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Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
9292983
retrieved
1 December 2016
title
Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
9292983
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
Hydroxymethylglutaryl-CoA reductase (NADPH) HMG1 YML075C
1 reference
stated in
GOA release 2020-03-11
squalene
1 reference
based on heuristic
inferred from title
author name string
K A Donald
series ordinal
1
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R Y Hampton
series ordinal
2
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I B Fritz
series ordinal
3
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language of work or name
English
0 references
publication date
September 1997
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published in
Applied and Environmental Microbiology
1 reference
stated in
PubMed
PubMed ID
9292983
retrieved
1 December 2016
volume
63
0 references
page(s)
3341-4
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issue
9
0 references
cites work
Antagonistic controls regulate copy number of the yeast 2 mu plasmid
1 reference
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PubMed Central
reference URL
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20 March 2017
Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase
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reference URL
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20 March 2017
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
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7 April 2017
Transcriptional regulation by ergosterol in the yeast Saccharomyces cerevisiae
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PubMed Central
reference URL
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retrieved
29 September 2017
Transcriptional regulation of a sterol-biosynthetic enzyme by sterol levels in Saccharomyces cerevisiae
1 reference
stated in
PubMed Central
reference URL
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retrieved
29 September 2017
The biology of HMG-CoA reductase: the pros of contra-regulation
1 reference
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PubMed Central
reference URL
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29 September 2017
3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Haloferax volcanii: purification, characterization, and expression in Escherichia coli
1 reference
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PubMed Central
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29 September 2017
Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
1 reference
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PubMed Central
reference URL
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29 September 2017
Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Oxygen requirements for formation and activity of the squalene epoxidase in Saccharomyces cerevisiae
1 reference
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PubMed Central
reference URL
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29 September 2017
Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis
1 reference
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PubMed Central
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29 September 2017
Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae
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29 September 2017
DMSO-enhanced whole cell yeast transformation
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29 September 2017
Metabolism of Sterols in Yeast
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29 September 2017
Synthesis of lipids in resting cells of Saccharomyces cerevisiae
1 reference
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reference URL
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retrieved
27 November 2018
Regulation of squalene synthetase and squalene epoxidase activities in Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9292983
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
[18] Yeast sterols: Yeast mutants as tools for the study of sterol metabolism
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9292983
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Net synthesis of sterols in resting cells of Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9292983
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/AEM.63.9.3341-3344.1997
0 references
OpenCitations bibliographic resource ID
605922
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
605922
PMCID
168639
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
605922
PubMed ID
9292983
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
605922
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