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- aggregation classification "A1".
- aggregation creator B88923.
- aggregation creator B88924.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "1997".
- aggregation format "application/pdf".
- aggregation hasFormat 182216.bibtex.
- aggregation hasFormat 182216.csv.
- aggregation hasFormat 182216.dc.
- aggregation hasFormat 182216.didl.
- aggregation hasFormat 182216.doc.
- aggregation hasFormat 182216.json.
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- aggregation hasFormat 182216.txt.
- aggregation hasFormat 182216.xls.
- aggregation hasFormat 182216.yaml.
- aggregation isPartOf urn:issn:0002-9297.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I and II".
- aggregation abstract "The Ehlers-Danlos syndrome (EDS) is a heterogeneous connective-tissue disorder of which at least nine subtypes are recognized. Considerable clinical overlap exists between the EDS I and II subtypes, suggesting that both are allelic disorders. Recent evidence based on linkage and transgenic mice studies suggest that collagen V is causally involved in human EDS. Collagen V forms heterotypic fibrils with collagen I in many tissues and plays an important role in collagen I fibrillogenesis. We have identified a mutation in COL5A1, the gene encoding the proal(V) collagen chain, segregating with EDS I in a four-generation family. The mutation causes the substitution of the most 5' cysteine residue by a serine within a highly conserved sequence of the proal(V) C-propeptide domain and causes reduction of collagen V by preventing incorporation of the mutant proal(V) chains in the collagen V trimers. In addition, we have detected splicing defects in the COL5A1 gene in a patient with EDS I and in a family with EDS II. These findings confirm the causal role of collagen V in at least a subgroup of EDS I, prove that EDS I and II are allelic conditions, and represent a, so far, unique example of a human collagen disorder caused by substitution of a highly conserved cysteine residue in the C-propeptide domain of a fibrillar collagen.".
- aggregation authorList BK229595.
- aggregation endPage "554".
- aggregation issue "3".
- aggregation startPage "547".
- aggregation volume "60".
- aggregation aggregates 1040604.
- aggregation isDescribedBy 182216.
- aggregation similarTo LU-182216.