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Article

Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.

Journal of molecular biology - 8 Nov 1996

Langosch D, Brosig B, Kolmar H, Fritz H J

Abstract excerpt

Specific interactions between membrane spanning polypeptide segments are important for folding and oligomerisation of integral membrane proteins. Previously the dimerisation of glycophorin A has been shown to depend on interactions between its transmembrane segment by studying chimeric proteins i...

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Identifiers

PMID: 8918935
DOI: 10.1006/jmbi.1996.0595

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8918935-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.PMID 8918935Read ↗

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Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer.Semantic proximity Read ↗

Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations.Semantic proximity Read ↗

Mutations in toxR and toxS that separate transcriptional activation from DNA binding at the cholera toxin gene promoter.Semantic proximity Read ↗

Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif.Semantic proximity Read ↗

Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer.Semantic proximity Read ↗

Motifs of serine and threonine can drive association of transmembrane helices.Semantic proximity Read ↗

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