T. Maeda

发表

Role of Basic Residues for the Binding of ω-Conotoxin GVIA to N-Type Calcium Channels

Kazuki Sato, T. Kohno, M. Takahashi, 1993 .

Role of basic residues for the binding of omega-conotoxin GVIA to N-type calcium channels.

T. Kohno, M. Takahashi, N. Park, 1993, Biochemical and biophysical research communications.

Three-dimensional structure in solution of the calcium channel blocker omega-conotoxin MVIIA.

T. Kohno, K. Kobayashi, J I Kim, 1995, Biochemistry.

Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid beta(25-35) peptide as analyzed by single alanine substitution.

K. Imahori, A. Takashima, Kazuki Sato, 1995, Journal of biochemistry.

High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.

T. Kohno, T. Tsukahara, K. Sato, 1998, Biochemistry.

Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment.

A. Takashima, T. Kohno, K. Kobayashi, 1996, Biochemistry.

Formation of sheared G:A base pairs in an RNA duplex modelled after ribozymes, as revealed by NMR.

S. Fujii, T. Kohno, M. Katahira, 1994, Nucleic acids research.

Dimerization and DNA binding facilitate alpha-helix formation of Max in solution.

T. Saito, M. Katahira, S. Uesugi, 1997, Journal of biochemistry.

Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.

T. Kohno, S. Endo, K. Wakamatsu, 1996, Journal of biochemistry.