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Article

Formation of a disulfide bond in the immunoglobulin domain of the myelin P0 protein is essential for its adhesion.

Journal of neurochemistry - 1 Jul 1994

Zhang K, Filbin M T

Abstract excerpt

It is widely accepted, although never demonstrated, that the formation of a disulfide bond in the majority of immunoglobulin (Ig)-like domains stabilizes their final conformation and thus is essential to their functioning as adhesion/recognition molecules. The myelin P0 protein, which has been shown directly to behave as a homophilic adhesion molecule, contains a single Ig-like domain, stabilized by a putative...

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PMID: 7515951
DOI: 10.1046/j.1471-4159.1994.63010367.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Formation of a disulfide bond in the immunoglobulin domain of the myelin P0 protein is essential for its adhesion.PMID 7515951Read ↗

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Structural bases for the Charcot-Marie-Tooth disease induced by single amino acid substitutions of myelin protein zero.Semantic proximity Read ↗

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How Does Protein Zero Assemble Compact Myelin?Semantic proximity Read ↗

Structural bases for the Charcot–Marie–Tooth disease induced by single amino acid substitutions of myelin protein zeroSemantic proximity Read ↗

Conservation of topology, but not conformation, of the proteolipid proteins of the myelin sheath.Semantic proximity Read ↗

New mutation of the myelin P0 gene in a pedigree of Charcot-Marie-Tooth neuropathy 1.Semantic proximity Read ↗

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Charcot-Marie-Tooth neuropathy type 1B is associated with mutations of the myelin P0 gene.Semantic proximity Read ↗

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