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Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
18799613
retrieved
1 December 2016
title
Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum
(English)
1 reference
stated in
PubMed
PubMed ID
18799613
retrieved
1 December 2016
main subject
cell biology
0 references
endoplasmic reticulum
0 references
Voa1p YGR106C
1 reference
stated in
GOA release 2020-03-11
author name string
Margret Ryan
series ordinal
1
0 references
Laurie A Graham
series ordinal
2
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Tom H Stevens
series ordinal
3
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language of work or name
English
0 references
publication date
December 2008
0 references
published in
Molecular Biology of the Cell
1 reference
stated in
PubMed
PubMed ID
18799613
retrieved
1 December 2016
volume
19
0 references
issue
12
0 references
page(s)
5131-42
0 references
cites work
An in vivo map of the yeast protein interactome
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PubMed Central
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PKR1 encodes an assembly factor for the yeast V-type ATPase.
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The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex
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PubMed Central
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Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.
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Role of Vma21p in assembly and transport of the yeast vacuolar ATPase
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Topological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae.
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The RAVE complex is essential for stable assembly of the yeast V-ATPase
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Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p
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20 March 2017
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.
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20 March 2017
Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly
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Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex
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VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H+-ATPase assembly
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Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase
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The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector.
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Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex
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Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex
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STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p
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Purification and properties of H+-translocating, Mg2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
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The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase
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Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
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Structure and assembly of the yeast V-ATPase
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Early steps in assembly of the yeast vacuolar H+-ATPase
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Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry
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VMA12 is essential for assembly of the vacuolar H(+)-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae
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Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
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Arabidopsis has two functional orthologs of the yeast V-ATPase assembly factor Vma21p
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Arrangement of subunits in the proteolipid ring of the V-ATPase
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The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
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29 September 2017
The V-type H+ ATPase: molecular structure and function, physiological roles and regulation
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ABG1, a novel and essential Candida albicans gene encoding a vacuolar protein involved in cytokinesis and hyphal branching.
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Subcellular fractionation of secretory organelles
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Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle
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Rotation of the proteolipid ring in the V-ATPase
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Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits
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27 November 2018
Partial assembly of the yeast vacuolar H(+)-ATPase in mutants lacking one subunit of the enzyme.
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27 November 2018
Molecular characterization of the yeast vacuolar H+-ATPase proton pore
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18799613
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Site-specific mutagenesis by using an accurate recombinant polymerase chain reaction method
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18799613
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
RAVE is essential for the efficient assembly of the C subunit with the vacuolar H(+)-ATPase
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18799613
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Site-directed mutagenesis of the yeast V-ATPase B subunit (Vma2p)
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18799613
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.E08-06-0629
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1238814
OpenCitations bibliographic resource ID
1238814
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1238814
PMCID
2592645
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1238814
PubMed ID
18799613
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1238814
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