Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Angela Bisso"'
Autor:
Antonio De Flora, Michela Tonetti, Camillo Rosano, Gaetano Izzo, Martino Bolognesi, Angela Bisso, Laura Sturla
Publikováno v:
Journal of Molecular Biology. 303:77-91
GDP-4-keto-6-deoxy- d -mannose epimerase/reductase is a bifunctional enzyme responsible for the last step in the biosynthesis of GDP- l -fucose, the substrate of fucosyl transferases. Several cell-surface antigens, including the leukocyte Lewis syste
Publikováno v:
FEBS Letters. 456:370-374
GDP-D-mannose-4,6-dehydratase (GMD) is the key enzyme in the ‘de novo’ pathway of GDP-L-fucose biosynthesis. The reported cDNA sequences for human GMD predict three forms of different length, whose ‘in vivo’ occurrence and molecular propertie
Autor:
Angela Bisso, Antonio De Flora, Laura Sturla, Davide Zanardi, Michela Tonetti, Umberto Benatti
Publikováno v:
Biochimie. 80:923-931
L-fucose and L-rhamnose are two 6-deoxyhexoses naturally occurring in several complex carbohydrates. In prokaryotes both of them are found in polysaccharides of the cell wall, while in animals only L-fucose has been described, which mainly participat
Publikováno v:
Biochemical and Biophysical Research Communications. 230:636-640
Co-cultures of the murine macrophagic cell line RAW 264.7 with the L929 fibrosarcoma cell line, but not with the leukemia L1210 cell line, showed enhanced NO production over control RAW 264.7 cells. This potentiating effect, which was observed in det
Autor:
Santina Bruzzone, Angela Bisso, Luisa Franco, Elena Zocchi, Antonio De Flora, Lucrezia Guida, Cesare Usai, Paola Contini
Publikováno v:
Scopus-Elsevier
Connexin 43 (Cx43) hexameric hemichannels, recently demonstrated to mediate NAD(+) transport, functionally interact in the plasma membrane of several cells with the ectoenzyme CD38 that converts NAD(+) to the universal calcium mobilizer cyclic ADP-ri
Autor:
Menico Rizzi, P Vigevani, Michela Tonetti, Laura Sturla, A. De Flora, Martino Bolognesi, Angela Bisso
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 54(Pt 4)
The GDP-4-keto-6-deoxy-D-mannose epimerase/reductase (GM_ER) isolated from E. coli has been overexpressed as a GST-fusion protein and purified to homogeneity. The enzyme, an NADP+(H)-binding homodimer of 70 kDa, is responsible for the production of G
Autor:
Michela Tonetti, Angela Bisso, Antonio De Flora, Giovanni De Flora, Amos Etzioni, Lorenzo Silengo, Laura Sturla, Davide Zanardi
Publikováno v:
FEBS letters. 429(3)
Leukocyte adhesion deficiency type II (LAD II) is a rare genetic disease characterized by severe immunodeficiency which is related to defective expression in leukocytes of sialyl-Lewis X (SLeX), a fucosylated ligand for endothelial selectins. The mol
Expression, Purification and Characterization of GDP-D-Mannose 4,6-Dehydratase from Escherichia Coli
Autor:
Davide Zanardi, Umberto Benatti, Michela Tonetti, Laura Sturla, Angela Bisso, Antonio De Flora
GDP-D-mannose dehydratase (GMD) catalyzes the first step of the pathway that converts GDP-D-mannose to GDP- L-fucose in bacteria, plants and mammals. Recently, the gene coding for GMD has been identified and sequenced in E. coli. Based on this sequen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad6e93ec46229338e5877009d5bc9905
http://hdl.handle.net/11567/186490
http://hdl.handle.net/11567/186490
Publikováno v:
The Journal of biological chemistry. 271(44)
FX is a homodimeric NADP(H)-binding protein of 68 kDa, first identified in human erythrocytes, from which it was purified to homogeneity. Its function has been unrecognized despite partial structural and genetic characterization. Recently, on the bas
Autor:
Martino Bolognesi, Antonio De Flora, Laura Sturla, Domenico Bordo, Menico Rizzi, Michela Tonetti, Pierpaolo Vigevani, Angela Bisso
Publikováno v:
Scopus-Elsevier
Background: The process of guanosine 5′-diphosphate L-fucose (GDP-L-fucose) biosynthesis is conserved throughout evolution from prokaryotes to man. In animals, GDP-L-fucose is the substrate of fucosyltransferases that participate in the biosynthesi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0741cb6653d609885341fed72db6e43c
http://www.scopus.com/inward/record.url?eid=2-s2.0-0032534052&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0032534052&partnerID=MN8TOARS