(Q41977606)

English

Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export

scientific article published on February 1994

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export (English)

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

author name string

S Sapperstein

1

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

C Berkower

2

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

S Michaelis

3

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

language of work or name

0 references

publication date

1 February 1994

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Molecular and Cellular Biology

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

14

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

2

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

1438-1449

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Physical maps of the six smallest chromosomes of Saccharomyces cerevisiae at a resolution of 2.6 kilobase pairs

1 reference

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1 reference

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5 June 2018

Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: carboxyl methyltransferase

1 reference

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Biochemistry of multidrug resistance mediated by the multidrug transporter

1 reference

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STE6, the yeast a-factor transporter

1 reference

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A simple method for displaying the hydropathic character of a protein

1 reference

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DNA sequence required for efficient transcription termination in yeast

1 reference

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The structure of transposable yeast mating type loci

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The a-factor pheromone of Saccharomyces cerevisiae is essential for mating

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Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells

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Molecular mechanisms of transcriptional regulation in yeast

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The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein

1 reference

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Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate

1 reference

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Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae

1 reference

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Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the ras protein

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Saccharomyces cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone

1 reference

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Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins

1 reference

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Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing

1 reference

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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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Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone

1 reference

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Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product

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Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B).

1 reference

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Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily

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Dependence of Ypt1 and Sec4 membrane attachment on Bet2.

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Maturation of isoprenylated proteins in Saccharomyces cerevisiae. Multiple activities catalyze the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro

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Endoproteolytic processing of a farnesylated peptide in vitro

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The prenylation of proteins

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Protein prenylation: more than just glue?

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Identifiers

10.1128/MCB.14.2.1438

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

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