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Processing and fatty acid acylation of RAS1 and RAS2 proteins in Saccharomyces cerevisiae
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
3513173
retrieved
1 December 2016
title
Processing and fatty acid acylation of RAS1 and RAS2 proteins in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
3513173
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
fatty acid
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Ras family GTPase RAS1 YOR101W
1 reference
stated in
GOA release 2020-03-11
author name string
A Fujiyama
series ordinal
1
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F Tamanoi
series ordinal
2
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language of work or name
English
0 references
publication date
March 1986
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published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
3513173
retrieved
1 December 2016
volume
83
0 references
page(s)
1266-70
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issue
5
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Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses
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Only membrane-associated RSV src proteins have amino-terminally bound lipid
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ras-Related gene sequences identified and isolated from Saccharomyces cerevisiae
1 reference
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Acylation of bovine rhodopsin by [3H]palmitic acid
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based on heuristic
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Requirement of either of a pair of ras-related genes of Saccharomyces cerevisiae for spore viability
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/3513173
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1073/PNAS.83.5.1266
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ADS bibcode
1986PNAS...83.1266F
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PMCID
323056
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PubMed ID
3513173
1 reference
stated in
PubMed
PubMed ID
3513173
retrieved
1 December 2016
ResearchGate publication ID
19649094
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