Giachin, Gabriele
Overview
| Works: | 22 works in 23 publications in 1 language and 56 library holdings |
|---|---|
| Roles: | Editor, Contributor |
Publication Timeline
.
Most widely held works by
Gabriele Giachin
The prion phenomena in neurodegenerative diseases : new frontiers in neuroscience(
)
2 editions published in 2015 in English and held by 34 WorldCat member libraries worldwide
2 editions published in 2015 in English and held by 34 WorldCat member libraries worldwide
A novel expression system for production of soluble prion proteins in E. coli by Romany NN Abskharon(
)
1 edition published in 2012 in English and held by 2 WorldCat member libraries worldwide
1 edition published in 2012 in English and held by 2 WorldCat member libraries worldwide
Structural features of human prion protein variants revealed by NMR(
)
1 edition published in 2017 in English and held by 1 WorldCat member library worldwide
1 edition published in 2017 in English and held by 1 WorldCat member library worldwide
Structural differences of mule deer prion protein provides insight into chronic wasting disease(
)
1 edition published in 2018 in English and held by 1 WorldCat member library worldwide
1 edition published in 2018 in English and held by 1 WorldCat member library worldwide
Insights into molecular structures of human prion proteins with inherited mutations by NMR(
)
1 edition published in 2013 in English and held by 1 WorldCat member library worldwide
1 edition published in 2013 in English and held by 1 WorldCat member library worldwide
NMR structural studies of human cellular prion proteins(
)
1 edition published in 2013 in English and held by 1 WorldCat member library worldwide
1 edition published in 2013 in English and held by 1 WorldCat member library worldwide
NMR insights into early stages of structural conversion of human prion proteins related to inherited diseases(
)
1 edition published in 2014 in English and held by 1 WorldCat member library worldwide
1 edition published in 2014 in English and held by 1 WorldCat member library worldwide
Characterization of prion protein function by focal neurite stimulation(
)
1 edition published in 2016 in English and held by 1 WorldCat member library worldwide
The cellular prion protein (PrPC), encoded by the PRNP gene, is a ubiquitous glycoprotein, which is highly expressed in the brain. This protein, mainly known for its role in neurodegenerative diseases, is involved in several physiological processes including neurite outgrowth. By using a novel focal stimulation technique, we explored the potential function of PrPC, in its soluble form, as a signaling molecule. Thus, soluble recombinant prion proteins (recPrP) encapsulated in micro-vesicles were released by photolysis near the hippocampal growth cones. Local stimulation of wild-type growth cones with full-length recPrP induced neurite outgrowth and rapid growth cone turning towards the source. This effect was shown to be concentration dependent. Notably, PrPC-knockout growth cones were insensitive to recPrP stimulation, but this property was rescued in PrP-knockout growth cones expressing GFP-PrP. Taken together, our findings indicate that recPrP functions as a signaling molecule, and that its homophilic interaction with membrane-anchored PrPC might promote neurite outgrowth and facilitate growth cone guidance
1 edition published in 2016 in English and held by 1 WorldCat member library worldwide
The cellular prion protein (PrPC), encoded by the PRNP gene, is a ubiquitous glycoprotein, which is highly expressed in the brain. This protein, mainly known for its role in neurodegenerative diseases, is involved in several physiological processes including neurite outgrowth. By using a novel focal stimulation technique, we explored the potential function of PrPC, in its soluble form, as a signaling molecule. Thus, soluble recombinant prion proteins (recPrP) encapsulated in micro-vesicles were released by photolysis near the hippocampal growth cones. Local stimulation of wild-type growth cones with full-length recPrP induced neurite outgrowth and rapid growth cone turning towards the source. This effect was shown to be concentration dependent. Notably, PrPC-knockout growth cones were insensitive to recPrP stimulation, but this property was rescued in PrP-knockout growth cones expressing GFP-PrP. Taken together, our findings indicate that recPrP functions as a signaling molecule, and that its homophilic interaction with membrane-anchored PrPC might promote neurite outgrowth and facilitate growth cone guidance
NMR insights into the effects of disease-related mutations on human prion protein structure(
)
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
The N terminus of the prion protein mediates functional interactions with the neuronal cell adhesion molecule (NCAM) fibronectin
domain(
)
1 edition published in 2016 in English and held by 1 WorldCat member library worldwide
1 edition published in 2016 in English and held by 1 WorldCat member library worldwide
NMR insights into predisposition for structural conversion of inherited human prion diseases(
)
1 edition published in 2014 in English and held by 1 WorldCat member library worldwide
1 edition published in 2014 in English and held by 1 WorldCat member library worldwide
PrPC N-terminus mediated cross-talk with NCAM fibronectin domain(
)
1 edition published in 2017 in English and held by 1 WorldCat member library worldwide
1 edition published in 2017 in English and held by 1 WorldCat member library worldwide
Structural basis for the interaction between prion protein and the fibronectin type III domain of the neuronal cell adhesion
molecule(
)
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
Structural insights into disease-associated human prion protein mutants by NMR(
)
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
Epitope mapping of a PrP(Sc)-specific monoclonal antibody : identification of a novel C-terminally truncated prion fragment(
)
1 edition published in 2011 in English and held by 1 WorldCat member library worldwide
Monoclonal antibodies (mAbs) against prion proteins (PrPs) are indispensable in research and diagnosis of prion diseases, however the majority of these bind both the cellular (PrPC) and the disease-associated (PrPSc) isoforms. According to the widely accepted protein-only hypothesis the two isoforms share the same sequence, but differ in their conformation. In the present study we set to determine the critical binding residues of our PrPSc-specific mAbs with the view of discerning which residues play a key role in the conformational transition between PrPC and PrPSc. Focussing on the V5B2 mAb that provided differential labelling of prion-affected tissue from individualspositive for transmissible spongiform encephalopathies, we performed alanine scanning and phage-display epitope mapping to elucidate the antigenic determinants of this mAb and gain insight into its specificity on a molecular level. We observed that instead of discriminating between the two prion protein isoforms based on conformational differences, V5B2 binds a previously uncharacterized C-terminally truncated form of PrPSc that ends withthe residue Y226, which we named PrP226*. The addition of a single C-terminal amino-acid residue completely abolished V5B2 binding, while Westernblots using recombinant full-length PrPs and PrPs terminating at Y226 confirmed that the V5B2 mAb discriminates between the two based on their difference in length
1 edition published in 2011 in English and held by 1 WorldCat member library worldwide
Monoclonal antibodies (mAbs) against prion proteins (PrPs) are indispensable in research and diagnosis of prion diseases, however the majority of these bind both the cellular (PrPC) and the disease-associated (PrPSc) isoforms. According to the widely accepted protein-only hypothesis the two isoforms share the same sequence, but differ in their conformation. In the present study we set to determine the critical binding residues of our PrPSc-specific mAbs with the view of discerning which residues play a key role in the conformational transition between PrPC and PrPSc. Focussing on the V5B2 mAb that provided differential labelling of prion-affected tissue from individualspositive for transmissible spongiform encephalopathies, we performed alanine scanning and phage-display epitope mapping to elucidate the antigenic determinants of this mAb and gain insight into its specificity on a molecular level. We observed that instead of discriminating between the two prion protein isoforms based on conformational differences, V5B2 binds a previously uncharacterized C-terminally truncated form of PrPSc that ends withthe residue Y226, which we named PrP226*. The addition of a single C-terminal amino-acid residue completely abolished V5B2 binding, while Westernblots using recombinant full-length PrPs and PrPs terminating at Y226 confirmed that the V5B2 mAb discriminates between the two based on their difference in length
Analysis of molecular mobility in pathogenic and protective mutants of human prion protein from [sup] 15N relaxation data(
)
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
Structure of mule deer prion protein provides insight into chronic wasting disease(
)
1 edition published in 2018 in English and held by 1 WorldCat member library worldwide
1 edition published in 2018 in English and held by 1 WorldCat member library worldwide
NMR insights into structural differences of cellular prion protein caused by mutations in human genome(
)
1 edition published in 2014 in English and held by 1 WorldCat member library worldwide
1 edition published in 2014 in English and held by 1 WorldCat member library worldwide
Structural studies on cervids prion proteins(
)
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
1 edition published in 2015 in English and held by 1 WorldCat member library worldwide
Unique structural features of mule deer prion protein provide insights into chronic wasting disease(
)
1 edition published in 2019 in English and held by 1 WorldCat member library worldwide
1 edition published in 2019 in English and held by 1 WorldCat member library worldwide
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