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Paolo Viglino

Researcher at University of Udine

Publications -  103
Citations -  3031

Paolo Viglino is an academic researcher from University of Udine. The author has contributed to research in topics: Superoxide dismutase & Protein structure. The author has an hindex of 30, co-authored 103 publications receiving 2944 citations. Previous affiliations of Paolo Viglino include Ca' Foscari University of Venice.

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Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.

TL;DR: Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that δN6β2‐m could be a key intermediate of a proteolytic pathway of β2‐microglobulin.
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The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

TL;DR: The solution structure of human β2‐microglobulin (β2‐m), the nonpolymorphic component of class I major histocompatibility complex (MHC‐I), was determined by 1H NMR spectroscopy and restrained modeling calculations.
Journal Article

Superoxide ion as active intermediate in the autoxidation of ascorbate by molecular oxygen.

TL;DR: The oxidation of ascorbic acid by molecular oxygen was investigated by optical and magnetic resonance methods in the presence and in the absence of copper and iron complexes and an upper limit for the kinetic rate constant of the reaction between the ascorBate radical and the superoxide ion is reported.
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Superoxide ion as active intermediate in the autoxidation of ascorbate by molecular oxygen. Effect of superoxide dismutase.

TL;DR: In this article, an upper limit for the kinetic rate constant of the reaction between the ascorbate radical and the superoxide ion is reported, and the effect of addition of Cu,Zn superoxide dismutase was discussed and a reaction mechanism was proposed.
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Polarographic determination of superoxide dismutase.

TL;DR: The results fit very well with data previously obtained with other methods and show that this polarographic procedure can be used under conditions that render the other methods unsuitable for the measurement of the enzyme activity.