Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Francesco P Nicoletti"'
Autor:
Alessio Bocedi, Giampiero De Sanctis, Chiara Ciaccio, Grazia R Tundo, Alessandra Di Masi, Gabriella Fanali, Francesco P Nicoletti, Mauro Fasano, Giulietta Smulevich, Paolo Ascenzi, Massimo Coletta
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e58842 (2013)
Human serum albumin (HSA), the most abundant protein in human plasma, could be considered as a prototypic monomeric allosteric protein, since the ligand-dependent conformational adaptability of HSA spreads beyond the immediate proximity of the bindin
Externí odkaz:
https://doaj.org/article/c480cc9f4a5845c685ed0f6f59ccff39
Autor:
Daniela Giordano, Ignacio Boron, Stefania Abbruzzetti, Wendy Van Leuven, Francesco P Nicoletti, Flavio Forti, Stefano Bruno, C-H Christina Cheng, Luc Moens, Guido di Prisco, Alejandro D Nadra, Darío Estrin, Giulietta Smulevich, Sylvia Dewilde, Cristiano Viappiani, Cinzia Verde
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e44508 (2012)
The Antarctic icefish Chaenocephalus aceratus lacks the globins common to most vertebrates, hemoglobin and myoglobin, but has retained neuroglobin in the brain. This conserved globin has been cloned, over-expressed and purified. To highlight similari
Externí odkaz:
https://doaj.org/article/b9f7268e7c4140a3b2f62ffbeed68267
Autor:
Luigi Vitagliano, Daniela Giordano, Anna Balsamo, Daniela Coppola, Giulietta Smulevich, Francesco P. Nicoletti, Antonello Merlino, Barry D. Howes, Lelio Mazzarella, Guido di Prisco, Alessandro Vergara, Cinzia Verde
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:1536-1540
The blood of the sub-Antarctic fish Eleginops maclovinus (Em) contains three haemoglobins. The major haemoglobin (Hb1Em) displays the Root effect, a drastic decrease in the oxygen affinity and a loss of cooperativity at acidic pH. The carbomonoxy for
Autor:
Matthew K. Thompson, Barry D. Howes, Michael F. Davis, Francesco P. Nicoletti, Vesna de Serrano, Giulietta Smulevich, Stefan Franzen
Publikováno v:
Biophysical Journal. 99:1586-1595
Dehaloperoxidase (DHP) from the annelid Amphitrite ornata is a catalytically active hemoglobin-peroxidase that possesses a unique internal binding cavity in the distal pocket above the heme. The previously published crystal structure of DHP shows 4-i
Autor:
Leonardo Boechi, Alberto Boffi, Giulietta Smulevich, Alessandra Comandini, Fernando Martín Boubeta, Alessandra Bonamore, Francesco P. Nicoletti, Alessandro Feis
Publikováno v:
Biochemistry. 49:2269-2278
The truncated hemoglobins from Bacillus subtilis (Bs-trHb) and Thermobifida fusca (Tf-trHb) have been shown to form high-affinity complexes with hydrogen sulfide in their ferric state. The recombinant proteins, as extracted, from Escherichia coli cel
Autor:
Giulietta Smulevich, Francesco P. Nicoletti, Matthew K. Thompson, Stefan Franzen, Barry D. Howes
Publikováno v:
Biochemistry. 49:1903-1912
The present work highlights the important role played by the distal histidine in controlling the binding of heme ligands in dehaloperoxidase (DHP) as compared to myoglobin and peroxidases. In DHP the distal histidine is highly mobile and undergoes a
Autor:
Giulietta Smulevich, Mauro Fasano, Maria Fittipaldi, Barry D. Howes, Francesco P. Nicoletti, Gabriella Fanali, Paolo Ascenzi
Publikováno v:
Journal of the American Chemical Society. 130:11677-11688
Human serum albumin (HSA), the most prominent protein in blood plasma, is able to bind a wide range of endogenous and exogenous compounds. Among the endogenous ligands, HSA is a significant transporter of heme, the heme-HSA complex being present in b
Autor:
Francesco P. Nicoletti, Giulietta Smulevich, Maria Fittipaldi, Alberto Boffi, Enrica Droghetti, Juan Pablo Bustamante, Alessandra Bonamore, Darío A. Estrin, Paola Baiocco, Barry D. Howes, Alessandro Feis
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2014, pp.9. ⟨10.1021/bi501132a⟩
Biochemistry, American Chemical Society, 2014, pp.9. ⟨10.1021/bi501132a⟩
The unique architecture of the active site of Thermobifida fusca truncated hemoglobin (Tf-trHb) and other globins belonging to the same family has stimulated extensive studies aimed at understanding the interplay between iron-bound ligands and distal
Autor:
Barry D. Howes, Darío A. Estrin, Alessandro Feis, Francesco P. Nicoletti, Natascia Sciamanna, Giulietta Smulevich, Alessandra Bonamore, Enrica Droghetti, Alberto Boffi, Juan Pablo Bustamante
Publikováno v:
BBA-Biochimica et Biophysica Acta
BBA-Biochimica et Biophysica Acta, Elsevier, 2013, 1834 (9), pp.1901-9. ⟨10.1016/j.bbapap.2013.02.033⟩
BBA-Biochimica et Biophysica Acta, Elsevier, 2013, 1834 (9), pp.1901-9. ⟨10.1016/j.bbapap.2013.02.033⟩
The ferric form of truncated hemoglobin II from Thermobifida fusca (Tf-trHb) and its triple mutant WG8F-YB10F-YCD1F at neutral and alkaline pH, and in the presence of CN− have been characterized by resonance Raman spectroscopy, electron paramagneti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e820143440b15fab93cad3bdc74e3e14
https://hal-riip.archives-ouvertes.fr/pasteur-01024175
https://hal-riip.archives-ouvertes.fr/pasteur-01024175
Autor:
Francesco P. Nicoletti, Paolo Ascenzi, Massimo Coletta, Chiara Ciaccio, Giulietta Smulevich, Gabriella Fanali, Mauro Fasano, Alessio Bocedi, Giampiero De Sanctis, Alessandra di Masi, Grazia R. Tundo
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 3, p e58842 (2013)
PLoS ONE, Vol 8, Iss 3, p e58842 (2013)
Human serum albumin (HSA), the most abundant protein in human plasma, could be considered as a prototypic monomeric allosteric protein, since the ligand-dependent conformational adaptability of HSA spreads beyond the immediate proximity of the bindin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d963c2ae197dcc30a48c47093a3b13a
http://hdl.handle.net/2108/90391
http://hdl.handle.net/2108/90391