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Article

Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.

The Journal of biological chemistry - 1 Jul 2024

Wirth Daniel, Özdemir Ece, Wimley William C, Pasquale Elena B, Hristova Kalina

Abstract excerpt

The transmembrane helices of receptor tyrosine kinases (RTKs) have been proposed to switch between two different dimeric conformations, one associated with the inactive RTK and the other with the active RTK. Furthermore, recent work has demonstrated that some full-length RTKs are associated into oligomers that are larger than dimers, raising questions about the roles of the TM helices in the assembly and function...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 38838777
DOI: 10.1016/j.jbc.2024.107441
PMCID: PMC11263659

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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