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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Structure of the LKB1-STRAD-MO25 Complex Reveals an Allosteric Mechanism of Kinase Activation

Open access
Zeqiraj, Elton, Filippi, Beatrice Maria, Deak, Maria, Alessi, Dario R., van Aalten, Daan M. F.·2009·Science

Abstract

Solving Pseudokinases: Mutations of the protein kinase LKB1 are associated with cancer in humans. Many kinases are activated by phosphorylation, but LKB1 is activated by STRADα, a pseudokinase that is similar to protein kinases and binds ATP, but does not phosphorylate substrates. By solving the crystal structure of an activating complex containing LKB, Zeqiraj et al. (p. 1707 , published online 5 November) show that STRADα works with another protein, MO25α, to hold LKB1 in an active conformation. The results may help explain the evolutionary origin of pseudokinases, the biological roles of other pseudokinases, and the mechanisms of disease-causing mutations in LKB1.

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Metadata

Authors
Zeqiraj, E., Filippi, B. M., Deak, M., Alessi, D. R., & van Aalten, D. M. F.
Venue
Science
Published
2009-12-18
Volume
326
Issue
5960
Pages
1707-1711
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2127192155
Cited by
365
References
5
FWCI
8.76
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Structure of the LKB1-STRAD-MO25 Complex Reveals an Allosteric Mechanism of Kinase Activation. https://app.cochat.ai/papers/10.1126/science.1178377
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Zeqiraj, E., Filippi, B. M., Deak, M., Alessi, D. R., & van Aalten, D. M. F. (2009). Structure of the LKB1-STRAD-MO25 Complex Reveals an Allosteric Mechanism of Kinase Activation. Science. https://doi.org/10.1126/science.1178377

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