O
Oliviero Carugo
Researcher at University of Pavia
Publications - 184
Citations - 5004
Oliviero Carugo is an academic researcher from University of Pavia. The author has contributed to research in topics: Protein structure & Protein crystallization. The author has an hindex of 37, co-authored 177 publications receiving 4587 citations. Previous affiliations of Oliviero Carugo include Max F. Perutz Laboratories & International Centre for Genetic Engineering and Biotechnology.
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Journal ArticleDOI
Structure and bonding in metal sulfoxide complexes
Mario Calligaris,Oliviero Carugo +1 more
TL;DR: In this paper, structural parameters of free and coordinated sulfoxides are comprehensively reviewed and average values derived, and principal component analyses have been performed in order to evidence the deformation pathways of sulfoxide upon coordination.
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A normalized root-mean-spuare distance for comparing protein three-dimensional structures
Oliviero Carugo,Sándor Pongor +1 more
TL;DR: A simple procedure is presented to make the root‐mean‐square distances between pairs of three‐dimensional structures independent of their dimensions, which may be useful in evolutionary and fold classification studies as well as in simple comparisons between different structural models.
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NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding.
Oliviero Carugo,Patrick Argos +1 more
TL;DR: A systematic analysis of several crystal structures of NAD(P)‐protein complexes show that the NADP coenzymes are more flexible in conformation than those of NAD; although the protein‐cofactor interactions are largely conserved in the NAD complexes, they are quite variable in those of NadP; and in both cases the pocket around the nicotinamide moiety is substrate dependent.
Journal ArticleDOI
Protein-protein crystal-packing contacts.
Oliviero Carugo,Patrick Argos +1 more
TL;DR: The results suggest that protein crystallization depends on random protein‐ protein interactions, which have little in common with physiological protein‐protein recognition processes, and that the possibility of engineering macromolecular crystallization to improve crystal quality could be widened.
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A Mek1-Mek2 heterodimer determines the strength and duration of the Erk signal.
Federica Catalanotti,Gloria Reyes,Gloria Reyes,Veronika Jesenberger,Gergana Galabova-Kovacs,Ricardo De Matos Simoes,Oliviero Carugo,Manuela Baccarini +7 more
TL;DR: The role of Mek1 and Mek2 in growth factor–induced Erk phosphorylation is not interchangeable, and Mek1 is established as the crucial modulator of Mek and Erk signaling.