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Article

A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1.

The Journal of biological chemistry - 11 Aug 2006

Noordeen Nafeesa A, Carafoli Federico, Hohenester Erhard, Horton Michael A, Leitinger Birgit

Abstract excerpt

Receptor tyrosine kinases of the discoidin domain family, DDR1 and DDR2, are activated by different types of collagen and play important roles in cell adhesion, migration, proliferation, and matrix remodeling. In a previous study, we found that collagen binding by the discoidin domain receptors (DDRs) requires dimerization of their extracellular domains (Leitinger, B. (2003) J. Biol. Chem. 278, 16761-16769),...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16774916
DOI: 10.1074/jbc.M603233200

Genes

DDR1
DDR2

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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