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Article

Fibrillin domain folding and calcium binding: significance to Marfan syndrome.

Chemistry & biology - 1 Feb 1995

Wu Y S, Bevilacqua V L, Berg J M

Abstract excerpt

BACKGROUND: Marfan syndrome is a heritable disorder of connective tissue which has been associated with mutations in a gene encoding fibrillin, a 350 kD glycoprotein found in microfibrils. This protein consists of approximately 60 domains, 47 of which have similarity to epidermal growth factor (EGF). The first mutations to be detected were found in two sporadic cases that had identical Arg to Pro changes within...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 9383409
DOI: 10.1016/1074-5521(95)90281-3

Genes

EGF

Provenance

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.

Related research

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Fibrillin domain folding and calcium binding: significance to Marfan syndrome.PMID 9383409Read ↗

The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1.Semantic proximity Read ↗

Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndromeSemantic proximity Read ↗

Fibrillin-1, a calcium binding protein of extracellular matrix.Semantic proximity Read ↗

The fibrillin-Marfan syndrome connection.Semantic proximity Read ↗

Substitution of a cysteine residue in a non-calcium binding, EGF-like domain of fibrillin segregates with the Marfan syndrome in a large kindred.Semantic proximity Read ↗

Mutations in calcium-binding epidermal growth factor modules render fibrillin-1 susceptible to proteolysis. A potential disease-causing mechanism in Marfan syndrome.Semantic proximity Read ↗

Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.Semantic proximity Read ↗

A Gly --> Ser change causes defective folding in vitro of calcium-binding epidermal growth factor-like domains from factor IX and fibrillin-1.Semantic proximity Read ↗

Cellular and molecular studies of Marfan syndrome mutations identify co-operative protein folding in the cbEGF12-13 region of fibrillin-1.Semantic proximity Read ↗

Fibrillin-1 Misfolding and DiseaseSemantic proximity Read ↗

Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory TGFβ-binding siteSemantic proximity Read ↗

A G1127S change in calcium-binding epidermal growth factor-like domain 13 of human fibrillin-1 causes short range conformational effects.Semantic proximity Read ↗

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