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The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product

Crews, Craig M., Alessandrini, Alessandro, Erikson, Raymond L.·1992·Science

Abstract

Mitogen-activated protein (MAP) kinases, also known as extracellular signal-regulated kinases (ERKs), are thought to act at an integration point for multiple biochemical signals because they are activated by a wide variety of extracellular signals, rapidly phosphorylated on threonine and tyrosine, and highly conserved. A critical protein kinase lies upstream of MAP kinase and stimulates the enzymatic activity of MAP kinase. The structure of this protein kinase, denoted MEK1, for M AP kinase or E RK k inase, was elucidated from a complementary DNA sequence and shown to be a protein of 393 amino acids (43,500 daltons) that is related most closely in size and sequence to the product encoded by the Schizosaccharomyces pombe byr1 gene. The MEK gene was highly expressed in murine brain, and the product expressed in bacteria phosphorylated the ERK gene product.

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Metadata

Authors
Crews, C. M., Alessandrini, A., & Erikson, R. L.
Venue
Science
Published
1992-10-16
Volume
258
Issue
5081
Pages
478-480
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1992494265
Cited by
913
References
0
FWCI
37.41
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product. https://app.cochat.ai/papers/10.1126/science.1411546
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Crews, C. M., Alessandrini, A., & Erikson, R. L. (1992). The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product. Science. https://doi.org/10.1126/science.1411546

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.