Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Rebecca Del Conte"'
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18329 (2011)
A structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-x(L), which defines the protein-protein interaction surface, was obtained from solution NMR chemical shift perturbation data. The atomic level inform
Externí odkaz:
https://doaj.org/article/5f40a10d621b40948b7099ffda8eb3f6
Autor:
Harald Schwalbe, Peter Schmieder, Marco Fragai, Nils Trieloff, Rebecca Del Conte, Hartmut Oschkinat, Edgar Specker, Lucia Banci, Kamal Azzaoui, Vladimir V. Ivanov, Till Kuehn, Sridhar Sreeramulu, Christian Richter, Marcel J. J. Blommers, Marc Nazaré
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular Nmr
Journal of Biomolecular Nmr
Fragment-based screening has evolved as a remarkable approach within the drug discovery process both in the industry and academia. Fragment screening has become a more structure-based approach to inhibitor development, but also towards development of
Autor:
Pawel, Dubiela, Rebecca, Del Conte, Francesca, Cantini, Tomasz, Borowski, Roberta, Aina, Christian, Radauer, Merima, Bublin, Karin, Hoffmann-Sommergruber, Stefano, Alessandri
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-11 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-11 (2019)
Plant non-specific lipid transfer proteins type 1 (nsLTP1) are small basic proteins with a hydrophobic cavity able to host a number of different ligands: i.e. fatty acids, fatty acyl-CoA, phospholipids, glycolipids, and hydroxylated fatty acids. Howe
Autor:
Katiuska González-Arzola, Paola Turano, Blas Moreno-Beltrán, Antonio Díaz-Quintana, Sofía García-Mauriño, Adrián Velázquez-Campoy, Irene Díaz-Moreno, Carlos Santos-Ocaña, Miguel A. De la Rosa, Rebecca Del Conte, Sofia Diaz-Moreno, Alejandra Guerra-Castellano
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
Zaguán. Repositorio Digital de la Universidad de Zaragoza
Regulation of mitochondrial activity allows cells to adapt to changing conditions and to control oxidative stress, and its dysfunction can lead to hypoxia-dependent pathologies such as ischemia and cancer. Although cytochrome c phosphorylation—in p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b0f0eced7c20a20e43d9e093b8b3989
http://zaguan.unizar.es/record/69672
http://zaguan.unizar.es/record/69672
Autor:
Blas, Moreno-Beltrán, Alejandra, Guerra-Castellano, Antonio, Díaz-Quintana, Rebecca, Del Conte, Sofía M, García-Mauriño, Sofía, Díaz-Moreno, Katiuska, González-Arzola, Carlos, Santos-Ocaña, Adrián, Velázquez-Campoy, Miguel A, De la Rosa, Paola, Turano, Irene, Díaz-Moreno
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(15)
Cell response to physiological changes and oxidative stress involves the modulation of mitochondrial metabolism. Its dysfunction favors the development of hypoxia-dependent pathologies, including ischemia and cancer. A key modulator of mitochondrial
Autor:
Pawel, Dubiela, Roberta, Aina, Dominika, Polak, Sabine, Geiselhart, Piotr, Humeniuk, Barbara, Bohle, Stefano, Alessandri, Rebecca, Del Conte, Francesca, Cantini, Tomasz, Borowski, Merima, Bublin, Karin, Hoffmann-Sommergruber
Publikováno v:
The Journal of allergy and clinical immunology. 140(6)
Autor:
Antonio Díaz-Quintana, Miguel A. De la Rosa, Rebecca Del Conte, Pedro M. Nieto, Margarida Gairí, Irene Díaz-Moreno, José M. García-Heredia
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Often, deregulation of protein activity and turnover by tyrosine nitration drives cells toward pathogenesis. Hence, understanding how the nitration of a protein affects both its function and stability is of outstanding interest. Nowadays, most of the
Autor:
Alexander Dikiy, Rebecca Del Conte, Vadim N. Gladyshev, Geun-Hee Kwak, Finn Lillelund Aachmann, Hwa-Young Kim
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:3123-3131
Methionine sulfoxide reductases are antioxidant enzymes that repair oxidatively damaged methionine residues in proteins. Mammals have three members of the methionine-R-sulfoxide reductase family, including cytosolic MsrB1, mitochondrial MsrB2 and end
Autor:
Daniela Lalli, Mariangela Agamennone, Elisa Turlizzi, Rebecca Del Conte, Lucia Cesari, Alessandro Padova, Paola Turano, Stefano Mangani
Publikováno v:
ChemMedChem. 5:428-435
S100B contributes to cell proliferation by binding the C terminus of p53 and inhibiting its tumor suppressor function. The use of multiple computational approaches to screen fragment libraries targeting the human S100B-p53 interaction site is reporte
Publikováno v:
Journal of Molecular Modeling. 13:1123-1131
S100B protein is one of the factors involved in the down-regulation of tumor suppressor protein p53, a transcription activator that signals for cycle arrest and apoptosis. As the inactivation of normal p53 functions is found in over half of human can