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Cited by 1,435

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?

Open access
Hardie, D. Grahame, Carling, David, Carlson, Marian·1998·Annual Review of Biochemistry

Abstract

Mammalian AMP-activated protein kinase and yeast SNF1 protein kinase are the central components of kinase cascades that are highly conserved between animals, fungi, and plants. The AMP-activated protein kinase cascade acts as a metabolic sensor or “fuel gauge” that monitors cellular AMP and ATP levels because it is activated by increases in the AMP:ATP ratio. Once activated, the enzyme switches off ATP-consuming anabolic pathways and switches on ATP-producing catabolic pathways, such as fatty acid oxidation. The SNF1 complex in yeast is activated in response to the stress of glucose deprivation. In this case the intracellular signal or signals have not been identified; however, SNF1 activation is associated with depletion of ATP and elevation of AMP. The SNF1 complex acts primarily by inducing expression of genes required for catabolic pathways that generate glucose, probably by triggering phosphorylation of transcription factors. SNF1-related protein kinases in higher plants are likely to be involved in the response of plant cells to environmental and/or nutritional stress.

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Metadata

Authors
Hardie, D. G., Carling, D., & Carlson, M.
Venue
Annual Review of Biochemistry
Published
1998-06
Volume
67
Issue
1
Pages
821-855
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2147594695
Cited by
1,435
References
6
FWCI
3.08
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell? https://app.cochat.ai/papers/10.1146/annurev.biochem.67.1.821
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Hardie, D. G., Carling, D., & Carlson, M. (1998). THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell? Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.67.1.821

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