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The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
9693378
retrieved
1 December 2016
title
The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane
(English)
1 reference
stated in
PubMed
PubMed ID
9693378
retrieved
1 December 2016
main subject
endoplasmic reticulum
0 references
Saccharomyces cerevisiae
0 references
Protein-S-isoprenylcysteine carboxyl O-methyltransferase YDR410C
1 reference
stated in
GOA release 2020-03-11
author name string
J D Romano
series ordinal
1
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W K Schmidt
series ordinal
2
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S Michaelis
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3
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language of work or name
English
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publication date
August 1998
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published in
Molecular Biology of the Cell
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stated in
PubMed
PubMed ID
9693378
retrieved
1 December 2016
volume
9
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page(s)
2231-47
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issue
8
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cites work
Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum
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PubMed Central
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Pex19p, a farnesylated protein essential for peroxisome biogenesis
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Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins.
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Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
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The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins
1 reference
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Protein prenylation: molecular mechanisms and functional consequences
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1 reference
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1 reference
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PubMed Central
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1 reference
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PubMed Central
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1 reference
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PubMed Central
reference URL
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2 June 2018
Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
1 reference
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PubMed Central
reference URL
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1 reference
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PubMed Central
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2 June 2018
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1 reference
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PubMed Central
reference URL
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2 June 2018
Characterization of a plasma membrane-associated prenylcysteine-directed alpha carboxyl methyltransferase in human neutrophils
1 reference
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PubMed Central
reference URL
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27 November 2018
Prenylcysteine analogs to study function of carboxylmethylation in signal transduction.
1 reference
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PubMed Central
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27 November 2018
Plasmid construction by homologous recombination in yeast.
1 reference
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PubMed Central
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27 November 2018
In vitro and in vivo products of E. coli lactose permease gene are identical
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9693378
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Product of SEC53 is required for folding and glycosylation of secretory proteins in the lumen of the yeast endoplasmic reticulum
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9693378
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9693378
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Mutagenesis of conserved residues in the phosphorylation domain of the yeast plasma membrane H(+)-ATPase. Effects on structure and function
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9693378
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Prenylcysteine-directed carboxyl methyltransferase activity in human neutrophil membranes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9693378
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.9.8.2231
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4086298
OpenCitations bibliographic resource ID
4086298
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4086298
PMCID
25475
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4086298
PubMed ID
9693378
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4086298
ResearchGate publication ID
13592633
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