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

Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome

1 Jan 1993

Abstract excerpt

Marfan syndrome results from mutations in an extracellular matrix glycoprotein, fibrillin. Previous studies have characterized approximately 6.9-kb of the estimated 10-kb fibrillin transcript. We have now completed the primary structure of fibrillin, elucidated the exon/intron organization of the gene and derived a physical map of the genetic locus. Pre-fibrillin consists of 2,871 amino acids which, excluding the...

Read the complete abstract on PubMed

Topics

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

Share to Cardiac Valve Diseases and Treatments
Share to Connective tissue disorders research
Share to Protease and Inhibitor Mechanisms

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

Source

Identifiers

PMID: 8268958
DOI: 10.1093/hmg/2.10.1762

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

Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndromePMID 8268958Read ↗

The fibrillin-Marfan syndrome connection.Semantic proximity Read ↗

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

Fibrillln mutations in Marfan syndrome and related phenotypes.Semantic proximity Read ↗

Fibrillin Binds Calcium and Is Coded by cDNAs That Reveal a Multidomain Structure and Alternatively Spliced Exons at the 5′ EndSemantic proximity Read ↗

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

Structure and function of the mammalian fibrillin gene family: implications for human connective tissue diseases.Semantic proximity Read ↗

Fibrillin-containing microfibrils: structure and function in health and disease.Semantic proximity Read ↗

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

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

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

The molecular basis of Marfan syndrome.Semantic proximity Read ↗

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