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Biochemistry|April 17, 2002
A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substituted formIvano Bertini, Carl J Carrano, Claudio Luchinat, et al.
Inorganic Chemistry|October 24, 2001
1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme MoietyIvano Bertini, Alexander Dikiy, Claudio Luchinat, et al.
FEBS Letters|November 5, 1997
ePHOGSY experiments on a paramagnetic protein: location of the catalytic water molecule in the heme crevice of the oxidized form of horse heart cytochrome cI Bertini, C Dalvit, J G Huber, et al.
Biochemistry|August 8, 1995
Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced speciesI Bertini, A Dikiy, D H Kastrau, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 15, 2011
Solid-state NMR of proteins sedimented by ultracentrifugationIvano Bertini, Claudio Luchinat, Giacomo Parigi, et al.
The American Journal of Clinical Nutrition|November 20, 2015
Metabolomic fingerprint of severe obesity is dynamically affected by bariatric surgery in a procedure-dependent mannerEwa Gralka, Claudio Luchinat, Leonardo Tenori, et al.
Biochemistry|September 14, 1993
The electronic structure of [Fe4S4]3+ clusters in proteins. An investigation of the oxidized high-potential iron-sulfur protein II from Ectothiorhodospira vacuolataL Banci, I Bertini, S Ciurli, et al.
Bioconjugate Chemistry|March 12, 2009
Biotin-tagged probes for MMP expression and activation: design, synthesis, and binding propertiesElisa Dragoni, Vito Calderone, Marco Fragai, et al.
Journal of Magnetic Resonance. Series B|July 1, 1994
Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase III Bertini, B H Jonsson, C Luchinat, et al.
Computational and Structural Biotechnology Journal|January 24, 2020
A protocol to automatically calculate homo-oligomeric protein structures through the integration of evolutionary constraints and NMR ambiguous contactsDavide Sala, Linda Cerofolini, Marco Fragai, et al.
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