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Cited by 195

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

Evidence for Two Catalytically Active Kinase Domains in pp90 rsk

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Fisher, Tracey L., Blenis, John·1996·Molecular and Cellular Biology

Abstract

Mitogen-activated protein kinase and one of its targets, pp90rsk (ribosomal S6 kinase [RSK]), represent two serine/threonine kinases in the Ras-activated signalling cascade that are capable of directly regulating gene expression. pp90rsk has been shown to have two highly conserved and distinct catalytic domains. However, whether both domains are active and which domain is responsible for its various identified phosphotransferase activities have not been determined. Here we demonstrate that the N-terminal domain is responsible for its phosphotransferase activity towards a variety of substrates which contain an RXXS motif at the site of in vitro phosphorylation, including serum response factor, c-Fos, Nur77, and the 40S ribosomal protein S6. We also provide evidence that the C-terminal domain is catalytically active and can be further activated by mitogen-activated protein kinase phosphorylation.

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Crossref · 10.1128/mcb.16.3.1212

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Metadata

Authors
Fisher, T. L., & Blenis, J.
Venue
Molecular and Cellular Biology
Published
1996-03
Volume
16
Issue
3
Pages
1212-1219
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W1860814838
Cited by
195
References
1
FWCI
3.71
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Evidence for Two Catalytically Active Kinase Domains in pp90 rsk. https://app.cochat.ai/papers/10.1128/mcb.16.3.1212
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Fisher, T. L., & Blenis, J. (1996). Evidence for Two Catalytically Active Kinase Domains in pp90 rsk. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.16.3.1212

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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