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Valeria Cafaro

Researcher at University of Naples Federico II

Publications -  49
Citations -  1319

Valeria Cafaro is an academic researcher from University of Naples Federico II. The author has contributed to research in topics: RNase P & Ribonuclease. The author has an hindex of 19, co-authored 46 publications receiving 1141 citations.

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Phenol Hydroxylase and Toluene/o-Xylene Monooxygenase from Pseudomonas stutzeri OX1: Interplay between Two Enzymes

TL;DR: Data on the specificity and the kinetic constants of ToMO and PH strongly support the hypothesis that coupling between the two enzymatic systems optimizes the use of nonhydroxylated aromatic molecules by the draining effect of PH on the product(s) of oxidation catalyzed by ToMO, thus avoiding phenol accumulation.
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Ribonuclease A can be transformed into a dimeric ribonuclease with antitumor activity.

TL;DR: A cDNA coding for bovine pancreatic RNase A was mutagenized to insert a proline, a leucine, and 2 cysteine residues, i.e. the residues present at corresponding positions in the subunit of seminal RNase, the only dimeric RNase of the pancreatic-type superfamily.
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Antimicrobial potency of cationic antimicrobial peptides can be predicted from their amino acid composition: Application to the detection of "cryptic" antimicrobial peptides.

TL;DR: It is shown that antimicrobial potency of CAMPs is linearly correlated to the product CmHnL where C is the net charge of the peptide, H is a measure of its hydrophobicity and L its length, and an accurate map of the molecular determinants of their antimicrobial activity is drawn.
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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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The antitumor action of seminal ribonuclease and its quaternary conformations

TL;DR: Antitumor activity assays, carried out on homogeneous quaternary forms of the enzyme, as well as on dimeric mutants of bovine pancreatic RNase A, reveal that another structural determinant of the antitumor action of BS‐RNase is the exchange of N‐terminal ends between subunits.