Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Giulia Canevari"'
Autor:
Elena Casale, Patrizia Carpinelli, Claudia Perrera, Ulisse Cucchi, Giulia Canevari, Barbara Forte, Eduard R. Felder, J.A. Bertrand, Stefania Re Depaolini
Publikováno v:
Biochemistry. 52:6380-6387
Maternal embryonic leucine zipper kinase (MELK) is upregulated in several types of tumor, including breast, prostate, and brain tumors. Its expression is generally associated with cell survival, cell proliferation, and resistance to apoptosis. Theref
Autor:
F. Ciriello, S. Baroni, Giulia Canevari, Martino Bolognesi, Alessandro Aliverti, V. Pandini, Mario Milani
Publikováno v:
Journal of Molecular Biology 411 (2011): 463–473. doi:10.1016/j.jmb.2011.06.010
info:cnr-pdr/source/autori:Milani, Mario; Ciriello, Francesco; Baroni, Sara; Pandini, Vittorio; Canevari, Giulia; Bolognesi, Martino; Aliverti, Alessandro/titolo:FAD-Binding Site and NADP Reactivity in Human Renalase: A New Enzyme Involved in Blood Pressure Regulation/doi:10.1016%2Fj.jmb.2011.06.010/rivista:Journal of Molecular Biology/anno:2011/pagina_da:463/pagina_a:473/intervallo_pagine:463–473/volume:411
info:cnr-pdr/source/autori:Milani, Mario; Ciriello, Francesco; Baroni, Sara; Pandini, Vittorio; Canevari, Giulia; Bolognesi, Martino; Aliverti, Alessandro/titolo:FAD-Binding Site and NADP Reactivity in Human Renalase: A New Enzyme Involved in Blood Pressure Regulation/doi:10.1016%2Fj.jmb.2011.06.010/rivista:Journal of Molecular Biology/anno:2011/pagina_da:463/pagina_a:473/intervallo_pagine:463–473/volume:411
Renalase is a recently discovered flavoprotein that regulates blood pressure, regulates sodium and phosphate excretion, and displays cardioprotectant action through a mechanism that is barely understood to date. It has been proposed to act as a catec
Autor:
Domenico Delia, Eloise Mastrangelo, Carlo Scolastico, Martino Bolognesi, Francesca Malvezzi, Mario Milani, Giulia Canevari, Daniele Lecis, Pierfausto Seneci, Federica Cossu
Publikováno v:
Protein Science. 19:2418-2429
Inhibitor of apoptosis proteins (IAPs) are negative regulators of apoptosis. As IAPs are overexpressed in many tumors, where they confer chemoresistance, small molecules inactivating IAPs have been proposed as anticancer agents. Accordingly, a number
Autor:
V. Pandini, Giuliana Zanetti, Martino Bolognesi, Alessandro Aliverti, D. Crobu, Giulia Canevari, Maria A. Vanoni, Mario Milani
Publikováno v:
Biochemistry (Wash. D.C., Online) 48 (2009): 9525–9533. doi:10.1021/bi9013209
info:cnr-pdr/source/autori:Crobu D; Canevari G; Milani M; Pandini V; Vanoni MA; Bolognesi M; Zanetti G; Aliverti A./titolo:Plasmodium falciparum Ferredoxin-NADP(+) Reductase His286 Plays a Dual Role in NADP(H) Binding and Catalysis/doi:10.1021%2Fbi9013209/rivista:Biochemistry (Wash. D.C., Online)/anno:2009/pagina_da:9525/pagina_a:9533/intervallo_pagine:9525–9533/volume:48
info:cnr-pdr/source/autori:Crobu D; Canevari G; Milani M; Pandini V; Vanoni MA; Bolognesi M; Zanetti G; Aliverti A./titolo:Plasmodium falciparum Ferredoxin-NADP(+) Reductase His286 Plays a Dual Role in NADP(H) Binding and Catalysis/doi:10.1021%2Fbi9013209/rivista:Biochemistry (Wash. D.C., Online)/anno:2009/pagina_da:9525/pagina_a:9533/intervallo_pagine:9525–9533/volume:48
The NADP-binding site of Plasmodium falciparum ferredoxin-NADP(+) reductase contains two basic residues, His286 and Lys249, conserved within the Plasmodium genus, but not in other plant-type homologues. Previous crystal studies indicated that His286
Autor:
Giulia Canevari, Elena Casale, Nilla Avanzi, Elena Ardini, Arturo Galvani, Nadia Amboldi, Antonella Ermoli, Daniele Donati, Dario Ballinari, Sonia Troiani, Cinzia Cristiani, Alessandra Cirla, Paolo Polucci, Federico Riccardi Sirtori, Marina Ciomei, Eduard R. Felder, Patrizia Banfi, Antonella Isacchi, Ilaria Motto, Maria Menichincheri, Francesco Caprera
Publikováno v:
Cancer Research. 77:2082-2082
RET, a receptor tyrosine kinase (RTK) expressed mainly in neural crest-derived tissues, plays a role in cell growth and differentiation and its physiological activation depends upon binding to the GDNF family. Genetic aberrations leading to constitut
Autor:
Sabrina Cribioli, Giulia Canevari, Antonella Isacchi, Maria Gabriella Brasca, Daniele Donati, Riccardo Colombo, Marina Ciomei, Eduard R. Felder, Alessia Montagnoli, Marisa Montemartini, Arturo Galvani, Nadia Amboldi, Helena Posteri, Dario Ballinari, Patrizia Carpinelli, Walter Ceccarelli, Nilla Avanzi, Stefania Re Depaolini
Publikováno v:
Cancer Research. 76:3795-3795
Maternal Embryonic Leucine zipper Kinase (MELK) is a serine-threonine kinase implicated in stem cell renewal, override of cell cycle checkpoints, pre-mRNA splicing and resistance to apoptosis, while MELK gene expression levels correlate inversely wit
Autor:
Wilma Pastori, Simona Bindi, Daniele Casero, Marina Ciomei, Sabrina Cribioli, Nadia Amboldi, Cinzia Pellizzoni, Paola Gnocchi, Nilla Avanzi, Daniele Donati, Elena Ardini, Giulia Canevari, Gemma Texido, Arturo Galvani, Marcella Nesi, Maria Gabriella Brasca, Eduard R. Felder, Antonella Isacchi, Cinzia Cristiani, Roberta Ceruti, Veronica Patton
Publikováno v:
Molecular Cancer Therapeutics. 14:A179-A179
The Janus Kinases (JAK1, JAK2, JAK3, TYK2) are non-receptor tyrosine kinases that play important roles in hematopoiesis and immune response. In particular, gene ablation of JAK1 or JAK2 in the mouse is incompatible with life, due to neurological defe
Autor:
Martino Bolognesi, Carmelo Drago, Carlo Scolastico, Mario Milani, Giulia Canevari, Federica Servida, Daniele Lecis, Patrice Vachette, Federica Cossu, Pierfausto Seneci, Domenico Delia, Eloise Mastrangelo, Vincenzo Rizzo, Leonardo Manzoni
Publikováno v:
Journal of Molecular Biology 392 (2009): 630–644. doi:10.1016/j.jmb.2009.04.033
info:cnr-pdr/source/autori:Cossu, Federica; Milani, Mario; Mastrangelo, Eloise; Vachette, Patrice; Servida, Federica; Lecis, Daniele; Canevari, Giulia; Delia, Domenico; Drago, Carmelo; Rizzo, Vincenzo; Manzoni, Leonardo; Seneci, Pierfausto; Scolastico, Carlo; Bolognesi, M/titolo:Structural Basis for Bivalent Smac-Mimetics Recognition in the IAP Protein Family/doi:10.1016%2Fj.jmb.2009.04.033/rivista:Journal of Molecular Biology/anno:2009/pagina_da:630/pagina_a:644/intervallo_pagine:630–644/volume:392
info:cnr-pdr/source/autori:Cossu, Federica; Milani, Mario; Mastrangelo, Eloise; Vachette, Patrice; Servida, Federica; Lecis, Daniele; Canevari, Giulia; Delia, Domenico; Drago, Carmelo; Rizzo, Vincenzo; Manzoni, Leonardo; Seneci, Pierfausto; Scolastico, Carlo; Bolognesi, M/titolo:Structural Basis for Bivalent Smac-Mimetics Recognition in the IAP Protein Family/doi:10.1016%2Fj.jmb.2009.04.033/rivista:Journal of Molecular Biology/anno:2009/pagina_da:630/pagina_a:644/intervallo_pagine:630–644/volume:392
XIAP is an apoptotic regulator protein that binds to the effector caspases -3 and -7 through its BIR2 domain, and to initiator caspase-9 through its BIR3 domain. Molecular docking studies suggested that Smac-DIABLO may antagonize XIAP by concurrently
We have studied the normal modes of hydrogenated and oxidized silicon nanocrystals, namely SiH4 (silan), H2SiO (silanon), Si10H16 and Si10H14O. The small clusters (SiH4 and H2SiO) have been used for convergence tests and their bondlengths and frequen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33856536ba247fdccb0393ad4b4abe82