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Article

Studies of receptor tyrosine kinase transmembrane domain interactions: the EmEx-FRET method.

The Journal of membrane biology - 1 Feb 2007

Merzlyakov Mikhail, Chen Lirong, Hristova Kalina

Abstract excerpt

The energetics of transmembrane (TM) helix dimerization in membranes and the thermodynamic principles behind receptor tyrosine kinase (RTK) TM domain interactions during signal transduction can be studied using Förster resonance energy transfer (FRET). For instance, FRET studies have yielded the...

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Share to Amino Acid Substitution
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

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Share to Protein Structure, Tertiary

Share to Receptor, Fibroblast Growth Factor, Type 3

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Source

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Identifiers

PMID: 17565424
DOI: 10.1007/s00232-007-9009-0
PMCID: PMC2770890

Genes

FGFR3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17565424-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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