M
Martino Bolognesi
Researcher at University of Milan
Publications - 474
Citations - 19590
Martino Bolognesi is an academic researcher from University of Milan. The author has contributed to research in topics: Protein structure & Heme. The author has an hindex of 67, co-authored 465 publications receiving 18390 citations. Previous affiliations of Martino Bolognesi include Katholieke Universiteit Leuven & University of Genoa.
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Journal ArticleDOI
Atlas of the clinical genetics of human dilated cardiomyopathy
Jan Haas,Karen S. Frese,Barbara Peil,Wanda Kloos,Andreas Keller,Rouven Nietsch,Zhu Feng,Sabine Müller,Elham Kayvanpour,Britta Vogel,Farbod Sedaghat-Hamedani,Wei Keat Lim,Xiaohong Zhao,Dmitriy Fradkin,Doreen Köhler,Simon Fischer,Jennifer Franke,Sabine Marquart,Ioana Barb,Daniel Tian Li,Ali Amr,Philipp Ehlermann,Derliz Mereles,Tanja Weis,Sarah Hassel,Andreas Kremer,Vanessa King,Emil Wirsz,Emil Wirsz,Richard Isnard,Michel Komajda,Alessandra Serio,Maurizia Grasso,Petros Syrris,Eleanor Wicks,Vincent Plagnol,Luis R. Lopes,Tenna Gadgaard,Hans Eiskjær,Mads E. Jørgensen,Diego García-Giustiniani,Martin Ortiz-Genga,María G. Crespo-Leiro,Rondal H Lekanne Dit Deprez,Imke Christiaans,Ingrid A.W. van Rijsingen,Arthur A.M. Wilde,Anders Waldenström,Martino Bolognesi,Riccardo Bellazzi,Stellan Mörner,Justo Lorenzo Bermejo,Lorenzo Monserrat,Eric Villard,Jens Mogensen,Yigal M. Pinto,Philippe Charron,Perry M. Elliott,Eloisa Arbustini,Hugo A. Katus,Benjamin Meder +60 more
TL;DR: This is to the authors' knowledge, the first study that comprehensively investigated the genetics of DCM in a large-scale cohort and across a broad gene panel of the known DCM genes and underline the high analytical quality and feasibility of Next-Generation Sequencing in clinical genetic diagnostics.
Journal ArticleDOI
Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
Albrecht Messerschmidt,Rudolf Ladenstein,Robert Huber,Martino Bolognesi,Luciana Avigliano,Raffaele Petruzzelli,Antonello Rossi,Alessandro Finazzi-Agrò +7 more
TL;DR: The crystal structure of the fully oxidized form of ascorbate oxidase from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution, using an energy-restrained least-squares refinement procedure.
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X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.
Albrecht Messerschmidt,Antonello Rossi,Rudolf Ladenstein,Robert Huber,Martino Bolognesi,Guiseppina Gatti,Augusto Marchesini,Raffaele Petruzzelli,Alessandro Finazzi-Agrò +8 more
TL;DR: Two crystal forms of the multi-copper protein ascorbate oxidase from Zucchini have been analysed at 2.5 A resolution and a model of the polypeptide chain and the copper ions and their ligands has been built.
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Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants
TL;DR: Crystal structures show that trHb tertiary structure is based on a 2-on-2 -hel-ical sandwich, which represents an unprecedented editing of the highly conserved globin fold, and may provide a path for ligand diffusion to the heme.
Journal ArticleDOI
Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution.
Hugo L. Monaco,Giuseppe Zanotti,Paola Spadon,Martino Bolognesi,Lindsay Sawyer,Elias Eliopoulos +5 more
TL;DR: The structure of the trigonal crystal form of bovine beta-lactoglobulin has been determined by X-ray diffraction methods and an electron density map served as a starting point for alternate cycles of model building and restrained least-squares refinement.