The human rhabdomyosarcoma cell line A204 lays down a highly insoluble matrix composed mainly of alpha 1 type-XI and alpha 2 type-V collagen chains.
about
The pro-alpha3(V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chainsTranscriptional promoter of the human alpha 1(V) collagen gene (COL5A1)The transcription factor CCAAT-binding factor CBF/NF-Y regulates the proximal promoter activity in the human alpha 1(XI) collagen gene (COL11A1)Macromolecular specificity of collagen fibrillogenesis: fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheathBiosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertasesThe human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagensStructural and functional analysis of the promoter of the human alpha 1(XI) collagen geneTargeted disruption of Col11a2 produces a mild cartilage phenotype in transgenic mice: comparison with the human disorder otospondylomegaepiphyseal dysplasia (OSMED)Regulation of collagen fibril nucleation and initial fibril assembly involves coordinate interactions with collagens V and XI in developing tendonCharacterization of type XI collagen-glycosaminoglycan interactions.Distinct maturations of N-propeptide domains in fibrillar procollagen molecules involved in the formation of heterotypic fibrils in adult sea urchin collagenous tissues.Characterization of the six zebrafish clade B fibrillar procollagen genes, with evidence for evolutionarily conserved alternative splicing within the pro-alpha1(V) C-propeptide.Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer.The transcription factor CCAAT-binding factor CBF/NF-Y and two repressors regulate the core promoter of the human pro-alpha3(V) collagen gene (COL5A3).Basic fibroblast growth factor decreases type V/XI collagen expression in cultured bovine aortic smooth muscle cells.Alternative exon splicing within the amino-terminal nontriple-helical domain of the rat pro-alpha 1(XI) collagen chain generates multiple forms of the mRNA transcript which exhibit tissue-dependent variation.The bone morphogenetic protein 1/Tolloid-like metalloproteinasesα3 Chains of type V collagen regulate breast tumour growth via glypican-1.Discoidin domain receptors: a proteomic portrait.Col11a1 Regulates Bone Microarchitecture during Embryonic Development.The mRNAs for the three chains of human collagen type XI are widely distributed but not necessarily co-expressed: implications for homotrimeric, heterotrimeric and heterotypic collagen moleculesAssociation of type XI collagen genes with chronic Achilles tendinopathy in independent populations from South Africa and Australia.Developmental pattern of expression of the mouse alpha 1 (XI) collagen gene (Col11a1).Alternative mRNA Processing Occurs in the Variable Region of the Pro-1(XI) and Pro-2(XI) Collagen Chains
P2860
Q22253347-CDF8CA91-C31C-4E3B-8FE0-645D09A551BFQ24528206-9EB309CE-6F08-4D3A-B758-C13A257A2A30Q28178924-20C55D55-AB78-455A-BE91-1F2EC5698F07Q28187983-3E7D2E21-6571-4965-B122-DE7A9FAE6689Q28210727-1A6F5C38-504C-4797-A684-8B297722862CQ28289363-19DEB542-E55C-4824-98A2-69FD8478AD59Q28305033-78FFE338-0B5B-457C-840D-26DDA23EA8A2Q28510785-9325325C-AF59-4DB6-9263-868FB8045072Q28512376-C331C90E-2491-49FF-8AC5-D7A0A36065D1Q30964954-73895E87-46EE-436C-AAF8-EB002CC6E624Q31031925-9C3866AA-C0A1-4440-A849-C496AD654FE3Q33823304-CB1D1C1C-5159-49D4-83B8-F291E81459C7Q34319950-72B57FFB-EB9B-479B-8EDE-02979AB35D3CQ34341777-6FBC7B0B-0718-454D-9500-1F6C7A0854ADQ34453782-09DD6DFE-13E4-45A8-AE1D-68D0EEA6278AQ36700771-A30205A7-E045-44EB-98E0-D34FBFD356A5Q36846125-4BACF599-1D51-47A5-A37D-78CCBAC242F2Q37598516-B2143B42-6FD8-41F6-A93F-F59ABDE692EEQ38202550-F3FA7573-FDEB-4EAC-942E-38F4A8B23CFEQ40095285-B9A12926-5B20-488B-A457-0D1C0725E597Q42137627-32396A57-A4DD-4C54-B2CB-286208782406Q46846364-6D828AEB-15D3-4BA7-99C9-48EBCCDB6285Q52206179-F76E9CC9-1537-42B1-A7DA-470F49C5FCA8Q55919461-8D2BB9B3-96FB-4136-8BD5-777CE96FA0B0
P2860
The human rhabdomyosarcoma cell line A204 lays down a highly insoluble matrix composed mainly of alpha 1 type-XI and alpha 2 type-V collagen chains.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The human rhabdomyosarcoma cel ...... lpha 2 type-V collagen chains.
@en
type
label
The human rhabdomyosarcoma cel ...... lpha 2 type-V collagen chains.
@en
prefLabel
The human rhabdomyosarcoma cel ...... lpha 2 type-V collagen chains.
@en
P2093
P2860
P1433
P1476
The human rhabdomyosarcoma cel ...... lpha 2 type-V collagen chains.
@en
P2093
D J Hartmann
J P Kleman
M van der Rest
P2860
P304
P356
10.1111/J.1432-1033.1992.TB17425.X
P407
P577
1992-11-01T00:00:00Z