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Article

N-Ras forms dimers at POPC membranes.

Biophysical journal - 3 Oct 2012

Güldenhaupt Jörn, Rudack Till, Bachler Peter, Mann Daniel, Triola Gemma, Waldmann Herbert, Kötting Carsten, Gerwert Klaus

Abstract excerpt

Ras is a central regulator of cellular signaling pathways. It is mutated in 20-30% of human tumors. To perform its function, Ras has to be bound to a membrane by a posttranslationally attached lipid anchor. Surprisingly, we identified here dimerization of membrane anchored Ras by combining attenuated total reflectance Fourier transform infrared spectroscopy, biomolecular simulations, and Förster resonance energy...

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Share to Fluorescence Resonance Energy Transfer
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 23062351
DOI: 10.1016/j.bpj.2012.08.043
PMCID: PMC3471449

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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