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The substitution of glycine 661 by arginine in type III collagen produces mutant molecules with different thermal stabilities and causes Ehlers-Danlos syndrome type IV.
Previous studies have shown that Ehlers-Danlos syndrome type IV (EDS IV) is caused by mutations of type III collagen (COL3A1). Here we have characterised the most amino-terminal glycine substitution so far described in a patient with EDS IV. A combination of peptide mapping and chemical cleavage ana...
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| Hauptverfasser: | , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
1993
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1016501/ https://ncbi.nlm.nih.gov/pubmed/8411057 |
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