Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Barry M. Steiglitz"'
Publikováno v:
Journal of Biological Chemistry. 281:10786-10798
Bone morphogenetic protein 1 (BMP1) is the prototype of a subgroup of metalloproteinases with manifold roles in morphogenesis. Four mammalian subgroup members exist, including BMP1 and mammalian Tolloid-like 1 (mTLL1). Subgroup members have a conserv
Publikováno v:
Molecular and Cellular Biology. 23:4428-4438
Bone morphogenetic protein 1 (BMP-1) and mammalian Tolloid (mTLD), two proteinases encoded by Bmp1, provide procollagen C-proteinase (pCP) activity that converts procollagens I to III into the major fibrous components of mammalian extracellular matri
Autor:
Wei-Man Wang, Mitchell C. Brenner, M. Leah Allen, Barry M. Steiglitz, Ian C. Scott, Kazuhiko Takahara, Seungbok Lee, Carter C. Lebares, Daniel S. Greenspan
Publikováno v:
Journal of Biological Chemistry. 278:19549-19557
The metalloproteinase ADAMTS-2 has procollagen I N-proteinase activity capable of cleaving procollagens I and II N-propeptides in vitro, whereas mutations in the ADAMTS-2 gene in dermatosparaxis and Ehlers-Danlos syndrome VIIC show this enzyme to be
Autor:
Yasutada Imamura, William N. Pappano, Christine Unsöld, Daniel S. Greenspan, Barry M. Steiglitz
Publikováno v:
Journal of Biological Chemistry. 277:5596-5602
The low abundance fibrillar collagen type V is incorporated into and regulates the diameters of type I collagen fibrils. Bone morphogenetic protein-1 (BMP-1) is a metalloprotease that plays key roles in regulating formation of vertebrate extracellula
Publikováno v:
Developmental Dynamics. 217:449-456
Chordin is an antagonist of TGFβ-like bone morphogenetic proteins (BMPs) that plays roles in dorsoventral axis formation and in induction, maintenance and/or differentiation of neural tissue in early vertebrate embryogenesis. In contrast, little is
Autor:
Elizabeth P. Frankenburg, Guy G. Hoffman, Steven A. Goldstein, Magnus Höök, Jeffrey A. Meganck, Daniel S. Greenspan, Jaclynn M. Kreider, Xiaowen Liang, Barry M. Steiglitz, David E. Birk, William N. Pappano
Procollagen C proteinases (pCPs) cleave type I to III procollagen C propeptides as a necessary step in assembling the major fibrous components of vertebrate extracellular matrix. The protein PCOLCE1 (procollagen C proteinase enhancer 1) is not a prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8444477a69a9acc9585a2ab60113569d
https://europepmc.org/articles/PMC1317636/
https://europepmc.org/articles/PMC1317636/
Publikováno v:
The Journal of biological chemistry. 279(2)
Bone morphogenetic protein-1 (BMP-1)/Tolloid-like metalloproteinases play key roles in formation of mammalian extracellular matrix (ECM), through the biosynthetic conversion of precursor proteins into their mature functional forms. These proteinases
Autor:
Wei-Man, Wang, Seungbok, Lee, Barry M, Steiglitz, Ian C, Scott, Carter C, Lebares, M Leah, Allen, Mitchell C, Brenner, Kazuhiko, Takahara, Daniel S, Greenspan
Publikováno v:
The Journal of biological chemistry. 278(21)
The metalloproteinase ADAMTS-2 has procollagen I N-proteinase activity capable of cleaving procollagens I and II N-propeptides in vitro, whereas mutations in the ADAMTS-2 gene in dermatosparaxis and Ehlers-Danlos syndrome VIIC show this enzyme to be
Autor:
Christine Ebel, Denise Eichenberger, Gilbert Deléage, Sylvie Ricard-Blum, Maxim V. Petoukhov, Christophe Geourjon, Dmitri I. Svergun, Barry M. Steiglitz, Simonetta Bernocco, Florence Ruggiero, David J.S. Hulmes, Daniel S. Greenspan, Bernard Font
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (9), pp.7199-205. ⟨10.1074/jbc.M210857200⟩
Journal of Biological Chemistry, 2003, 278 (9), pp.7199-205. ⟨10.1074/jbc.M210857200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (9), pp.7199-205. ⟨10.1074/jbc.M210857200⟩
Journal of Biological Chemistry, 2003, 278 (9), pp.7199-205. ⟨10.1074/jbc.M210857200⟩
International audience; Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold.
Publikováno v:
The Journal of biological chemistry. 277(51)
The procollagen COOH-terminal proteinase enhancer (PCPE) is a glycoprotein that binds the COOH-terminal propeptide of type I procollagen and potentiates its cleavage by procollagen C-proteinases, such as bone morphogenetic protein-1 (BMP-1). Recently