Differential proteolytic sensitivity of yeast fatty acid synthetase subunits alpha and beta contributing to a balanced ratio of both fatty acid synthetase components (Q27929975)

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scientific article published on February 1, 1992

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English	Differential proteolytic sensitivity of yeast fatty acid synthetase subunits alpha and beta contributing to a balanced ratio of both fatty acid synthetase components	scientific article published on February 1, 1992

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scholarly article

1 reference

PubMed publication ID

1 December 2016

Differential proteolytic sensitivity of yeast fatty acid synthetase subunits alpha and beta contributing to a balanced ratio of both fatty acid synthetase components (English)

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PubMed publication ID

1 December 2016

0 references

1 reference

based on heuristic

inferred from title

Tetrafunctional fatty acid synthase subunit FAS1 YKL182W

1 reference

GOA release 2020-03-11

Trifunctional fatty acid synthase subunit FAS2 YPL231W

1 reference

GOA release 2020-03-11

1 reference

10.1111/J.1432-1033.1992.TB16590.X

https://api.crossref.org/works/10.1111/J.1432-1033.1992.TB16590.X

12 November 2022

author name string

H. J. Schüller

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1735446

12 November 2022

B. Förtsch

2

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1735446

12 November 2022

B. Rautenstrauss

3

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Europe PubMed Central

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12 November 2022

D. H. Wolf

4

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Europe PubMed Central

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12 November 2022

E. Schweizer

5

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Europe PubMed Central

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12 November 2022

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publication date

1 February 1992

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full work available at URL

https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1992.tb16590.x

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10.1111/J.1432-1033.1992.TB16590.X

https://api.crossref.org/works/10.1111/J.1432-1033.1992.TB16590.X

12 November 2022

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1992.tb16590.x/fullpdf

1 reference

10.1111/J.1432-1033.1992.TB16590.X

https://api.crossref.org/works/10.1111/J.1432-1033.1992.TB16590.X

12 November 2022

1 reference

PubMed publication ID

1 December 2016

203

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3

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607-14

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

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[12] One-step gene disruption in yeast

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RNA polymerase II: subunit structure and function

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Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases

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Processing pathway for protease B of Saccharomyces cerevisiae

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Effects of glucose and nitrogen source on the levels of proteinases, peptidases, and proteinase inhibitors in yeast

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Saccharomyces cerevisiae coordinates accumulation of yeast ribosomal proteins by modulating mRNA splicing, translational initiation, and protein turnover

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The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay

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Control of Fatty-Acid Synthetase Levels by Exogeneous Long-Chain Fatty Acids in the Yeasts Candida lipolytica and Saccharomyces cerevisiae

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Control of fatty-acid synthetase biosynthesis in Saccharomyces cerevisiae

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The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains.

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Proteinases, proteolysis and biological control in the yeast Saccharomyces cerevisiae

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Gene Linkage and Gene-Enzyme Relations in the Fatty-Acid-Synthetase System of Saccharomyces cerevisiae

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Purification and Characterization of Macromolecular Inhibitors of Proteinase A from Yeast

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Molecular cloning of the yeast fatty acid synthetase genes, FAS1 and FAS2: Illustrating the structure of the FAS1 cluster gene by transcript mapping and transformation studies

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High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A Saccharomyces cerevisiae mutant defective in saturated fatty acid biosynthesis

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Journal of Biological Chemistry

40

261

6835

author name string

Dice J. F.

publication date

1986

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The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein

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10.1111/J.1432-1033.1992.TB16590.X

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PubMed publication ID

1 reference

PubMed publication ID

1 December 2016

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