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The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
2183024
retrieved
1 December 2016
title
The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function
(English)
1 reference
stated in
PubMed
PubMed ID
2183024
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
Tethering complex ATP-binding subunit VPS33 YLR396C
1 reference
stated in
GOA release 2020-03-11
morphogenesis
1 reference
based on heuristic
inferred from title
author name string
Y Wada
series ordinal
1
0 references
K Kitamoto
series ordinal
2
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T Kanbe
series ordinal
3
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K Tanaka
series ordinal
4
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Y Anraku
series ordinal
5
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language of work or name
English
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publication date
May 1990
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published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
2183024
retrieved
1 December 2016
volume
10
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page(s)
2214-23
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issue
5
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cites work
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Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
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Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
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Purification and properties of H+-translocating, Mg2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
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DNA sequence required for efficient transcription termination in yeast
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Construction of a yeast actin gene intron deletion mutant that is defective in splicing and leads to the accumulation of precursor RNA in transformed yeast cells
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The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
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Mutants of Saccharomyces cerevisiae with defective vacuolar function
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Dynamic aspects of vacuolar and cytosolic amino acid pools of Saccharomyces cerevisiae
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29 September 2017
Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting
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PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
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PubMed Central
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The amino terminus of the yeast F1-ATPase beta-subunit precursor functions as a mitochondrial import signal
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Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae
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PubMed Central
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Assay of vacuolar pH in yeast and identification of acidification-defective mutants
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PubMed Central
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Characterization of the END1 gene required for vacuole biogenesis and gluconeogenic growth of budding yeast
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29 September 2017
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Substrate specificities of active transport systems for amino acids in vacuolar-membrane vesicles of Saccharomyces cerevisiae. Evidence of seven independent proton/amino acid antiport systems
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Two yeast mutants defective in endocytosis are defective in pheromone response
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PubMed Central
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2 June 2018
COX8, the structural gene for yeast cytochrome c oxidase subunit VIII. DNA sequence and gene disruption indicate that subunit VIII is required for maximal levels of cellular respiration and is derived from a precursor which is extended at both its N
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2 June 2018
Vacuolar ion channel of the yeast, Saccharomyces cerevisiae.
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2 June 2018
Studies of gene mutation in Saccharomyces
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27 November 2018
Nucleotide sequence of the CLS4 (CDC24) gene of Saccharomyces cerevisiae
1 reference
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PubMed Central
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27 November 2018
Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2183024
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12 December 2020
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Mitosis in the fission yeast Schizosaccharomyces pombe as revealed by freeze-substitution electron microscopy
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2183024
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12 December 2020
based on heuristic
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Endocytosis in yeast: Several of the yeast secretory mutants are defective in endocytosis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2183024
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/2183024
retrieved
12 December 2020
based on heuristic
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Identifiers
DOI
10.1128/MCB.10.5.2214
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PMCID
360569
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PubMed ID
2183024
1 reference
stated in
PubMed
PubMed ID
2183024
retrieved
1 December 2016
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