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Journal of Structural Biology|July 31, 2012
Structural characterization of CHCHD5 and CHCHD7: two atypical human twin CX9C proteinsLucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, et al.
Plos One|February 28, 2008
SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationLucia Banci, Ivano Bertini, Mirela Boca, et al.
Journal of the American Chemical Society|October 4, 2007
Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domainsIvano Bertini, Yogesh K Gupta, Claudio Luchinat, et al.
Journal of Medicinal Chemistry|November 24, 2005
Combining in silico tools and NMR data to validate protein-ligand structural models: application to matrix metalloproteinasesIvano Bertini, Marco Fragai, Andrea Giachetti, et al.
Journal of the American Chemical Society|January 10, 2012
An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALRLucia Banci, Ivano Bertini, Vito Calderone, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|June 19, 2009
Solution structure and dynamics of S100A5 in the apo and Ca2+-bound statesIvano Bertini, Soumyasri Das Gupta, Xiaoyu Hu, et al.
Journal of the American Chemical Society|March 20, 2012
Structural insights into the ferroxidase site of ferritins from higher eukaryotesIvano Bertini, Daniela Lalli, Stefano Mangani, et al.
Nature Chemical Biology|March 5, 2013
Atomic-resolution monitoring of protein maturation in live human cells by NMRLucia Banci, Letizia Barbieri, Ivano Bertini, et al.
The Journal of Biological Chemistry|March 14, 2009
Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)Ivano Bertini, Marco Fragai, Claudio Luchinat, et al.
Journal of the American Chemical Society|September 3, 2009
Transverse-dephasing optimized homonuclear j-decoupling in solid-state NMR spectroscopy of uniformly 13C-labeled proteinsSégolène Laage, Anne Lesage, Lyndon Emsley, et al.
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