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Fabrizio Dal Piaz

Researcher at University of Salerno

Publications -  175
Citations -  3955

Fabrizio Dal Piaz is an academic researcher from University of Salerno. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 33, co-authored 152 publications receiving 3272 citations. Previous affiliations of Fabrizio Dal Piaz include University of Bologna.

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Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3.

TL;DR: The data strongly suggest that the stability and aggregation properties of non-expanded ataxin-3 are determined by those of the Josephin domain, which is sufficient to reproduce the behaviour of the full-length protein.
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Very low protein diet reduces indoxyl sulfate levels in chronic kidney disease.

TL;DR: VLPD supplemented with ketoanalogues reduced IS serum levels in CKD patients not yet on dialysis, even preceded by an LPD, and after only 1 week of a VLPD, CKD Patients showed a significant reduction ofIS serum levels.
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Role of intracellular and extracellular annexin A1 in migration and invasion of human pancreatic carcinoma cells

TL;DR: The findings suggest that ANXA1 protein could regulate metastasis by favouring cell migration/invasion intracellularly, as cytoskeleton remodelling factor, and extracellularly like FPR ligand.
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Expression and purification of the recombinant subunits of toluene/o-xylene monooxygenase and reconstitution of the active complex

TL;DR: The cloning of the genes coding for each component of the complex of toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1 is described, and experimental evidence is reported which strongly support a model for the electron transfer.
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Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein.

TL;DR: It is demonstrated that, while determined by polyglutamine expansion, ataxin-1 aggregation is noticeably reduced by deletion of AXH or by replacement with the homologous sequence from the transcription factor HBP1, which has no known tendency to aggregate.