Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.

The Journal of biological chemistry - 30 Jul 2004

Vollbrandt Tillman, Tiedemann Kerstin, El-Hallous Ehab, Lin Guoqing, Brinckmann Jürgen, John Harald, Bätge Boris, Notbohm Holger, Reinhardt Dieter P

Abstract excerpt

Mutations in fibrillin-1 lead to Marfan syndrome and some related genetic disorders. Many of the more than 600 mutations currently known in fibrillin-1 eliminate or introduce cysteine residues in epidermal growth factor-like modules. Here we report structural and functional consequences of three selected cysteine mutations (R627C, C750G, and C926R) in fibrillin-1. The mutations have been analyzed by means of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Circular Dichroism
Share to Cysteine

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

Share to Epidermal Growth Factor

Share to Epitope Mapping

Share to Fibrillin-1

Share to Fibrillins

Share to Microfilament Proteins

Share to Ultraviolet Rays

Source

Identifiers

PMID: 15161917
DOI: 10.1074/jbc.M405239200

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.PMID 15161917Read ↗

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 ↗

Cysteine substitutions in epidermal growth factor-like domains of fibrillin-1: distinct effects on biochemical and clinical phenotypes.Semantic 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 ↗

Fibrillin-1 Misfolding and DiseaseSemantic proximity Read ↗

Differential effect of FBN1 mutations on in vitro proteolysis of recombinant fibrillin-1 fragments.Semantic proximity Read ↗

Defective secretion of recombinant fragments of fibrillin-1: implications of protein misfolding for the pathogenesis of Marfan syndrome and related disorders.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 ↗

Fibrillin domain folding and calcium binding: significance to Marfan syndrome.Semantic proximity Read ↗

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

Structural consequences of cysteine substitutions C1977Y and C1977R in calcium-binding epidermal growth factor-like domain 30 of human fibrillin-1.Semantic proximity Read ↗

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

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

⌁Select a neighboring publication to make it the new centre.