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
Atom depth as a descriptor of the protein interior.
TL;DR: It is shown that dpx values can be used to partition atoms in discrete layers according to their depth and to identify atoms that, although buried, are potential targets for posttranslational modifications like phosphorylation.
Journal ArticleDOI
How root-mean-square distance (r.m.s.d.) values depend on the resolution of protein structures that are compared
Oliviero Carugo,Oliviero Carugo +1 more
TL;DR: In this paper, the root-mean-square distance (r.m.s.) between equivalent atoms is computed after optimal superposition of the two structures that are compared. But the dependence of the r.ms.s. values on the protein-pair dimensions is unknown.
Journal ArticleDOI
DPX: for the analysis of the protein core
TL;DR: A simple and fast algorithm that measures the depth of each atom in a protein (dpx), defined as its distance from the closest solvent accessible atom, is described.
Journal ArticleDOI
Direct Interaction of Actin Filaments with F-Bar Protein Pacsin2.
Julius Kostan,Ulrich Salzer,Ulrich Salzer,Albina Orlova,Imre Törö,Vesna Hodnik,Yosuke Senju,Juan Zou,Claudia Schreiner,Julia Steiner,Jari Meriläinen,Marko Nikki,Ismo Virtanen,Oliviero Carugo,Oliviero Carugo,Juri Rappsilber,Juri Rappsilber,Pekka Lappalainen,Veli-Pekka Lehto,Gregor Anderluh,Edward H. Egelman,Kristina Djinović-Carugo,Kristina Djinović-Carugo +22 more
TL;DR: It is shown that the F‐BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N‐B BAR and F‐ BAR proteins (endophilin, CIP4 and FCHO2) do not associate withActin.
Journal ArticleDOI
Targeted proteolysis of plectin isoform 1a accounts for hemidesmosome dysfunction in mice mimicking the dominant skin blistering disease EBS-Ogna.
Gernot Walko,Nevena Vukasinovic,Karin Gross,Irmgard Fischer,Sabrina Sibitz,Peter Fuchs,Siegfried Reipert,Ute Jungwirth,Walter Berger,Ulrich Salzer,Oliviero Carugo,Oliviero Carugo,Maria J. Castañón,Gerhard Wiche +13 more
TL;DR: Focal self-association of plectin molecules as a novel mechanism contributing to hemidesmosome homeostasis and stabilization is proposed.