Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Biochemical Journal

• Publication date

  2006-02-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1042/BJ20051213PMID 16201971PMCID PMC1360733
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The Ca2+/Calmodulin-dependent Protein Kinase Kinases Are AMP-activated Protein Kinase Kinases*

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• The Reg1-interacting Proteins, Bmh1, Bmh2, Ssb1, and Ssb2, Have Roles in Maintaining Glucose Repression in Saccharomyces cerevisiae*

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• Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases

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• Elm1p is one of three upstream kinases for the Saccharomyces cerevisiae SNF1 complex.

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• Isolation of Mutations in the Catalytic Domain of the Snf1 Kinase That Render Its Activity Independent of the Snf4 Subunit

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  2002cited by this paper
• Purification and Characterization of Snf1 Kinase Complexes Containing a Defined β Subunit Composition*

  2002influential reference
• Purification and characterization of Snf1 kinase complexes containing a defined Beta subunit composition.

  2002cited by this paper
• Functional organization of the yeast proteome by systematic analysis of protein complexes

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• Regulation of Snf1 Kinase ACTIVATION REQUIRES PHOSPHORYLATION OF THREONINE 210 BY AN UPSTREAM KINASE AS WELL AS A DISTINCT STEP MEDIATED BY THE Snf4 SUBUNIT*

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  2019cites this paper
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  2017cites this paper
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  2017cites this paper
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