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Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: relationship to "bypass Sec14p" and inositol auxotrophy
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
10397762
retrieved
1 December 2016
title
Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: relationship to "bypass Sec14p" and inositol auxotrophy
(English)
1 reference
stated in
PubMed
PubMed ID
10397762
retrieved
1 December 2016
main subject
Choline-phosphate cytidylyltransferase YGR202C
1 reference
stated in
GOA release 2020-03-11
pleiotropy
1 reference
based on heuristic
inferred from title
author name string
M P Rivas
series ordinal
1
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B G Kearns
series ordinal
2
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Z Xie
series ordinal
3
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S Guo
series ordinal
4
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M C Sekar
series ordinal
5
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K Hosaka
series ordinal
6
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S Kagiwada
series ordinal
7
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J D York
series ordinal
8
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V A Bankaitis
series ordinal
9
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language of work or name
English
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publication date
July 1999
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published in
Molecular Biology of the Cell
1 reference
stated in
PubMed
PubMed ID
10397762
retrieved
1 December 2016
volume
10
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page(s)
2235-50
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issue
7
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cites work
SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
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Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
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INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype
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STT4 is an essential phosphatidylinositol 4-kinase that is a target of wortmannin in Saccharomyces cerevisiae
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Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis.
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SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast.
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The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity
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Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
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PubMed Central
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Transformation of intact yeast cells treated with alkali cations
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Suppressors of yeast actin mutations
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The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
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The gene encoding the phosphatidylinositol transfer protein is essential for cell growth.
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An essential role for a phospholipid transfer protein in yeast Golgi function
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Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
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One-step gene disruption in yeast
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Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects
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Sac1p plays a crucial role in microsomal ATP transport, which is distinct from its function in Golgi phospholipid metabolism
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The yeast BSD2-1 mutation influences both the requirement for phosphatidylinositol transfer protein function and derepression of phospholipid biosynthetic gene expression in yeast.
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Sac1p mediates the adenosine triphosphate transport into yeast endoplasmic reticulum that is required for protein translocation
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A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes
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Effects of unsaturated fatty acid deprivation on neutral lipid synthesis in Saccharomyces cerevisiae.
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[12] One-step gene disruption in yeast
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29 September 2017
Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function
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Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation.
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Phospholipid biosynthesis in yeast
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Essential role for diacylglycerol in protein transport from the yeast Golgi complex.
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Crystallization and initial X-ray crystallographic characterization of recombinant bovine inositol polyphosphate 1-phosphatase produced in Spodoptera frugiperda cells
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Phosphatidylinositol transfer proteins: the long and winding road to physiological function
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12 December 2020
based on heuristic
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Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells
1 reference
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reference URL
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based on heuristic
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Phospholipid transfer proteins: a biological debut
1 reference
stated in
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reference URL
https://pubmed.ncbi.nlm.nih.gov/10397762
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
In vitro studies of phospholipid biosynthesis in Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10397762
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based on heuristic
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A dominant mutation that alters the regulation of INO1 expression in Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10397762
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.10.7.2235
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4831455
OpenCitations bibliographic resource ID
4831455
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4831455
PMCID
25439
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4831455
PubMed ID
10397762
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4831455
ResearchGate publication ID
12901052
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