about
Tyrosine-rich acidic matrix protein (TRAMP) is a tyrosine-sulphated and widely distributed protein of the extracellular matrixProcollagen C-proteinase enhancer-1 (PCPE-1) interacts with beta2-microglobulin (beta2-m) and may help initiate beta2-m amyloid fibril formation in connective tissues.Building collagen molecules, fibrils, and suprafibrillar structures.Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein.The collagen superfamily--diverse structures and assemblies.Development of ex vivo organ culture models to mimic human corneal scarringInsights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity.Electron microscopy shows periodic structure in collagen fibril cross sectionsProduction and crystallization of the C-propeptide trimer from human procollagen III.Collagen content of alveolar wall tissue in emphysematous and non-emphysematous lungs.Proteolytic control of TGF-β co-receptor activity by BMP-1/tolloid-like proteases revealed by quantitative iTRAQ proteomics.Radial packing, order, and disorder in collagen fibrils.Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1.Folding and activity of recombinant human procollagen C-proteinase enhancer.Developmental changes in the type I procollagen processing pathway in chick-embryo cornea.Enzymatic cleavage specificity of the proalpha1(V) chain processing analysed by site-directed mutagenesis.Chick corneal development in vitro: diverse effects of pH on collagen assembly.Development of a hemicornea from human primary cell cultures for pharmacotoxicology testing.The proteolytic processing site of the precursor of lysyl oxidase.Use of magnetically oriented orthogonal collagen scaffolds for hemi-corneal reconstruction and regeneration.An ultrafiltration assay for lysyl oxidase.Changes in proteoglycan content of articular cartilage during avian degenerative joint disease.Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation.Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1.Procollagen type I C-proteinase enhancer is a naturally occurring connective tissue glycoprotein.Neutron scattering by Collagen.Inhibition of lysyl oxidase activity can delay phenotypic modulation of chondrocytes in two-dimensional culture.Procollagen binding to sphingomyelin.The crystal structure of the Bacillus anthracis spore surface protein BclA shows remarkable similarity to mammalian proteins.Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases.Structural requirements for fibromodulin binding to collagen and the control of type I collagen fibrillogenesis--critical roles for disulphide bonding and the C-terminal region.TRAMP (tyrosine rich acidic matrix protein), a protein that co-purifies with lysyl oxidase from porcine skin. Identification of TRAMP as the dermatan sulphate proteoglycan-associated 22K extracellular matrix protein.Abnormal collagen assembly, though normal phenotype, in alginate bead cultures of chick embryo chondrocytes.Clinical, structural, biochemical and X-ray crystallographic correlates of pathogenicity for variants in the C-propeptide region of the COL3A1 gene.Identification of integrin alpha 2 beta 1 as cell surface receptor for the carboxyl-terminal propeptide of type I procollagenStructure of collagen in cartilage of intervertebral diskInterpretation of the meridional X-ray diffraction pattern from collagen fibres in terms of the known amino acid sequenceLetter: Ionic clustering and collagen specificityD-periodic assemblies of type I procollagenAssembly of type I collagen fibrils de novo by the specific enzymic cleavage of pC collagen. The fibrils formed at about 37 degrees C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue
P50
Q28247892-0B5A4E2C-6977-4E83-9E32-FA6332BCFFC1Q33312776-CF535C68-591E-49D7-BBF9-16DBFEC7E375Q34133305-B95D7C94-B8FC-45B3-AA29-3448DFEEF701Q34165291-CFFD5973-B3AC-4B9A-B01E-114029B96DA6Q34259147-346C2372-0A95-42D2-9AB3-BAE2616B214BQ34509341-01494FFD-9445-4B99-BC8D-4177E08F0EFBQ34620832-836BDAFB-F962-4DF1-AD9C-5AF7A8BA6FBEQ35378652-9C8596FB-003D-448C-911A-20060E4D5FFDQ36398682-D7649B25-D87B-46D9-A405-18F910335391Q36580111-2A39AA0E-978B-4E50-8F84-CDDF82C0B7BCQ38423146-AC98E58B-512C-4646-B1C1-9B4CF6BE725DQ39660137-FFFE961C-7A43-429C-A236-126D2051D9EAQ40434283-E09F63C1-D38B-440B-8E02-DC9935835E9FQ40805254-C60F8F2C-785A-42FA-BF3B-00E73C613E42Q42026637-17E60281-B06D-40FA-80DE-1B070DB76DA2Q42262963-48DC4CF3-F2C3-45BD-AE88-BE931CF682ABQ42502315-80A0D202-15CC-46AC-AA3D-889AA347BEF7Q42510051-064C70E0-0521-43A7-B40E-FD53F66E2690Q42824263-B26F0A0D-F343-4CCC-90CF-27F3625CD771Q42937918-BD9272D6-AEA3-4883-8F00-FB4F58E6C994Q43518209-91BF6297-73BA-4194-BD8C-AECAAAA4AE41Q43590818-AB4956A2-5F10-488B-8CD1-E0F0B5CCAB47Q43738147-9E0462B3-9D63-4FC0-893D-FC164161D817Q43783344-66BA491D-E9DF-4AFD-AF89-DD1E67CE7236Q44004994-515DE2E4-1AB9-46CB-8B25-5341E0B461C4Q45029619-A2499C77-ACC0-44BF-A1C1-998C1D1D0C77Q45253065-B9D75F5C-BE38-4C27-8D59-FF6639AAC692Q46296405-4F80150F-45E4-4DE5-825F-E8FEE8926D45Q46774429-B0355D4F-0076-4E56-9D6D-B04B5D6DF25CQ47145785-A1ED2F2A-6A13-43B8-96AF-ED769F511D0DQ47751393-69997850-0417-4E3F-A5E7-1759DBA94DF4Q50783334-CA9D9289-33A1-4305-8440-1839AE8B2C85Q52533321-B633AF6D-42E4-4EFF-AAD7-304D40C724E4Q53225417-B8BED0C1-9CE1-4255-BB57-06C2289A20F5Q58058227-5CD2BE1E-C67D-40A9-9C04-5A462334FB50Q67258304-838B7C6D-7876-40D7-AB3A-CDEB441B3641Q67571097-6B2D1859-60D9-4F73-B4B3-9E2DF2951D9EQ67796038-A1FC693C-818B-4BBC-9D72-6A51F4CB1BB8Q68718025-C849C07D-FB02-4CD8-BBDA-BBF2B03F9184Q68779676-0BA73ABB-5A88-42DA-B39B-99E83796A363
P50
description
Forscher
@de
chercheur
@fr
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
研究者
@zh
name
D J Hulmes
@ast
D J Hulmes
@es
D J Hulmes
@nl
David Hulmes
@br
David Hulmes
@co
David Hulmes
@cs
David Hulmes
@da
David Hulmes
@de
David Hulmes
@en
David Hulmes
@fr
type
label
D J Hulmes
@ast
D J Hulmes
@es
D J Hulmes
@nl
David Hulmes
@br
David Hulmes
@co
David Hulmes
@cs
David Hulmes
@da
David Hulmes
@de
David Hulmes
@en
David Hulmes
@fr
altLabel
D J Hulmes
@en
prefLabel
D J Hulmes
@ast
D J Hulmes
@es
D J Hulmes
@nl
David Hulmes
@br
David Hulmes
@co
David Hulmes
@cs
David Hulmes
@da
David Hulmes
@de
David Hulmes
@en
David Hulmes
@fr
P108
P106
P21
P31
P496
0000-0002-0651-1317