Cited by 126HER2/EGFR in Cancer ResearchLung Cancer Treatments and MutationsProtein Kinase Regulation and GTPase Signaling

Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations

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Littlefield, Peter, Liu, Lijun, Mysore, Venkatesh, Shan, Yibing, Shaw, David E., Jura, Natalia·2014·Science Signaling

Abstract

Cancer-associated mutations in the catalytically inactive receptor HER3 enhance its ability to activate other members of the human epidermal growth factor receptor family.

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Authors
Littlefield, P., Liu, L., Mysore, V., Shan, Y., Shaw, D. E., & Jura, N.
Affiliations
  • University of California, San Francisco (US)
  • D. E. Shaw Research (US)
Corresponding author
Jura, Natalia
Venue
Science Signaling
Published
2014-12-02
Volume
7
Issue
354
Pages
ra114-ra114
ISSN
  • 1937-9145 (ISSN-L)
  • 1945-0877
OpenAlex
W2157884341
Cited by
126
References
69
Citations by year
2026: 7 · 2025: 7 · 2024: 6 · 2023: 12 · 2022: 12 · 2021: 15 · 2020: 13 · 2019: 14 · 2018: 13 · 2017: 10 · 2016: 9 · 2015: 6 · 2014: 2
FWCI
4.34
Type
journal article
Language
en
Open access
Locations
  • Science Signaling (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • U.S. Public Health Service (R01 RGM109176A)
  • National Institute of General Medical Sciences (R01GM109176)
Topics
  • Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
  • Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
HER3, EGFR, heterodimerization, allosteric activation, kinase domain crystal structure, cancer-associated mutations, dimer interface, HER2, receptor tyrosine kinase signaling
MeSH terms
Cloning, Molecular, Crystallization, Humans, Models, Molecular, Mutation, Signal Transduction, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Dimerization, Receptor, ErbB-3, Molecular Dynamics Simulation, ErbB Receptors

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