P
Patrizia Polverino de Laureto
Researcher at University of Padua
Publications - 103
Citations - 7458
Patrizia Polverino de Laureto is an academic researcher from University of Padua. The author has contributed to research in topics: Protein structure & Protein folding. The author has an hindex of 39, co-authored 95 publications receiving 6910 citations. Previous affiliations of Patrizia Polverino de Laureto include International Centre for Genetic Engineering and Biotechnology.
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Journal ArticleDOI
Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
Giampietro Schiavo,Fabio Benfenati,Bernard Poulain,Ornella Rossetto,Patrizia Polverino de Laureto,Bibhuti R. DasGupta,Cesare Montecucco +6 more
TL;DR: The results indicate that tetanus and botulinum B neurotoxins block neurotransmitter release by cleaving synaptobrevin-2, a protein that, on the basis of the results, seems to play a key part in neurotransmitterRelease.
Journal ArticleDOI
Probing protein structure by limited proteolysis.
Angelo Fontana,Patrizia Polverino de Laureto,Barbara Spolaore,Erica Frare,Paola Picotti,Marcello Zambonin +5 more
TL;DR: The results underscore the utility of the limited proteolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics-function relationships of a novel and rare protein, especially if available in minute amounts.
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Identification of the nerve terminal targets of botulinum neurotoxin serotypes A, D, and E.
Giampietro Schiavo,Ornella Rossetto,S Catsicas,Patrizia Polverino de Laureto,B.R. DasGupta,Fabio Benfenati,Cesare Montecucco +6 more
TL;DR: It is shown that botulinum neurotoxin serotypes A, D, and E are zinc endoproteases specific for components of the synaptic vesicle docking and fusion complex, and the proteolytic activity of these neurotoxins is inhibited by EDTA and captopril.
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Probing the partly folded states of proteins by limited proteolysis
Angelo Fontana,Patrizia Polverino de Laureto,Vincenzo De Filippis,Elena Scaramella,Marcello Zambonin +4 more
TL;DR: This review focuses on the use of proteolytic enzymes as probes of the structure and dynamics of folding intermediates and shows that this simple biochemical technique can provide useful information, complementing that obtained by other commonly used techniques and approaches.
Journal ArticleDOI
Global analysis of protein structural changes in complex proteomes
Yuehan Feng,Giorgia De Franceschi,Abdullah Kahraman,Martin Soste,Andre Melnik,Paul J. Boersema,Patrizia Polverino de Laureto,Yaroslav Nikolaev,Ana Paula Oliveira,Paola Picotti +9 more
TL;DR: This approach assessed the structural features of more than 1,000 yeast proteins simultaneously and detected altered conformations for ∼300 proteins upon a change of nutrients, finding that some branches of carbon metabolism are transcriptionally regulated whereas others are regulated by enzyme conformational changes.