VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly
Open Access
- 1 October 1997
- journal article
- Published by Elsevier
- Vol. 272 (41), 25928-25934
- https://doi.org/10.1074/jbc.272.41.25928
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- VMA11 and VMA16 Encode Second and Third Proteolipid Subunits of the Saccharomyces cerevisiae Vacuolar Membrane H+-ATPasePublished by Elsevier ,1997
- Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro.The Journal of cell biology, 1996
- Site-directed Mutagenesis of the 100-kDa Subunit (Vph1p) of the Yeast Vacuolar (H+)-ATPasePublished by Elsevier ,1996
- Resolution of Subunit Interactions and Cytoplasmic Subcomplexes of the Yeast Vacuolar Proton-translocating ATPasePublished by Elsevier ,1996
- Vma22p Is a Novel Endoplasmic Reticulum-associated Protein Required for Assembly of the Yeast Vacuolar H+-ATPase ComplexPublished by Elsevier ,1995
- Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast.The Journal of cell biology, 1994
- The cyclophilin homolog ninaA is required in the secretory pathwayCell, 1991
- The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsinsCell, 1991
- The structure of an antigenic determinant in a proteinCell, 1984
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981