Výsledky vyhledávání

Procollagen C-proteinase enhancer-1 (PCPE-1) interacts with beta2-microglobulin (beta2-m) and may help initiate beta2-m amyloid fibril formation in connective tissues

Autor: Morimoto, H., Wada, J., Font, B., Mott, Jd, Hulmes, Dj, Ookoshi, T., Naiki, H., Yasuhara, A., Nakatsuka, A., Fukuoka, K., Takatori, Y., Ichikawa, H., Akagi, S., Nakao, K., Makino, H.

Dialysis related amyloidosis (DRA) is a progressive and serious complication in patients under long-term hemodialysis and mainly leads to osteo-articular diseases. Although beta(2)-microglobulin (beta2-m) is the major structural component of beta2-m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::16c3415e5dace43fec5ea564218db127
https://hal.archives-ouvertes.fr/hal-00315165

Zobrazit plný text záznamu

Trimerization of collagen IX alpha-chains does not require the presence of the COL1 and NC1 domains

Autor: Jaalinoja, J., Ylostalo, J., Beckett, W., Hulmes, Dj, Ala-Kokko, L.

Collagen IX is a heterotrimer of three alpha-chains, which consists of three COL domains (collagenous domains) (COL1-COL3) and four NC domains (non-collagenous domains) (NC1-NC4), numbered from the C-terminus. Although collagen IX chains have been sh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::d6f1d0b0581f174ac126c898216b8e69
https://hal.archives-ouvertes.fr/hal-00315130

Zobrazit plný text záznamu

Insights 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

Autor: Blanc, G., Font, B., Eichenberger, D., Moreau, C., Ricard-Blum, S., Hulmes, Dj, Moali, C.

Procollagen C-proteinase enhancers (PCPE-1 and -2) are extracellular glycoproteins that can stimulate the C-terminal processing of fibrillar procollagens by tolloid proteinases such as bone morphogenetic protein-1. They consist of two CUB domains (CU

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::9df284a39168b70efa17d47a68b7932f
https://hal.archives-ouvertes.fr/hal-00315112

Zobrazit plný text záznamu

Intra-articular hyaluronate in experimental rabbit osteoarthritis can prevent changes in cartilage proteoglycan content

Autor: Hulmes, Dj, Marsden, Me, Strachan, Rk, Harvey, Re, Mcinnes, N., Gardner, Dl

OBJECTIVE: The purpose of this study was to determine the effects of intra-articular injections of high molecular weight (2000 kDa) sodium hyaluronate (HA) on the progression of articular cartilage degeneration in a rabbit partial medial meniscectomy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::9b1f376c0a95832faa813bcada327873
https://hal.archives-ouvertes.fr/hal-00313820

Zobrazit plný text záznamu

Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily

Autor: Mcalinden, A., Smith, Ta, Sandell, Lj, Ficheux, D., Parry, Da, Hulmes, Dj

Alpha-helical coiled-coils are widely occurring protein oligomerization motifs. Here we show that most members of the collagen superfamily contain short, repeating heptad sequences typical of coiled coils. Such sequences are found at the N-terminal e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::2f002ceecad4947036d1e4fc984a1024
https://hal.archives-ouvertes.fr/hal-00313821

Zobrazit plný text záznamu

Folding and activity of recombinant human procollagen C-proteinase enhancer

Autor: Moschcovich, L., Bernocco, S., Font, B., Rivkin, H., Eichenberger, D., Chejanovsky, N., Hulmes, Dj, Kessler, E.

Recombinant human procollagen C-proteinase enhancer (rPCPE) was expressed using a baculovirus system and purified to homogeneity using a three-step procedure including heparin affinity chromatography. Heparin binding was dependent on the C-terminal n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::952ab385403002f596648bf9aa497d34
https://hal.archives-ouvertes.fr/hal-00313826

Zobrazit plný text záznamu

Changes in proteoglycan content of articular cartilage during avian degenerative joint disease

Autor: Anderson-Mackenzie, Jm, Robins, Sp, Thorp, Bh, Hulmes, Dj

OBJECTIVE: To determine the biochemical changes in articular cartilage composition associated with the development of avian degenerative joint disease (DJD) in ad libitum fed broiler fowl, in comparison to feed-restricted broilers and J-lin fowl (non

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::6a6fe482df3120060d430eae01e35365
https://hal.archives-ouvertes.fr/hal-00313827

Zobrazit plný text záznamu

Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1

Autor: Borel, A., Eichenberger, D., Farjanel, J., Kessler, E., Gleyzal, C., Hulmes, Dj, Sommer, P., Font, B.

Recently several cDNAs have been described encoding lysyl oxidase-like proteins. Their deduced amino acid sequences are characterized by a strong similarity in the C-terminal region, corresponding to the lysyl oxidase family catalytic domain, and by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::44e858b05fbbe68e2c94a0562dd40363
https://hal.archives-ouvertes.fr/hal-00313824

Zobrazit plný text záznamu

Liquid crystalline ordering of procollagen as a determinant of three-dimensional extracellular matrix architecture

Autor: Martin, Roland, Farjanel, J., Eichenberger, D., Colige, A., Kessler, E., Hulmes, Dj, Giraud-Guille, Marie-Madeleine

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2000, 301, pp.11-17

International audience; The precise molecular mechanisms that determine the three-dimensional architectures of tissues remain largely unknown. Within tissues rich in extracellular matrix, collagen fibrils are frequently arranged in a tissue-specific

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::663559c643b49a1a0486693bded33173
https://hal.archives-ouvertes.fr/hal-00313828

Zobrazit plný text záznamu

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

Autor: Font, B., Eichenberger, D., Goldschmidt, D., Boutillon, Mm, Hulmes, Dj

Fibromodulin belongs to the family of small, leucine-rich proteoglycans which have been reported to interact with collagens and to inhibit type I collagen fibrillogenesis. Decorin and fibromodulin exhibit a noticeable degree of sequence similarity. H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______166::53c33a6ac29b00a52834008a15944675
https://hal.archives-ouvertes.fr/hal-00313833

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání