Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Mario Domenighini"'
Autor:
Maria Scarselli, Neri Niccolai, Mario Domenighini, Rino Rappuoli, Andrea Bernini, Gennaro Esposito, Gigliola Burroni, M. Teresa De Magistris
Publikováno v:
European Journal of Biochemistry. 254:313-317
A synthetic tridecapeptide, corresponding to the 30242 fragment of the S1 subunit of pertussis toxin,has been structurally characterised by using NMR spectroscopy. The molecule corresponds to a T-cellepitope of the bacterial toxin which has been exte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcef784ed715bca1b5528b3d23533220
https://doi.org/10.1046/j.1432-1327.1998.2540313.x
https://doi.org/10.1046/j.1432-1327.1998.2540313.x
Autor:
Mario Domenighini, Rino Rappuoli
Publikováno v:
Molecular Microbiology. 21:667-674
It has been previously reported that the three-dimensional structures of the NAD-binding and catalytic site of bacterial toxins with ADP-ribosylating activity are superimposable, and that the key amino acids for the enzymatic activity are conserved.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e0456df6aa131bcfd84048a4d82108
https://doi.org/10.1046/j.1365-2958.1996.321396.x
https://doi.org/10.1046/j.1365-2958.1996.321396.x
Autor:
Steve Sarfaty, Mario Domenighini, Ethan A. Merritt, Mariagrazia Pizza, Wim G. J. Hol, Rino Rappuoli
Publikováno v:
Nature Structural & Molecular Biology. 2:269-272
The structure of an inactive mutant, heat-labile enterotoxin raises the possibility of a direct functional role for an internal, water-filled cavity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::039ef3455bbb0cbc3d2af4d2af40fa44
https://doi.org/10.1038/nsb0495-269
https://doi.org/10.1038/nsb0495-269
Autor:
Valentine Giannelli, Mario Domenighini, Samuele Peppoloni, Maria Rita Fontana, Wim G. J. Hol, Claudia Magagnoli, Rino Rappuoli, Roberto Manetti, Mariagrazia Pizza, Marzia Monica Giuliani
Publikováno v:
Molecular Microbiology. 14:51-60
Summary Computer analysis of the crystallographic structure of the A subunit of Escherichia coil heat-labile toxin (LT) was used to predict residues involved in NAD binding, catalysis and toxicity. Following site-directed mutagenesis, the mutants obt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3239ef15b8d7da90f423846cbe00b05
https://doi.org/10.1111/j.1365-2958.1994.tb01266.x
https://doi.org/10.1111/j.1365-2958.1994.tb01266.x
Publikováno v:
Molecular Microbiology. 14:41-50
Computer analysis of the three-dimensional structure of ADP-ribosylating toxins showed that in all toxins the NAD-binding site is located in a cavity. This cavity consists of 18 contiguous amino acids that form an alpha-helix bent over a beta-strand.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df71e4d39bbb5ab3ef6f2be537119598
https://doi.org/10.1111/j.1365-2958.1994.tb01265.x
https://doi.org/10.1111/j.1365-2958.1994.tb01265.x
Publikováno v:
BioEssays. 15:99-104
Many bacteria respond in a coordinate manner to environmental changes. External stimuli, sensed by receptors, are transduced to regulatory proteins which participate in well defined pathways of gene expression by varying their structure and mode of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::992d0bfae07a890fec799d005047acfe
https://doi.org/10.1002/bies.950150205
https://doi.org/10.1002/bies.950150205
Publikováno v:
Infection and Immunity. 59:3313-3315
Filamentous hemagglutinin (FHA), a 220-kDa protein that mediates the adhesion of Bordetella pertussis to eukaryotic cells, is a component of acellular vaccines against whooping cough. To identify the subregions of FHA that are immunogenic for T cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71f363879ad7f245d424438a40ea4851
https://doi.org/10.1128/iai.59.9.3313-3315.1991
https://doi.org/10.1128/iai.59.9.3313-3315.1991
Publikováno v:
Molecular microbiology. 15(6)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b176d0d0b1b0b18d13d05fd27714a94f
https://pubmed.ncbi.nlm.nih.gov/7623669
https://pubmed.ncbi.nlm.nih.gov/7623669
Autor:
Lawrence Steinman, A Di Tommaso, S Censini, Jorge R. Oksenberg, A Tagliabue, A K Judd, Mario Domenighini, M T De Magistris, Rino Rappuoli, D O'Sullivan
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 89(7)
The interaction of the immunodominant pertussis toxin peptide containing residues 30-42 (p30-42) with soluble DR1 molecules and the T-cell receptor (TCR) of 12 DR1-restricted human T-cell clones has been analyzed. Peptide analogues of p30-42 containi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::233256ee3de2e9cf43f0dd28e49dc029
https://pubmed.ncbi.nlm.nih.gov/1313575
https://pubmed.ncbi.nlm.nih.gov/1313575
Autor:
R. Rappuoli, Anna Prugnola, C. Capiau, Mario Domenighini, David A. Relman, Vincenzo Scarlato, Stanley Falkow
Publikováno v:
Scopus-Elsevier
The nucleotide sequence of the structural gene for filamentous haemagglutinin (FHA), fhaB, a crucial adherence factor for Bordetella perfussis, has been determined. Its 10774 nucleotides are far more than necessary to encode the 220kD biologically ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66d50b43214fbbbad88554a06f1a992e
http://hdl.handle.net/11585/882566
http://hdl.handle.net/11585/882566
