segments of Subunits a and câ² of the Yeast V-ATPase Defined by Disulfide-mediated Cross-linking

Expression and Localization of the Mouse Homologue of the Yeast V-ATPase 21-kDa Subunit câ²â² (Vma16p)

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