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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt

Peso, Luis del, González-Garcı́a, Maribel, Page, Carmen, Herrera, Román, Nuñez, Gabriel·1997·Science
DOI 10.1126/science.278.5338.687
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Abstract

BAD is a distant member of the Bcl-2 family that promotes cell death. Phosphorylation of BAD prevents this. BAD phosphorylation induced by interleukin-3 (IL-3) was inhibited by specific inhibitors of phosphoinositide 3-kinase (PI 3-kinase). Akt, a survival-promoting serine-threonine protein kinase, was activated by IL-3 in a PI 3-kinase–dependent manner. Active, but not inactive, forms of Akt were found to phosphorylate BAD in vivo and in vitro at the same residues that are phosphorylated in response to IL-3. Thus, the proapoptotic function of BAD is regulated by the PI 3-kinase–Akt pathway.

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Crossref · 10.1126/science.278.5338.687

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1 of 1 references verified0 citation errors · 0 not checkable

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Research works printed but not linked: 23

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Metadata

Authors
Peso, L. D., González-Garcı́a, M., Page, C., Herrera, R., & Nuñez, G.
Affiliations
L. del Peso, M. González-Garcı́a, C. Page, G. Nuñez, Department of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1997-10-24
Volume
278
Issue
5338
Pages
687-689
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.278.5338.687
Cited by
1,797
References
1
Language
en

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