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Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomers.
J Biol Chem. 1988 Jul 25;263(21):10517-23
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A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away.
J Biol Chem. 1988 Dec 15;263(35):19249-55
PMID: 3198624
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Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly.
Proc Natl Acad Sci U S A. 1989 Jun;86(12):4549-53
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Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides.
J Biol Chem. 1989 Jul 5;264(19):11336-45
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The regulation of size and form in the assembly of collagen fibrils in vivo.
Biopolymers. 1989 Aug;28(8):1367-82
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A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos syndrome type VII.
EMBO J. 1989 Jun;8(6):1705-10
PMID: 2767050
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Temperature-dependent expression of a collagen splicing defect in the fibroblasts of a patient with Ehlers-Danlos syndrome type VII.
J Biol Chem. 1989 Oct 5;264(28):16804-9
PMID: 2777808
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Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide.
J Mol Biol. 1989 Nov 20;210(2):337-45
PMID: 2600969
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In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII.
J Biol Chem. 1990 Apr 15;265(11):6312-7
PMID: 2318855
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Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction.
Biochem J. 1990 Jun 1;268(2):339-43
PMID: 2363677
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Structural and functional characterization of a splicing mutation in the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient.
J Biol Chem. 1990 Sep 15;265(26):16007-11
PMID: 2394758
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A mutation in the pro alpha 2(I) gene (COL1A2) for type I procollagen in Ehlers-Danlos syndrome type VII: evidence suggesting that skipping of exon 6 in RNA splicing may be a common cause of the phenotype.
Am J Hum Genet. 1991 Feb;48(2):305-17
PMID: 1990839
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Ehlers-Danlos syndrome type VII: a single base change that causes exon skipping in the type I collagen alpha 2(I) chain.
Hum Genet. 1991 Jun;87(2):193-8
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Characterization of a COL1A1 splicing defect in a case of Ehlers-Danlos syndrome type VII: further evidence of molecular homogeneity.
Am J Hum Genet. 1991 Aug;49(2):400-6
PMID: 1867198
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A base substitution at the splice acceptor site of intron 5 of the COL1A2 gene activates a cryptic splice site within exon 6 and generates abnormal type I procollagen in a patient with Ehlers-Danlos syndrome type VII.
J Biol Chem. 1992 Mar 25;267(9):6361-9
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Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section.
J Biol Chem. 1992 May 5;267(13):9093-100
PMID: 1577745
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Human dermatosparaxis: a form of Ehlers-Danlos syndrome that results from failure to remove the amino-terminal propeptide of type I procollagen.
Am J Hum Genet. 1992 Aug;51(2):235-44
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Growing tips of type I collagen fibrils formed in vitro are near-paraboloidal in shape, implying a reciprocal relationship between accretion and diameter.
Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9855-9
PMID: 1409712
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Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule.
J Biol Chem. 1992 Dec 15;267(35):25521-8
PMID: 1460046
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A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase.
J Biol Chem. 1992 Dec 15;267(35):25529-34
PMID: 1460047
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Collagen made of extended -chains, procollagen, in genetically-defective dermatosparaxic calves.
Eur J Biochem. 1971 Dec 10;23(3):533-43
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Defect in conversion of procollagen to collagen in a form of Ehlers-Danlos syndrome.
Science. 1973 Oct 19;182(4109):298-300
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A hereditary dysplasia of collagen tissues in sheep.
J Pathol. 1974 Mar;112(3):183-8
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The biosynthesis of collagen and its disorders (first of two parts).
N Engl J Med. 1979 Jul 5;301(1):13-23
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Dermatosparaxis in a Himalayan cat: II. Ultrastructural studies of dermal collagen.
J Invest Dermatol. 1980 Feb;74(2):100-4
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Dermatosparaxis in a Himalayan cat: I. Biochemical studies of dermal collagen.
J Invest Dermatol. 1980 Feb;74(2):96-9
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Collagen fibril formation during embryogenesis.
Proc Natl Acad Sci U S A. 1983 Jun;80(11):3354-8
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A heterozygous collagen defect in a variant of the Ehlers-Danlos syndrome type VII. Evidence for a deleted amino-telopeptide domain in the pro-alpha 2(I) chain.
J Biol Chem. 1985 Sep 15;260(20):11322-9
PMID: 2993307
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Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization.
J Biol Chem. 1985 Dec 15;260(29):15996-6003
PMID: 3905801
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Collagen fibrillogenesis in human skin.
Ann N Y Acad Sci. 1985;460:246-57
PMID: 3914229
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Surface-induced aggregation of type I procollagen.
J Mol Biol. 1987 Jun 5;195(3):543-53
PMID: 3656425
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Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process.
J Biol Chem. 1987 Nov 15;262(32):15696-701
PMID: 3316206
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Identification of a mutation that causes exon skipping during collagen pre-mRNA splicing in an Ehlers-Danlos syndrome variant.
J Biol Chem. 1988 Jun 25;263(18):8561-4
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