Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation.
about
Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences.Complete primary structure of rainbow trout type I collagen consisting of alpha1(I)alpha2(I)alpha3(I) heterotrimers.Relation of PvuII site polymorphism in the COL1A2 gene to the risk of fractures in prepubertal Finnish girls.Clinical variability of osteogenesis imperfecta linked to COL1A2 and associated with a structural defect in the type I collagen molecule.Determination of a new collagen type I alpha 2 gene point mutation which causes a Gly640 Cys substitution in osteogenesis imperfecta and prenatal diagnosis by DNA hybridisation.Single base mutation in the pro alpha 2(I) collagen gene that causes efficient splicing of RNA from exon 27 to exon 29 and synthesis of a shortened but in-frame pro alpha 2(I) chain.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.Type 1 neurofibromatosis: selective expression of extracellular matrix genes by Schwann cells, perineurial cells, and fibroblasts in mixed cultures.Sequencing of cDNA from 50 unrelated patients reveals that mutations in the triple-helical domain of type III procollagen are an infrequent cause of aortic aneurysms.Osteogenesis imperfecta type I is commonly due to a COL1A1 null allele of type I collagen.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.Analysis of the cellular basis of keratinocyte growth factor overexpression in inflammatory bowel disease.Expression of mRNAs for type I and type III procollagens in serous ovarian cystadenomas and cystadenocarcinomasPvuII polymorphism at the COL1A2 locusMapping the heparin-binding sites on type I collagen monomers and fibrils.Defining the domains of type I collagen involved in heparin- binding and endothelial tube formation.Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagens.Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta.Regulatory role of the conserved stem-loop structure at the 5' end of collagen alpha1(I) mRNA.Molecular cloning of type I collagen cDNA and nutritional regulation of type I collagen mRNA expression in grass carp.Clearance of NH2-terminal propeptides of types I and III procollagen is a physiological function of the scavenger receptor in liver endothelial cells.Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-aStructure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen.Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation.Expression of wild-type and modified proalpha chains of human type I procollagen in insect cells leads to the formation of stable [alpha1(I)]2alpha2(I) collagen heterotrimers and [alpha1(I)]3 homotrimers but not [alpha2(I)]3 homotrimers.Expression of genes of type I and type II collagen in the formation and development of the blastema of regenerating newt limb.Structure of cDNA clones coding for human type II procollagen. The alpha 1(II) chain is more similar to the alpha 1(I) chain than two other alpha chains of fibrillar collagens.Conformational selection and collagenolysis in type III collagen.Corticosteroids alter the differentiated phenotype of articular chondrocytes.Correlation between mRNA levels for bone cell proteins and bone formation in long bones of maturing rats.Collagen-specific cytotoxic T lymphocyte responses in patients with ankylosing spondylitis and reactive arthritis.Genomic organization of the human procollagen alpha 1(II) collagen gene.Forehead wrinkles: a histological and immunohistochemical evaluation.The occurrence of two types of collagen proalpha-chain in the abalone Haliotis discus muscle.Expression of a stable articular cartilage phenotype without evidence of hypertrophy by adult human articular chondrocytes in vitro.Bioactive molecules from the Blue Lagoon: in vitro and in vivo assessment of silica mud and microalgae extracts for their effects on skin barrier function and prevention of skin ageing.A Gly859Ser substitution in the triple helical domain of the α2 chain of type I collagen resulting in osteogenesis imperfecta type III in two unrelated individuals
P2860
Q30393151-D1C72CBA-28DC-4410-B1B0-D3861D78FDE6Q31916814-0D5370D5-10FF-4693-8641-5EABD75434A3Q33187450-3E209B9A-34FE-4AE7-9B23-50596910B494Q33593003-2109CBEB-5114-473B-A81F-5A7679E3197CQ33596338-678DAEA6-6078-460B-AE20-E8FE8D3C6195Q33633029-9B6A1A2A-4831-4BF6-A718-F8A055FD0AEFQ34263964-6550A5D7-A98C-459C-AC40-EE8CC7BCD443Q34577394-D18D3543-FB61-4D00-AE7C-B193B6251766Q34731356-1D556620-3391-4054-A5CA-0DF1A1105DFCQ35195793-85162BCE-A600-4FEC-994D-DFAFFA36FA01Q35196578-C2834671-AE91-4009-BBEA-E1C3732909F8Q35358052-D439CF54-FE7B-4FB5-9627-D1038D9DC913Q35774146-8D0A9576-57D6-4E76-91C0-34263E66595BQ35878995-7039FCA9-1671-47C0-B667-01C2D4B6D0B3Q36234227-3FE6891A-CAE9-4FB5-8EB1-A1773F8BCE41Q36483511-897176A2-58B1-460C-A9ED-752FCF99F015Q36869153-4286F476-A033-46B0-9FBE-B0D4DA575C46Q37535564-EFEA7D54-44A2-480D-87A5-F82149247005Q39551522-47522EC1-F61E-4FF6-A0A1-A5EEC5C3558CQ39619130-44AB8C71-1876-46ED-867F-59C80545EBE1Q41489449-566CDD15-4C28-4B71-8973-7EEE6B1E169CQ41771617-90A63A13-3C4A-4454-82EE-F1510CAC769DQ41880888-C501A157-36D8-4DC5-9B8E-991FF270FDB2Q41937550-AC8918AE-4CEF-4820-88E3-949A16C76F23Q42061791-C5EEC1E1-4DBE-4779-8290-7F1EB69F74D3Q42477129-44165E26-5605-4AEF-9251-3BF6A90955EFQ42802724-A97E8E5C-AF6D-4650-ACC1-C50B1B1283E7Q43280889-F104F4E2-10CB-4751-A3C4-BB0DBDCF1B69Q43716640-B71D1C7F-5814-4CBE-83C9-2DD6C06D18E3Q44418145-FC69E075-2CEE-42A0-B556-94D7E6F867C3Q44480077-53C5DCEC-D150-45B4-AD34-245C2617D3A9Q44955789-87863780-D29F-460B-97B8-5F1B5BE00DB2Q46317818-23DB7CCD-2C3F-4FB5-B3A9-EC59E475B7F4Q47970030-881BFB75-F732-4FDF-90B4-B56AEF88153BQ47988998-AD677B9C-237D-4619-9964-6C9BFD17DB89Q50460562-B16CCD8B-8F5E-41E6-855E-1B10CE2B64EEQ57197836-73EC19B2-28C6-4F9B-B30C-7F21B155FF23
P2860
Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
1988年學術文章
@zh
1988年學術文章
@zh-hant
name
Structure of a full-length cDN ...... patterns of gene conservation.
@ast
Structure of a full-length cDN ...... patterns of gene conservation.
@en
type
label
Structure of a full-length cDN ...... patterns of gene conservation.
@ast
Structure of a full-length cDN ...... patterns of gene conservation.
@en
prefLabel
Structure of a full-length cDN ...... patterns of gene conservation.
@ast
Structure of a full-length cDN ...... patterns of gene conservation.
@en
P2860
P356
P1433
P1476
Structure of a full-length cDN ...... patterns of gene conservation.
@en
P2093
P2860
P304
P356
10.1042/BJ2520633
P407
P577
1988-06-01T00:00:00Z