Zobrazeno 1 - 10
of 22
pro vyhledávání: '"C. Beghdadi-Rais"'
Autor:
C. Beghdadi-Rais, Chantal Desponds, E Vargas, Nicolas Fasel, Christophe Reymond, M. X. P. van Bemmelen, Sócrates Herrera
Publikováno v:
Molecular and Biochemical Parasitology. 111:377-390
Nearly full-length Circumsporozoite protein (CSP) from Plasmodium falciparum, the C-terminal fragments from both P. falciparm and P. yoelii CSP and a fragment comprising 351 amino acids of P.vivax MSPI were expressed in the slime mold Dictyostelium d
Publikováno v:
Cell Biology International Reports. 15:1051-1064
Many cell surface glycoproteins are anchored in the lipid bilayer by a glycosylphosphatidyl-inositol (GPI) structure. Recently, a number of cell lines which are deficient in the biosynthesis and/or addition of this anchor have been described. In this
Autor:
Christophe Reymond, Giampietro Corradin, Dorinne Groux, Chantal Desponds, Michel Bernard, Claude Bron, Elizabeth A. Duarte, Mario Roggero, C. Beghdadi-Rais, Hugues Matile, Nicolas Fasel
Publikováno v:
The Journal of biological chemistry. 270(21)
The circumsporozoite protein (CSP), a major antigen of Plasmodium falciparum, was expressed in the slime mold Dictyostelium discoideum. Fusion of the parasite protein to a leader peptide derived from Dictyostelium contact site A was essential for exp
Autor:
U, Blum-Tirouvanziam, C, Beghdadi-Rais, M A, Roggero, D, Valmori, S, Bertholet, C, Bron, N, Fasel, G, Corradin
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 153(9)
We have studied the immunogenicity of Plasmodium falciparum circumsporozoite (CS) protein-derived synthetic polypeptides in mice. These synthetic peptides correspond to the N- and the C-terminal domains 22-125 and 289-390, respectively of the P. falc
Publikováno v:
Molecular immunology. 31(7)
Publikováno v:
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas. 27(2)
We designed a trap system to isolate different amino acid sequences which could target proteins to the cell surface via GPI anchor transfer. This selection procedure is based on the insertion of various sequences which regenerate a functional GPI anc
Autor:
R.J. Eisenberg, M. Schreyer, P. Borel, C. Beghdadi-Rais, Marga Rousseaux, Claude Bron, G.H. Cohen, Nicolas Fasel
Publikováno v:
Journal of cell science. 105
Glycosyl phosphatidylinositol (GPI)-anchored proteins contain in their COOH-terminal region a peptide segment that is thought to direct glycolipid addition. This signal has been shown to require a pair of small amino acids positioned 10–12 residues
Many cell surface glycoproteins are anchored in the lipid bilayer by a glycosylphosphatidyl-inositol (GPI) structure. Recently, a number of cell lines which are deficient in the biosynthesis and/or addition of this anchor have been described. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56f7e817201c240b41837431064c98d6
https://doi.org/10.1016/b978-0-12-159390-2.50018-0
https://doi.org/10.1016/b978-0-12-159390-2.50018-0
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