Zobrazeno 1 - 10
of 44
pro vyhledávání: '"François Pochon"'
Publikováno v:
Journal of Biological Chemistry. 271:25762-25769
The refined three-dimensional structure of native human alpha2-macroglobulin (alpha2M) has been determined by cryoelectron microscopy and three-dimensional reconstruction. New features corresponding to "sigmoid arches," "basal bodies," and "apical co
Publikováno v:
Annals of the New York Academy of Sciences. 737:202-211
Publikováno v:
Journal of Structural Biology. 112:148-159
The plasma proteinase inhibitor alpha 2-macroglobulin (alpha 2M) can trap small proteins including cytokines. With the four internal thiol ester bonds being involved in the covalent binding of proteinases and other ligands, it was of interest to prec
Autor:
Jean N. Lamy, Pawel A. Penczek, François Pochon, Joachim Frank, Nicolas Boisset, Etienne Delain, Robert A. Grassucci
Publikováno v:
Journal of Structural Biology. 109:39-45
Cysteine 949 and glutamine 952 are known to be part of the thiol ester site of each of the four subunits of human alpha 2-macroglobulin (alpha 2M). The hydrolysis of this thiol ester bound to methylamine results in the incorporation of the amine and
Publikováno v:
Annals of the New York Academy of Sciences. 737
Publikováno v:
Journal of structural biology. 113(1)
The architecture of the native human α 2 -macroglobulin was studied by cryoelectron microscopy and image processing techniques. The lip, padlock, doughnut , and four-petaled flower views of this homotetrameric proteinase inhibitor were observed in t
Publikováno v:
Journal of molecular biology. 232(2)
A frozen-hydrated sample embedded in vitreous ice of human α2-macroglobulin transformed by methylamine was imaged by cryoelectron microscopy and reconstructed in three dimensions. In the reconstruction, the cage-like architecture of this protease in
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 1992, 108 ((3)), pp.221-6
Journal of Structural Biology, 1992, 108 ((3)), pp.221-6
Journal of Structural Biology, Elsevier, 1992, 108 ((3)), pp.221-6
Journal of Structural Biology, 1992, 108 ((3)), pp.221-6
International audience; In order to covalently bind the hydrolyzed thiol ester groups of the human alpha 2-macroglobulin (alpha 2M) transformed by methylamine, the phospholipase A2 (PLA2), a small enzyme (M(r) = 13,000) from Naja nigricollis snake ve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86b1d39405a7203b257ac0f2f2cf75ef
https://hal.archives-ouvertes.fr/hal-00815242
https://hal.archives-ouvertes.fr/hal-00815242
Publikováno v:
Electron microscopy reviews. 5(2)
New results concerning the ultrastructure of human alpha 2-macroglobulin (alpha 2M) molecules are presented in connection and comparison with the historical, the current and our own most recent, even unpublished results on the structure and function
Autor:
Martine Barray, François Pochon, Jean-Christophe Taveau, Etienne Delain, Nicolas Boisset, Jean Lamy
Publikováno v:
Journal of structural biology. 106(1)
Human alpha 2-macroglobulin (alpha 2M), a large tetrameric plasma glycoprotein, inhibits a wide spectrum of proteinases by a particular "trapping" mechanism resulting from the proteolysis of peptide bonds at specific "bait" regions. This induces the