Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Katy Montin"'
Autor:
Paolo Monini, Aurelio Cafaro, Indresh K Srivastava, Sonia Moretti, Victoria A Sharma, Claudia Andreini, Chiara Chiozzini, Flavia Ferrantelli, Maria R Pavone Cossut, Antonella Tripiciano, Filomena Nappi, Olimpia Longo, Stefania Bellino, Orietta Picconi, Emanuele Fanales-Belasio, Alessandra Borsetti, Elena Toschi, Ilaria Schiavoni, Ilaria Bacigalupo, Elaine Kan, Leonardo Sernicola, Maria T Maggiorella, Katy Montin, Marco Porcu, Patrizia Leone, Pasqualina Leone, Barbara Collacchi, Clelia Palladino, Barbara Ridolfi, Mario Falchi, Iole Macchia, Jeffrey B Ulmer, Stefano Buttò, Cecilia Sgadari, Mauro Magnani, Maurizio P M Federico, Fausto Titti, Lucia Banci, Franco Dallocchio, Rino Rappuoli, Fabrizio Ensoli, Susan W Barnett, Enrico Garaci, Barbara Ensoli
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e48781 (2012)
Use of Env in HIV vaccine development has been disappointing. Here we show that, in the presence of a biologically active Tat subunit vaccine, a trimeric Env protein prevents in monkeys virus spread from the portal of entry to regional lymph nodes. T
Externí odkaz:
https://doaj.org/article/860549d9bb1144a29514347f7a77ea12
Autor:
Franco Dallocchio, Carlo Cervellati, Katy Montin, I. Capone, Stefania Hanau, L. Proietti d'Empaire
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844:785-792
The catalytic mechanism of 6-phosphogluconate dehydrogenase requires the inversion of a Lys/Glu couple from its natural ionization state. The pKa of these residues in free and substrate bound enzymes has been determined measuring by ITC the proton re
Autor:
Carlo Mischiati, Carlo Ferrari, Francesco Spinozzi, Katy Montin, Vincenzo Lanzara, Carlo M. Bergamini, Carlo Cervellati, Heinz Amenitsch, Monica Squerzanti, Paolo Mariani
Publikováno v:
Amino Acids. 42:2233-2242
Tissue transglutaminase undergoes thermal inactivation with first-order kinetics at moderate temperatures, in a process which is affected in opposite way by the regulatory ligands calcium and GTP, which stabilize different conformations. We have expl
Publikováno v:
Journal of Biological Chemistry. 285:21366-21371
The reductive carboxylation of ribulose-5-phosphate (Ru5P) by 6-phosphogluconate dehydrogenase (6PGDH) from Candida utilis was investigated using kinetic isotope effects. The intrinsic isotope effect for proton abstraction from Ru5P was found at 4.9
Publikováno v:
FEBS Journal. 274:6426-6435
6-Phosphogluconate dehydrogenase is a potential target for new drugs against African trypanosomiasis. Phosphorylated aldonic acids are strong inhibitors of 6-phosphogluconate dehydrogenase, and 4-phospho-d-erythronate (4PE) and 4-phospho-d-erythronoh
Publikováno v:
Current Bioactive Compounds. 3:161-169
The reductive carboxylation of ribulose-5-phosphate (Ru5P) by 6-phosphogluconate dehydrogenase (6PGDH) from Candida utilis was investigated using kinetic isotope effects. The intrinsic isotope effect for proton abstraction from Ru5P was found at 4.9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::075af1bf64525fc2b26d48ad8ef35584
http://hdl.handle.net/11392/1399524
http://hdl.handle.net/11392/1399524
Autor:
Carlo Mischiati, Vincenzo Lanzara, Carlo M. Bergamini, Katy Montin, Carlo Cervellati, Rita Casadio, Martin Griffin, Russell Collighan, Monica Squerzanti, Alessia Dondi, Gianluca Tasco
The transamidating activity of tissue transglutaminase is regulated by the ligands calcium and GTP, via conformational changes which facilitate or interfere with interaction with the peptidyl-glutamine substrate. We have analysed binding of these lig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc36c3cc21a6873e18987f55939bf9a1
http://hdl.handle.net/11392/1391076
http://hdl.handle.net/11392/1391076
6-Phosphogluconate dehydrogenase is a potential target for new drugs against African trypanosomiasis. Phosphorylated aldonic acids are strong inhibitors of 6-phosphogluconate dehydrogenase, and 4-phospho-d-erythronate (4PE) and 4-phospho-d-erythronoh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::61902ac1b6a8d22df78b985dda626056
http://hdl.handle.net/11392/470984
http://hdl.handle.net/11392/470984