Search Results - "De Sanctis, Giampiero"

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  1. 1

    Reciprocal allosteric modulation of carbon monoxide and warfarin binding to ferrous human serum heme-albumin by Bocedi, Alessio, De Sanctis, Giampiero, Ciaccio, Chiara, Tundo, Grazia R, Di Masi, Alessandra, Fanali, Gabriella, Nicoletti, Francesco P, Fasano, Mauro, Smulevich, Giulietta, Ascenzi, Paolo, Coletta, Massimo

    Published in PloS one (21-03-2013)
    “…Human serum albumin (HSA), the most abundant protein in human plasma, could be considered as a prototypic monomeric allosteric protein, since the…”
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  2. 2

    Reductive nitrosylation of ferric human serum heme-albumin by Ascenzi, Paolo, Cao, Yu, di Masi, Alessandra, Gullotta, Francesca, De Sanctis, Giampiero, Fanali, Gabriella, Fasano, Mauro, Coletta, Massimo

    Published in The FEBS journal (01-06-2010)
    “…Heme endows human serum albumin (HSA) with heme-protein-like reactivity and spectroscopic properties. Here, the kinetics and thermodynamics of reductive…”
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    Multiphasic Kinetics of Myoglobin/Sodium Dodecyl Sulfate Complex Formation by Feis, Alessandro, Tofani, Luca, De Sanctis, Giampiero, Coletta, Massimo, Smulevich, Giulietta

    Published in Biophysical journal (01-06-2007)
    “…We have carried out a kinetic analysis of the conformational changes that myoglobin (Mb) undergoes in the presence of the anionic surfactant sodium dodecyl…”
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  5. 5

    A Comparative Study on Axial Coordination and Ligand Binding in Ferric Mini Myoglobin and Horse Heart Myoglobin by De Sanctis, Giampiero, Petrella, Giovanni, Ciaccio, Chiara, Feis, Alessandro, Smulevich, Giulietta, Coletta, Massimo

    Published in Biophysical journal (15-09-2007)
    “…The absorption and resonance Raman spectra and the azide binding kinetics of ferric horse heart myoglobin (Mb) and mini myoglobin (a chemically truncated form…”
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    Reversible two-step unfolding of heme-human serum albumin: a ¹H-NMR relaxometric and circular dichroism study by Fanali, Gabriella, De Sanctis, Giampiero, Gioia, Magda, Coletta, Massimo, Ascenzi, Paolo, Fasano, Mauro

    “…Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reactivity center and a powerful spectroscopic probe. Here, the…”
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  8. 8

    rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization by Ciaccio, Chiara, Gambacurta, Alessandra, De Sanctis, Giampiero, Spagnolo, Domenico, Sakarikou, Christina, Petrella, Giovanni, Coletta, Massimo

    Published in Biochemical journal (15-04-2006)
    “…A Pichia pastoris expression system has for the first time been successfully developed to produce rhEPO (recombinant human eosinophil peroxidase). The…”
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  9. 9

    Effect of Axial Coordination on the Kinetics of Assembly and Folding of the Two Halves of Horse Heart Cytochrome c by De Sanctis, Giampiero, Ciaccio, Chiara, Fasciglione, Giovanni Francesco, Fiorucci, Laura, Gioia, Magda, Sinibaldi, Federica, Marini, Stefano, Santucci, Roberto, Coletta, Massimo

    Published in The Journal of biological chemistry (17-12-2004)
    “…The kinetics of the assembly of two complementary fragments of oxidized horse heart cytochrome c (cyt c), namely the heme-containing fragment-(1–56) and the…”
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  10. 10

    Relationships of Ligand Binding, Redox Properties, and Protonation in Coprinus cinereus Peroxidase by Ciaccio, Chiara, Rosati, Antonella, De Sanctis, Giampiero, Sinibaldi, Federica, Marini, Stefano, Santucci, Roberto, Ascenzi, Paolo, Welinder, Karen G., Coletta, Massimo

    Published in The Journal of biological chemistry (23-05-2003)
    “…The pH dependence of the redox potentials and kinetics for CO association and dissociation was determined between pH 3.0 and 13.0 at 25 °C for the wild-type…”
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  11. 11

    Modulation of the Catalytic Activity of Neutrophil Collagenase MMP-8 on Bovine Collagen I by Gioia, Magda, Fasciglione, Giovanni Francesco, Marini, Stefano, D'Alessio, Silvana, De Sanctis, Giampiero, Diekmann, Oliver, Pieper, Michael, Politi, Vincenzo, Tschesche, Harald, Coletta, Massimo

    Published in The Journal of biological chemistry (28-06-2002)
    “…The cleavage of bovine collagen I by neutrophil collagenase MMP-8 has been followed at pH 7.4, 37 °C. The behavior of the whole enzyme molecule (whMMP-8),…”
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  12. 12

    Cleavage of Bovine Collagen I by Neutrophil Collagenase MMP-8 by Marini, Stefano, Fasciglione, Giovanni Francesco, de Sanctis, Giampiero, D'Alessio, Silvana, Politi, Vincenzo, Coletta, Massimo

    Published in The Journal of biological chemistry (23-06-2000)
    “…The enzymatic processing of bovine collagen I by neutrophil collagenase (MMP-8) has been monitored at 37 °C, envisaging the occurrence of multiple intermediate…”
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  13. 13

    Coupling of the Oxygen-linked Interaction Energy for Inositol Hexakisphosphate and Bezafibrate Binding to Human HbA0 by Coletta, Massimo, Angeletti, Mauro, Ascenzi, Paolo, Bertollini, Alberto, Della Longa, Stefano, De Sanctis, Giampiero, Priori, Anna Maria, Santucci, Roberto, Amiconi, Gino

    Published in The Journal of biological chemistry (12-03-1999)
    “…The energetics of signal propagation between different functional domains (i.e. the binding sites for O2, inositol hexakisphospate (IHP), and bezafibrate…”
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  14. 14

    Enhanced heme accessibility in horse heart mini-myoglobin: Insights from molecular modelling and reactivity studies by Polticelli, Fabio, Zobnina, Veranika, Ciaccio, Chiara, de Sanctis, Giampiero, Ascenzi, Paolo, Coletta, Massimo

    Published in Archives of biochemistry and biophysics (01-11-2015)
    “…Mini-myoglobin (mini-HHMb) is a fragment of horse-heart myoglobin (HHMb) considered to be the prototype of the product encoded by the central exon of the HHMb…”
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  15. 15

    pH Dependence of Structural and Functional Properties of Oxidized Cytochrome c" from Methylophilus methylotrophus by Coletta, Massimo, Costa, Helena, De Sanctis, Giampiero, Neri, Francesca, Smulevich, Giulietta, Turner, David L., Santos, Helena

    Published in The Journal of biological chemistry (03-10-1997)
    “…Cytochrome c" fromMethylophilus methylotrophus is an unusual monoheme protein that undergoes a major redox-linked change in the heme arrangement: one of the…”
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  16. 16

    Folding of Apominimyoglobin by De Sanctis, G, Ascoli, F, Brunori, M

    “…The acid unfolding pathway of apominimyoglobin (apo-mini-Mb), a 108-aa fragment (aa 32-139) of horse heart apomyoglobin has been studied by means of circular…”
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  17. 17

    Thermodynamics of Inositol Hexakisphosphate Interaction with Human Oxyhemoglobin by Messana, I, Angeletti, M, Castagnola, M, De Sanctis, G, Di Stasio, E, Giardina, B, Pucciarelli, S, Coletta, M

    Published in The Journal of biological chemistry (19-06-1998)
    “…The interaction of inositol hexakisphosphate (IHP) with oxygenated human adult hemoglobin (Hb) was investigated at 25 °C. The affinity of IHP for oxygenated…”
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  18. 18

    Ibuprofen modulates allosterically NO dissociation from ferrous nitrosylated human serum heme-albumin by binding to three sites by Ascenzi, Paolo, di Masi, Alessandra, De Sanctis, Giampiero, Coletta, Massimo, Fasano, Mauro

    “…Human serum albumin (HSA) is a monomeric allosteric protein. Here, the effect of ibuprofen on denitrosylation kinetics ( k off) and spectroscopic properties of…”
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  19. 19

    Functional Modulation by Lactate of Myoglobin by Giardina, Bruno, Ascenzi, Paolo, Clementi, Maria Elisabetta, De Sanctis, Giampiero, Rizzi, Menico, Coletta, Massimo

    Published in The Journal of biological chemistry (19-07-1996)
    “…The effect of lactate on O2 binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH (i.e. pH 6.5, a…”
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  20. 20

    Reversible two-step unfolding of heme-human serum albumin: a (1)H-NMR relaxometric and circular dichroism study by Fanali, Gabriella, De Sanctis, Giampiero, Gioia, Magda, Coletta, Massimo, Ascenzi, Paolo, Fasano, Mauro

    Published in Journal of biological inorganic chemistry (01-02-2009)
    “…Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reactivity center and a powerful spectroscopic probe. Here, the…”
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