{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,2]],"date-time":"2026-08-02T22:06:13Z","timestamp":1785708373772,"version":"3.56.0"},"reference-count":13,"publisher":"BMJ","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Med Genet"],"published-print":{"date-parts":[[1993,8]]},"abstract":"<jats:p>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 analysis of cDNA localised the mutation in cyanogen bromide peptide CB5. Sequence analysis showed a G to A mutation, converting glycine 661 to arginine, which was a new dominant mutation. Analysis of type III collagen secreted by cultured fibroblasts showed an overmodified mutant protein with normal thermal stability. However, the intracellularly retained form melted 2 degrees C lower than normal. This indicated that molecules resulting from the same mutation can differ in their thermal stabilities.<\/jats:p>","DOI":"10.1136\/jmg.30.8.690","type":"journal-article","created":{"date-parts":[[2008,11,10]],"date-time":"2008-11-10T15:23:16Z","timestamp":1226330596000},"page":"690-693","source":"Crossref","is-referenced-by-count":8,"title":["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."],"prefix":"10.1136","volume":"30","author":[{"given":"A","family":"Richards","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Narcisi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J","family":"Lloyd","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C","family":"Ferguson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F M","family":"Pope","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"239","published-online":{"date-parts":[[1993,8,1]]},"reference":[{"key":"ref_1","first-page":"292","article-title":"Heritable disorders of connective tissue","author":"McKusick, V.A.","year":"1972","unstructured":"McKusick VA. Heritable disorders of connective tissue. 4th ed. St Louis: Mosby, 1972:292-371.","edition":"4th ed"},{"key":"ref_2","first-page":"351","article-title":"tissue and its heritable disorders, molecular genetic and medical aspects","author":"Steinmann, B.","year":"1993","unstructured":"Steinmann B, Royce PM, Superti-Furga A. In: Royce PM, Steinmann B, eds. Connective tissue and its heritable disorders, molecular genetic and medical aspects. New York: Wiley Liss, 1993:351-407."},{"key":"ref_3","first-page":"414","article-title":"A single base mutation in the gene for type III collagen (COL3A1) converts glycine 847 to glutamic acid in a family with Ehlers-Danlos syndrome type IV. An unaffected family member is mosaic for the mutation","volume":"89","author":"Richards, A.J.; Ward, P.N.; Narcisi, P.; Nicholls, A.C.; Lloyd, J.C.; Pope, F.M.","year":"1992","unstructured":"Richards AJ, Ward PN, Narcisi P, Nicholls AC, Lloyd JC, Pope FM. 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Linkage of a polymorphic marker for the type III collagen gene (COL3A1) to atypical autosomal dominant Ehlers-Danlos syndrome type IV in a large Belgian pedigree. Hum Genet 1988;78:276-81.","journal-title":"Hum Genet"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1136\/jmg.28.7.458","article-title":"Characterisation of a glycine to valine substitution at amino acid position 910 of the triple helical region of type III collagen in a patient with Ehlers-Danlos syndrome type IV","volume":"28","author":"Richards, A.J.; Lloyd, J.C.; Ward, P.N.; De Paepe, A.; Narcisi, P.; Pope, F.M.","year":"1991","unstructured":"Richards AJ, Lloyd JC, Ward PN, De Paepe A, Narcisi P, Pope FM. Characterisation of a glycine to valine substitution at amino acid position 910 of the triple helical region of type III collagen in a patient with Ehlers-Danlos syndrome type IV. Med Genet 1991;28:458-63.","journal-title":"Med Genet"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1007\/BF00197268","article-title":"A 27 bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV","volume":"88","author":"Richards, A.J.; Lloyd, J.C.; Narcisi, P.; Ward, P.N.; Nicholls, A.C.; De Paepe, A.; Pope, F.M.","year":"1992","unstructured":"Richards AJ, Lloyd JC, Narcisi P, Ward PN, Nicholls AC, De Paepe A, Pope FM. A 27 bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV. Hum Genet 1992;88:325-30.","journal-title":"Hum Genet"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1002\/ajmg.1320460308","article-title":"Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV","volume":"46","author":"Narcisi, P.; Wu, Y.; Tromp, G.","year":"1993","unstructured":"Narcisi P, Wu Y, Tromp G, et al. Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV. Am Med Genet 1993;46:278-83.","journal-title":"Am Med Genet"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1042\/bj2600509","article-title":"Structure of cDNA clones coding for the entire pre-proal(III) chain of human type III procollagen: differences in protein structure from type I procollagen and conservation of codon preferences","volume":"260","author":"Ala-Kokko, L.; Kontusaari, S.; Baldwin, C.T.; Kuivaniemi, H.; Prockop, D.J.","year":"1989","unstructured":"Ala-Kokko L, Kontusaari S, Baldwin CT, Kuivaniemi H, Prockop DJ. Structure of cDNA clones coding for the entire pre-proal(III) chain of human type III procollagen: differences in protein structure from type I procollagen and conservation of codon preferences. Biochem 1989;260:509-16.","journal-title":"Biochem"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1465","DOI":"10.1172\/JCI114863","article-title":"A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms","volume":"86","author":"Kontusaari, S.; Tromp, G.; Kuivaniemi, H.; Romanic, A.M.; Prockop, D.J.","year":"1990","unstructured":"Kontusaari S, Tromp G, Kuivaniemi H, Romanic AM, Prockop DJ. A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms. Clin Invest 1990;86:1465-73.","journal-title":"Clin Invest"},{"issue":"34","key":"ref_13","first-page":"17","article-title":"A mutation that substitutes Arg for Gly 136 in collagen III identified in a patient with fibromuscular dysplasia and an aortic aneurysm","volume":"13","author":"Earley, J.; Tromp, G.; Kuivaniemi, H.; Gatalica, Z.; Prockop, D.J.","year":"1993","unstructured":"Earley J, Tromp G, Kuivaniemi H, Gatalica Z, Prockop DJ. A mutation that substitutes Arg for Gly 136 in collagen III identified in a patient with fibromuscular dysplasia and an aortic aneurysm. Matrix 1993;13:34A. 17 Nuytinck L, Narcisi P, Nicholls A, Renard JP, Pope FM, De Paepe A. Detection and characterisation of an overmodified type III collagen by analysis of non-cutaneous connective tissues in a patient with Ehlers-Danlos syndrome IV. J7 Med Genet 1992;29:375-80.","journal-title":"Matrix; Detection and characterisation of an overmodified type III collagen by analysis of non-cutaneous connective tissues in a patient with Ehlers-Danlos syndrome IV"}],"container-title":["Journal of Medical Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1136\/jmg.30.8.690","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,17]],"date-time":"2025-10-17T20:17:18Z","timestamp":1760732238000},"score":1,"resource":{"primary":{"URL":"https:\/\/jmg.bmj.com\/lookup\/doi\/10.1136\/jmg.30.8.690"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,8]]},"references-count":13,"journal-issue":{"issue":"8","published-online":{"date-parts":[[1993,8,1]]},"published-print":{"date-parts":[[1993,8]]}},"alternative-id":["10.1136\/jmg.30.8.690"],"URL":"https:\/\/doi.org\/10.1136\/jmg.30.8.690","relation":{},"ISSN":["0022-2593","1468-6244"],"issn-type":[{"value":"0022-2593","type":"print"},{"value":"1468-6244","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,8]]}}}