The Experts below are selected from a list of 531 Experts worldwide ranked by ideXlab platform
Federico Benetti - One of the best experts on this subject based on the ideXlab platform.
-
Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site
Biochemistry, 2012Co-Authors: Paola D’angelo, Stefano Della Longa, Alessandro Arcovito, Giordano Mancini, Andrea Zitolo, Giovanni Chillemi, Gabriele Giachin, Giuseppe Legname, Federico BenettiAbstract:Prion diseases are a class of fatal neurodegenerative disorders characterized by Brain Spongiosis, synaptic degeneration, microglia and astrocytes activation, neuronal loss and altered redox control. These maladies can be sporadic, iatrogenic and genetic. The etiological agent is the prion, a misfolded form of the cellular prion protein, PrPC. PrPC interacts with metal ions, in particular copper and zinc, through the octarepeat and non-octarepeat binding sites. The physiological implication of this interaction is still unclear, as is the role of metals in the conversion. Since prion diseases present metal dyshomeostasis and increased oxidative stress, we described the copper-binding site located in the human C-terminal domain of PrP–HuPrP(90-231), both in the wild-type protein and in the protein carrying the pathological mutation Q212P. We used the synchrotron-based X-ray absorption fine structure technique to study the Cu(II) and Cu(I) coordination geometries in the mutant, and we compared them with thos...
Paola D’angelo - One of the best experts on this subject based on the ideXlab platform.
-
Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site
Biochemistry, 2012Co-Authors: Paola D’angelo, Stefano Della Longa, Alessandro Arcovito, Giordano Mancini, Andrea Zitolo, Giovanni Chillemi, Gabriele Giachin, Giuseppe Legname, Federico BenettiAbstract:Prion diseases are a class of fatal neurodegenerative disorders characterized by Brain Spongiosis, synaptic degeneration, microglia and astrocytes activation, neuronal loss and altered redox control. These maladies can be sporadic, iatrogenic and genetic. The etiological agent is the prion, a misfolded form of the cellular prion protein, PrPC. PrPC interacts with metal ions, in particular copper and zinc, through the octarepeat and non-octarepeat binding sites. The physiological implication of this interaction is still unclear, as is the role of metals in the conversion. Since prion diseases present metal dyshomeostasis and increased oxidative stress, we described the copper-binding site located in the human C-terminal domain of PrP–HuPrP(90-231), both in the wild-type protein and in the protein carrying the pathological mutation Q212P. We used the synchrotron-based X-ray absorption fine structure technique to study the Cu(II) and Cu(I) coordination geometries in the mutant, and we compared them with thos...
Gabriele Giachin - One of the best experts on this subject based on the ideXlab platform.
-
Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site
Biochemistry, 2012Co-Authors: Paola D’angelo, Stefano Della Longa, Alessandro Arcovito, Giordano Mancini, Andrea Zitolo, Giovanni Chillemi, Gabriele Giachin, Giuseppe Legname, Federico BenettiAbstract:Prion diseases are a class of fatal neurodegenerative disorders characterized by Brain Spongiosis, synaptic degeneration, microglia and astrocytes activation, neuronal loss and altered redox control. These maladies can be sporadic, iatrogenic and genetic. The etiological agent is the prion, a misfolded form of the cellular prion protein, PrPC. PrPC interacts with metal ions, in particular copper and zinc, through the octarepeat and non-octarepeat binding sites. The physiological implication of this interaction is still unclear, as is the role of metals in the conversion. Since prion diseases present metal dyshomeostasis and increased oxidative stress, we described the copper-binding site located in the human C-terminal domain of PrP–HuPrP(90-231), both in the wild-type protein and in the protein carrying the pathological mutation Q212P. We used the synchrotron-based X-ray absorption fine structure technique to study the Cu(II) and Cu(I) coordination geometries in the mutant, and we compared them with thos...
Alessandro Arcovito - One of the best experts on this subject based on the ideXlab platform.
-
Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site
Biochemistry, 2012Co-Authors: Paola D’angelo, Stefano Della Longa, Alessandro Arcovito, Giordano Mancini, Andrea Zitolo, Giovanni Chillemi, Gabriele Giachin, Giuseppe Legname, Federico BenettiAbstract:Prion diseases are a class of fatal neurodegenerative disorders characterized by Brain Spongiosis, synaptic degeneration, microglia and astrocytes activation, neuronal loss and altered redox control. These maladies can be sporadic, iatrogenic and genetic. The etiological agent is the prion, a misfolded form of the cellular prion protein, PrPC. PrPC interacts with metal ions, in particular copper and zinc, through the octarepeat and non-octarepeat binding sites. The physiological implication of this interaction is still unclear, as is the role of metals in the conversion. Since prion diseases present metal dyshomeostasis and increased oxidative stress, we described the copper-binding site located in the human C-terminal domain of PrP–HuPrP(90-231), both in the wild-type protein and in the protein carrying the pathological mutation Q212P. We used the synchrotron-based X-ray absorption fine structure technique to study the Cu(II) and Cu(I) coordination geometries in the mutant, and we compared them with thos...
Giuseppe Legname - One of the best experts on this subject based on the ideXlab platform.
-
Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site
Biochemistry, 2012Co-Authors: Paola D’angelo, Stefano Della Longa, Alessandro Arcovito, Giordano Mancini, Andrea Zitolo, Giovanni Chillemi, Gabriele Giachin, Giuseppe Legname, Federico BenettiAbstract:Prion diseases are a class of fatal neurodegenerative disorders characterized by Brain Spongiosis, synaptic degeneration, microglia and astrocytes activation, neuronal loss and altered redox control. These maladies can be sporadic, iatrogenic and genetic. The etiological agent is the prion, a misfolded form of the cellular prion protein, PrPC. PrPC interacts with metal ions, in particular copper and zinc, through the octarepeat and non-octarepeat binding sites. The physiological implication of this interaction is still unclear, as is the role of metals in the conversion. Since prion diseases present metal dyshomeostasis and increased oxidative stress, we described the copper-binding site located in the human C-terminal domain of PrP–HuPrP(90-231), both in the wild-type protein and in the protein carrying the pathological mutation Q212P. We used the synchrotron-based X-ray absorption fine structure technique to study the Cu(II) and Cu(I) coordination geometries in the mutant, and we compared them with thos...