Zobrazeno 1 - 7
of 7
pro vyhledávání: '"U M, Wallon"'
Publikováno v:
Journal of Biological Chemistry. 270:11555-11566
72-kDa gelatinase/type IV collagenase is an important matrix metalloproteinase in the degradation of basement membranes and denatured collagens (gelatin). These proteolytic processes are required for pathologic tissue destruction and physiologic tiss
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1ef916c1218743dd669fe8a91798e88
https://doi.org/10.1074/jbc.270.19.11555
https://doi.org/10.1074/jbc.270.19.11555
Autor:
C M, Overall, E, Tam, G A, McQuibban, C, Morrison, U M, Wallon, H F, Bigg, A E, King, C R, Roberts
Publikováno v:
The Journal of biological chemistry. 275(50)
On the cell surface, the 59-kDa membrane type 1-matrix metalloproteinase (MT1-MMP) activates the 72-kDa progelatinase A (MMP-2) after binding the tissue inhibitor of metalloproteinases (TIMP)-2. A 44-kDa remnant of MT1-MMP, with an N terminus at Gly(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b32e377df71d6fe1b87da59d54a24e48
https://pubmed.ncbi.nlm.nih.gov/10991943
https://pubmed.ncbi.nlm.nih.gov/10991943
Autor:
C M, Overall, A E, King, D K, Sam, A D, Ong, T T, Lau, U M, Wallon, Y A, DeClerck, J, Atherstone
Publikováno v:
The Journal of biological chemistry. 274(7)
Cell surface activation of progelatinase A occurs in a quaternary complex with the tissue inhibitor of metalloproteinases-2 (TIMP-2) and two membrane-type matrix metalloproteinases. We have mutated the unique cationic clusters found in hemopexin modu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4e26600fd19a44e2f33b34f6c5f0764d
https://pubmed.ncbi.nlm.nih.gov/9933646
https://pubmed.ncbi.nlm.nih.gov/9933646
Autor:
U M, Wallon, C M, Overall
Publikováno v:
The Journal of biological chemistry. 272(11)
The binding properties of the COOH-terminal hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2, 72-kDa gelatinase) were investigated to determine whether the C domain has binding affinity for extracellular matrix and b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f553e5f843124f9497e1d130c9c3f467
https://pubmed.ncbi.nlm.nih.gov/9054449
https://pubmed.ncbi.nlm.nih.gov/9054449
Publikováno v:
Archives of oral biology. 41(12)
Tissue remodelling is an important feature during embryogenesis. Although the matrix metalloproteinases are believed to participate in these processes, the relation between matrix metalloproteinases and tissue remodelling during craniofacial morphoge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3f4f7b7c96f245367c7b8389ad4ad9b
https://pubmed.ncbi.nlm.nih.gov/9134100
https://pubmed.ncbi.nlm.nih.gov/9134100
Publikováno v:
The Journal of biological chemistry. 270(19)
72-kDa gelatinase/type IV collagenase is an important matrix metalloproteinase in the degradation of basement membranes and denatured collagens (gelatin). These proteolytic processes are required for pathologic tissue destruction and physiologic tiss
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9cee9340e42be98973a60766885bf0f2
https://pubmed.ncbi.nlm.nih.gov/7744795
https://pubmed.ncbi.nlm.nih.gov/7744795
Publikováno v:
Molecular and cellular biochemistry. 146(1)
When Ehrlich ascites tumor cells were stimulated to grow, their ornithine decarboxylase (ODC) activity increased 20- to 30-fold. The increase in ODC mRNA content was one order of magnitude less during the corresponding period. Likewise, the subsequen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdb70f0ceee33303a5442ca0852d4b99
https://pubmed.ncbi.nlm.nih.gov/7651375
https://pubmed.ncbi.nlm.nih.gov/7651375