ŸEscherichia coli cyclophilin B binds a highly distorted form of trans-propyl peptide isomer.@by M. Konno, Y. Sano, K. Okudaira, Y. Kawaguchi, Y. Yamagishi-Ohmori, S. Fushinobu, & H. Matsuzawa Eur. J. Biochem. 271, 3794-3803 (2004)
ŸParameter landscape analysis for improving the performance of common motif detection algorithms. by N. Poluliakh, M. Konno, T. Takagi & K. Nakai Genome Informatics Series, 13, 430-431 (2002)
ŸCrystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3-A resolution: specific interactions at subunit interfaces. by H. Uchikoba, S. Fushinobu, T. Wakagi, M. Konno, H. Taguchi, H. Matsuzawa Proteins: Structure, Function, and Genetics, 46(2), 206-214 (2002)
Ÿ "Melina"- novel tool for elucidation of consensus motif in the promoter regions of functionally related DNA sequences. by N. Poluliakh, M. Konno, T. Takagi, & K. Nakai Genome Informatics Series, 12, 388-389 (2001)
ŸThe 2.0-A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules present In other class I enzymes. by I. Sugiura, O. Nureki, Y. Ugaji, S. Kuwabara, A. Shimada, M. Tateno, B. Lober, R. Giege, D. Moras, S. Yokoyama & M. Konno Structure , 8, 197-208 (2000)
ŸCrystal structure of E. coli methionyl-tRNA synthetase highlights species-specific feature. by Y. Mechulam, E. Schmitt, L. Maveyraud, C. Zelwer, O. Nureki, S. Yokoyama, M. Konno, & S. Blanquet, J. Mol. Biol. 294, 1287-1297 (1999)
ŸFunctional structures of class-I aminoacyl-tRNA synthetases. by O. Nureki, S. Sekine, A. Shimada, T. Nakama, S. Fukai, D.V. Vassylyev, I. Sugiura, S. Kuwabara, M. Tateno, M. Nakasako, D. Moras, M. Konno, & S. Yokoyama, RNA Biochemistry and Biotechnology, 149-158 (1999), J Barciszewski and B.F.C. Clark (eds).
Ÿ Crystal structure of the E166A mutant of extended spectrum ƒÀ-lactamase Toho-1 at 1.8 A resolution. by A. Ibuka, A. Taguchi, M. Ishiguro, S. Fushinobu, Y. Ishii, S. Kamitori, K. Okuyama, K. Yamaguchi, M. Konno, H. Matsuzawa J. Mol. Biol. 285, 2079-2087 (1999)
Ÿ Enzyme structure with two catalytic sites for double-sieve selection of substrate. by O. Nureki, D. G. Vassylyev, M. Tateno, A. Shimada, T. Nakama, S. Fukai, M. Konno, T. L. Hendrickson, P. Schimmel & S. Yokoyama Science, 280, 578-582 (1998)
Ÿ Crystallographic and mutational analyes of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH. by S. Fushinobu, K. Ito, M. Konno, T. Wakagi & H. Matsuzawa Protein Engineering, 11, 1121-1128 (1998)
Ÿ Crystal Structure of bis(diphenylglyoximato)nickel(II); Ni(pdg)2. by M. Konno, A. Kashima, I. Shirotani Zeitschrift fur Kristall. 212, 815-818 (1997).
Ÿ Structure and Absorption Spectra of the Thin Films of Triphenodithiazine, C18N2S2H10. by Y. Inagaki, I. Shirotani, M. Konno, N. Sato, H. Nishi Mol. Cryst. Liq. Cryst. 296, 397-407 (1997)
Ÿ Crystal Structure and Electrical Property of (BEDT-TTF)5[Pt(SCN)4]. by M. Konno, K. Ohfuchi, I. Shirotani, H. Yamochi, G. Saito Zeitschrift fur Kristall. 212, 121-125 (1997)
Ÿ New Organic Metals based on Vinylenedithio-annulated Diselenadithiafulvalene Derivatives. by J. Yamada, S. Satoki, H. Anzai, K. Hagiya, M. Tamura, Y. Nishio, K. Kajita, E. Watanabe, M. Konno, T. Sato, H. Nishikawa, & K. Kikuchi Chem. Commun. 1955-1956 (1996)
Ÿ The Substrate-Binding Site in Escherichia coli Cyclophilin A Preferably Recognizes a cis-Proline-Isomer or a Highly Distorted Form of the trans-Isomer. by M. Konno, M. Ito, T. Hayano & N. Takahashi J. Mol. Biol. 256,897-908 (1996)
Ÿ Aromatase Inhibitors: Synthesis, Biological Activity and Structure of 1,2-Imidazolyl Methylcyclopentanol Derivatives. by A. Kato, Y. Ikeda, N. Sugita, T. Nitta, H. Enari, A Kashima, M. Konno & K. Niimura C. P. Bull. 43, 2152-2158 (1995)
Ÿ The pH-dependent Changes of the Enzymic Activity and Spectroscopic Properties of Iron-Substituted Manganese Superoxide Dismutase. by F. Yamakura, K. Kobayashi, H. Ue & M. Konno Eur. J. Biochem. 227, 700-706 (1995)
Ÿ Search of Candidate to Supply Electron to MnSOD by M. Konno & Y. Suzuki Frontier of Reactive Oxygen Species in Biology and Medicine, Elsevier Amsterdam, 137-138 (1994)