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Nenad Ban : ウィキペディア英語版
Nenad Ban

Nenad Ban is a Croatian biochemist born in Zagreb, Croatia who currently works at the ETH Zurich, Swiss Federal Institute of Technology, as a professor of Structural Molecular Biology.
==Career==
Nenad Ban was educated at the University of Zagreb and continued with his studies in the United States where he obtained a PhD degree at the University of California, Riverside in the laboratory of Alexander McPherson. His interest in large macromolecular assemblies led him for his postdoctoral work to the Department of Molecular Biophysics and Biochemistry at Yale University where he determined the atomic structure of the large ribosomal subunit by X-ray crystallography, as part of the group in the laboratory of Thomas A. Steitz. These results demonstrated that the ribosome is a ribozyme.〔Ban N, Nissen P, Hansen J, Moore PB, Steitz TA. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science. 2000 Aug 11;289(5481):905-20. PubMed PMID 10937989.〕
Since 2000 Nenad Ban is a professor of structural molecular biology at the ETH Zurich. (Swiss Federal Institute of Technology). His group is studying structure and function of large cellular assemblies using a combination of crystallographic, electron microscopic and biochemical experiments. Specifically focusing on various ribosomal complexes 〔Greber BJ, Boehringer D, Montellese C, Ban N. (2012)
Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit. Nat Struct Mol Biol.(12):1228-33.〕〔Greber BJ, Boehringer D, Godinic-Mikulcic V, Crnkovic A, Ibba M, Weygand-Durasevic I, Ban N. (2012) Cryo-EM Structure of the Archaeal 50S Ribosomal Subunit in Complex with Initiation Factor 6 and Implications for Ribosome Evolution.
J Mol Biol. 2012 Jan 27. (ahead of print )〕 involved in co-translational protein processing,〔Nat Struct Mol Biol. 18(1):88-90〕〔Bingel-Erlenmeyer R, Kohler R, Kramer G, Sandikci A, Antolić S, Maier T, Schaffitzel C, Wiedmann B, Bukau B, Ban N. (2008) A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing. Nature 452(7183):108-11〕 folding,〔Trigger Factor in Complex with the Ribosome forms a Molecular Cradle for Nascent Proteins. Nature 431(7008):590-6〕〔Kramer, G., Rauch, T., Rist, W., Vorderwulbecke, S., Patzelt, H., Schulze-Specking, A., Ban, N., Deuerling, E., Bukau, B. (2002). L23 protein functions as a chaperone docking site on the ribosome.〕 and targeting.〔Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N. (2011) The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor. Science 331(6019):881-886〕〔Estrozi LF, Boehringer D, Shan SO, Ban N, Schaffitzel C. (2010) Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor.〕〔Schaffitzel C, Oswald M, Berger I, Ishikawa T, Abrahams JP, Koerten HK, Koning RI and Ban N. (2006) Structure of the E. coli signal recognition particle bound to a translating ribosome. Nature 444(7118):503-6〕〔Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E and Ban N. (2004)〕
His group has obtained detailed structural information on eukaryotic ribosomes, which are significantly larger and more complex than their bacterial counterparts, by determining the first complete structures of both eukaryotic ribosomal subunits each in complex with an initiation factor.〔Klinge S, Voigts-Hoffmann F, Leibundgut M, Arpagaus S, Ban N. (2011) Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6.Science 334(6058):941-948, Published Online November 3, 2011〕〔Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. (2010) Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331(6018):730-6〕 Furthermore, his group investigated giant multifunctional enzymes involved in fatty acid synthesis offer first mechanistic insights into substrate shuttling and delivery in such megasynthases, with direct implications for our understanding of polyketide synthases.〔Maier T, Leibundgut M, and Ban N (2008) The Crystal Structure of a Mammalian Fatty Acid Synthase. Science 321(5894):1315-22〕〔Leibundgut M, Jenni S, Frick C, Ban N. (2007) Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase.
Science 316(5822):288-290〕〔Jenni S, Leibundgut M, Boehringer D, Frick C, Mikolásek B, Ban N. (2007) Structure of Fungal Fatty Acid Synthase and Implications for Iterative Substrate Shuttling. Science 316:(5822):254-261. Pubmed〕〔Maier T, Jenni S, and Ban N. (2006) Architecture of mammalian fatty acid synthase at 4.5 Å resolution.
Science 311(5765):1258-62〕〔Jenni S, Leibundgut M, Maier T and Ban N. (2006) Architecture of a fungal fatty acid synthase at 5 Å resolution. Science 311(5765):1263-7〕

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