{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T00:06:07Z","timestamp":1768262767576,"version":"3.49.0"},"reference-count":48,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2004,6,1]],"date-time":"2004-06-01T00:00:00Z","timestamp":1086048000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Genetics and Metabolism"],"published-print":{"date-parts":[[2004,6]]},"DOI":"10.1016\/j.ymgme.2004.03.004","type":"journal-article","created":{"date-parts":[[2004,5,11]],"date-time":"2004-05-11T11:57:10Z","timestamp":1084276630000},"page":"144-153","source":"Crossref","is-referenced-by-count":8,"title":["Potential modifier role of the R618Q variant of pro\u03b12(I)collagen in type I collagen fibrillogenesis: in vitro assembly analysis"],"prefix":"10.1016","volume":"82","author":[{"given":"Anthony N","family":"Vomund","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen R","family":"Braddock","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gary F","family":"Krause","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Charlotte L","family":"Phillips","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ymgme.2004.03.004_BIB1","series-title":"The Metabolic and Molecular Basis of Inherited Disease","first-page":"5241","article-title":"Disorders of collagen biosynthesis and structure","author":"Byers","year":"2001"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB2","series-title":"Connective Tissue and its Heritable Disorders","first-page":"103","article-title":"The collagen family: structure, assembly, and organization in the extracellular matrix","author":"Kielty","year":"1993"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB3","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1042\/bj1180355","article-title":"Thermodynamic studies of the assembly in vitro of native collagen fibrils","volume":"118","author":"Cooper","year":"1970","journal-title":"Biochem. J."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB4","doi-asserted-by":"crossref","first-page":"15696","DOI":"10.1016\/S0021-9258(18)47783-6","article-title":"Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase","volume":"262","author":"Kadler","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB5","doi-asserted-by":"crossref","first-page":"11888","DOI":"10.1021\/bi980089+","article-title":"Sugars and polyols inhibit fibrillogenesis of type I collagen by disrupting hydrogen-bonded water bridges between the helices","volume":"37","author":"Kuznetsova","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB6","doi-asserted-by":"crossref","first-page":"6578","DOI":"10.1016\/S0021-9258(19)46970-6","article-title":"Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results","volume":"253","author":"Williams","year":"1978","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB7","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/S0021-9258(17)30289-2","article-title":"Collagen fibril formation. Evidence for a multistep process","volume":"254","author":"Gelman","year":"1979","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB8","doi-asserted-by":"crossref","first-page":"8098","DOI":"10.1016\/S0021-9258(19)70613-9","article-title":"Collagen fibril formation in vitro. A quasielastic light-scattering study of early stages","volume":"255","author":"Gelman","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB9","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/0141-8130(86)90020-6","article-title":"Reconstitution of collagen fibrils in vitro: the assembly process depends on the initiating procedure","volume":"8","author":"Holmes","year":"1986","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB10","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1042\/bj2680339","article-title":"Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction","volume":"268","author":"Kadler","year":"1990","journal-title":"Biochem. J."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB11","doi-asserted-by":"crossref","first-page":"2124","DOI":"10.1016\/S0006-3495(95)80393-0","article-title":"Sequential assembly of collagen revealed by atomic force microscopy","volume":"68","author":"Gale","year":"1995","journal-title":"Biophys. J."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB12","doi-asserted-by":"crossref","first-page":"7745","DOI":"10.1073\/pnas.78.12.7745","article-title":"Marfan syndrome: abnormal alpha 2 chain in type I collagen","volume":"78","author":"Byers","year":"1981","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB13","series-title":"Principles and Practice in Medical Genetics","first-page":"1027","article-title":"Marfan syndrome and other disorders of fibrillin","author":"Pyeritz","year":"1997"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB14","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1056\/NEJM199007193230303","article-title":"Immunohistologic abnormalities of the microfibrillar\u2013fiber system in the Marfan syndrome","volume":"323","author":"Hollister","year":"1990","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB15","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1172\/JCI114897","article-title":"A substitution at a non-glycine position in the triple-helical domain of pro alpha 2(I) collagen chains present in an individual with a variant of the Marfan syndrome","volume":"86","author":"Phillips","year":"1990","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB16","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/S0945-053X(98)90109-3","article-title":"An alpha2(I) glycine to aspartate substitution is responsible for the presence of a kink in type I collagen in a lethal case of osteogenesis imperfecta","volume":"17","author":"Forlino","year":"1998","journal-title":"Matrix Biol."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB17","doi-asserted-by":"crossref","first-page":"28837","DOI":"10.1074\/jbc.272.46.28837","article-title":"Gly-Pro-Arg confers stability similar to Gly-Pro-Hyp in the collagen triple-helix of host\u2013guest peptides","volume":"272","author":"Yang","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB18","doi-asserted-by":"crossref","first-page":"35007","DOI":"10.1074\/jbc.M202782200","article-title":"Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47","volume":"277","author":"Tasab","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB19","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/S0934-8832(11)80077-6","article-title":"Self-assembly into fibrils of a homotrimer of type I collagen","volume":"12","author":"McBride","year":"1992","journal-title":"Matrix"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB20","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/jmbi.1997.1106","article-title":"Altered collagen structure in mouse tail tendon lacking the alpha 2(I) chain","volume":"270","author":"McBride","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB21","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/0003-2697(81)90204-9","article-title":"Proteolytic enzymes as probes for the triple-helical conformation of procollagen","volume":"110","author":"Bruckner","year":"1981","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB22","doi-asserted-by":"crossref","first-page":"7153","DOI":"10.1021\/bi00444a004","article-title":"In vitro collagen fibril assembly: thermodynamic studies","volume":"28","author":"Na","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB23","doi-asserted-by":"crossref","first-page":"1734","DOI":"10.1016\/S0021-9258(18)89655-7","article-title":"Altered triple helical structure of type I procollagen in lethal perinatal osteogenesis imperfecta","volume":"260","author":"Bonadio","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB24","unstructured":"K.R. Robbins, A method, SAS program, and example for fitting the broken line to growth data, Research Report 86-09, The University of Tennessee Agriculture Experiment Station, Knoxville, Tennessee, 1986"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB25","doi-asserted-by":"crossref","first-page":"16376","DOI":"10.1016\/S0021-9258(18)49266-6","article-title":"Ehlers\u2013Danlos syndrome type VIIB. Deletion of 18 amino acids comprising the N-telopeptide region of a pro-alpha 2(I) chain","volume":"262","author":"Wirtz","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB26","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.1016\/S0021-9258(18)52286-9","article-title":"The effects of different cysteine for glycine substitutions within alpha 2(I) chains. Evidence of distinct structural domains within the type I collagen triple helix","volume":"266","author":"Wenstrup","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB27","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/0165-022X(81)90007-5","article-title":"The addition of SDS to the Bradford dye-binding protein assay, a modification with increased sensitivity to collagen","volume":"5","author":"Duhamel","year":"1981","journal-title":"J. Biochem. Biophys. Methods"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB28","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0009-8981(67)90167-2","volume":"18","author":"Stegemann","year":"1967","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB29","series-title":"Advanced Methods of Data Exploration and Modeling","author":"Everitt","year":"1983"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB30","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0968-4328(00)00045-7","article-title":"Structural variations of collagen in normal and pathological tissues: role of electron microscopy","volume":"32","author":"Eyden","year":"2001","journal-title":"Micron"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB31","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0174-173X(82)80041-1","article-title":"Segment-long-spacing crystallites, a powerful tool in collagen research","volume":"2","author":"K\u00fchn","year":"1982","journal-title":"Collagen Rel. Res."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB32","doi-asserted-by":"crossref","first-page":"3321","DOI":"10.1021\/ja01163a553","article-title":"Electron-microscope observations of certain fibrous structures obtained from connective-tissue extracts","volume":"72","author":"Highberger","year":"1950","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB33","series-title":"Structure and Function of Collagen Types","first-page":"1","article-title":"The classical collagens: types I, II, and III","author":"K\u00fchn","year":"1987"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB34","doi-asserted-by":"crossref","first-page":"3385","DOI":"10.1073\/pnas.82.10.3385","article-title":"Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2","volume":"82","author":"Emanuel","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB35","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1093\/nar\/25.1.181","article-title":"The human type I collagen mutation database","volume":"25","author":"Dalgleish","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB36","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1093\/nar\/26.1.253","article-title":"The Human Collagen Mutation Database 1998","volume":"26","author":"Dalgleish","year":"1998","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB37","doi-asserted-by":"crossref","first-page":"8795","DOI":"10.1021\/bi960773t","article-title":"Proteodermatan and proteokeratan sulfate (decorin, lumican\/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen","volume":"35","author":"Scott","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB38","doi-asserted-by":"crossref","first-page":"36083","DOI":"10.1074\/jbc.274.51.36083","article-title":"Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? Effect of proteolytic cleavage on fibrillogenesis and on collagen\u2013collagen interaction in fibers","volume":"274","author":"Kuznetsova","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB39","doi-asserted-by":"crossref","first-page":"25870","DOI":"10.1074\/jbc.M003700200","article-title":"Possible involvement of aminotelopeptide in self-assembly and thermal stability of collagen I as revealed by its removal with proteases","volume":"275","author":"Sato","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB40","doi-asserted-by":"crossref","first-page":"2621","DOI":"10.1073\/pnas.81.9.2621","article-title":"Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: hydration forces between parallel DNA double helices","volume":"81","author":"Rau","year":"1984","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB41","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1073\/pnas.91.1.276","article-title":"Direct measurement of forces between self-assembled proteins: temperature-dependent exponential forces between collagen triple helices","volume":"91","author":"Leikin","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB42","doi-asserted-by":"crossref","first-page":"2650","DOI":"10.1016\/S0021-9258(18)45930-3","article-title":"Temperature-induced post-translational over-modification of type I procollagen","volume":"267","author":"Torre-Blanco","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB43","doi-asserted-by":"crossref","first-page":"2639","DOI":"10.1096\/fasebj.6.9.1612287","article-title":"Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues","volume":"6","author":"Scott","year":"1992","journal-title":"FASEB J."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB44","series-title":"Dermatan Sulphate Proteoglycans: Chemistry, Biology, Chemical Pathology","first-page":"81","article-title":"Proteoglycan\u2013fibrillar collagen interactions in tissues: dermatan sulphate proteoglycan as a tissue organizer","author":"Scott","year":"1993"},{"key":"10.1016\/j.ymgme.2004.03.004_BIB45","doi-asserted-by":"crossref","first-page":"21801","DOI":"10.1074\/jbc.C000278200","article-title":"Decorin binds near the C terminus of type I collagen","volume":"275","author":"Keene","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB46","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1007\/s000180050048","article-title":"Independent modulation of collagen fibrillogenesis by decorin and lumican","volume":"57","author":"Neame","year":"2000","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB47","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1042\/bj2420761","article-title":"Dermatan sulphate proteoglycans from sclera examined by rotary shadowing and electron microscopy","volume":"242","author":"Ward","year":"1987","journal-title":"Biochem. J."},{"key":"10.1016\/j.ymgme.2004.03.004_BIB48","doi-asserted-by":"crossref","first-page":"4223","DOI":"10.1074\/jbc.M110709200","article-title":"Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen","volume":"277","author":"Di Lullo","year":"2002","journal-title":"J. Biol. Chem."}],"container-title":["Molecular Genetics and Metabolism"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1096719204001064?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1096719204001064?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,17]],"date-time":"2021-06-17T13:00:54Z","timestamp":1623934854000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1096719204001064"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,6]]},"references-count":48,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2004,6]]}},"alternative-id":["S1096719204001064"],"URL":"https:\/\/doi.org\/10.1016\/j.ymgme.2004.03.004","relation":{},"ISSN":["1096-7192"],"issn-type":[{"value":"1096-7192","type":"print"}],"subject":[],"published":{"date-parts":[[2004,6]]}}}