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

Differential effect of FBN1 mutations on in vitro proteolysis of recombinant fibrillin-1 fragments.

Human genetics - 1 Sept 2000

Booms P, Tiecke F, Rosenberg T, Hagemeier C, Robinson P N

Abstract excerpt

Mutations in the fibrillin-1 gene (FBN1) cause Marfan syndrome (MFS), an autosomal dominant disorder of connective tissue with highly variable clinical manifestations. FBN1 contains 47 epidermal growth factor (EGF)-like modules, 43 of which display a consensus sequence for calcium binding (cbEGF). Calcium binding by cbEGF modules is thought to be essential for the conformation and stability of fibrillin-1....

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Ectopia Lentis
Share to Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fibrillin-1

Share to Fibrillins

Share to Marfan Syndrome

Share to Microfilament Proteins

Share to Peptide Fragments

Source

Identifiers

PMID: 11071382
DOI: 10.1007/s004390000368

Genes

FBN1
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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Differential effect of FBN1 mutations on in vitro proteolysis of recombinant fibrillin-1 fragments.PMID 11071382Read ↗

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 ↗

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

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

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

Clustering of fibrillin (FBN1) missense mutations in Marfan syndrome patients at cysteine residues in EGF-like domains.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 ↗

The extracellular matrix glycoprotein fibrillin-1 in health and diseaseSemantic 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 ↗

Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1.Semantic proximity Read ↗

Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1.Semantic proximity Read ↗

Fibrillin-1 Misfolding and DiseaseSemantic proximity Read ↗

A novel fibrillin-1 gene missense mutation associated with neonatal Marfan syndrome: a case report and review of the mutation spectrum.Semantic proximity Read ↗

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