J. Wakayama

发表

Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction.

H. Iwamoto, N. Yagi, Katsuaki Inoue, 2009, Biophysical journal.

Phospholipid interference In the Enzymic Hydrolysis as Determined by Adding Phosphoiipids in Water or in a Pooled Serum

J., J. Wakayama, 2004 .

Studies on irreversible inhibition of serine proteases by α-sulfonyloxyketone derivatives

E. Ikeda, J. Wakayama, H. Takei, 1996 .

Mechanism-based inactivation of α-chymotrypsin

E. Ikeda, J. Wakayama, H. Takei, 1996 .

Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy

N. Akiyama, D. Miyashiro, J. Wakayama, 2013, The Journal of Physiological Sciences.

Radial stiffness characteristics of the overlap regions of sarcomeres in isolated skeletal myofibrils in pre-force generating state

S. Ishiwata, Y. Shimamoto, D. Miyashiro, 2017, Biophysics and physicobiology.

Zigzag motions of the myosin-coated beads actively sliding along actin filaments suspended between immobilized beads.

Makoto Shohara, Takenori Yamada, Yuki Kunioka, 2002, Biochimica et biophysica acta.

Static and dynamic x-ray diffraction recordings from living mammalian and amphibian skeletal muscles.

H. Iwamoto, N. Yagi, T. Fujisawa, 2003, Biophysical journal.

Diversity of structural behavior in vertebrate conventional myosins complexed with actin.

H. Iwamoto, J. Sellers, Takuya Suzuki, 2007, Journal of molecular biology.

Methods for reducing nonspecific interaction in antibody-antigen assay via atomic force microscopy.

S. Akanuma, T. Ohtani, S. Sugiyama, 2008, Analytical biochemistry.

Evaluation of temperature effect on the interaction between β-lactoglobulin and anti-β-lactoglobulin antibody by atomic force microscopy.

S. Sugiyama, J. Wakayama, 2012, Biochemistry.

Molecular organizations of myofibrils of skeletal muscle studied by atomic force microscopy.

M. Aimi, N. Akiyama, J. Wakayama, 2003, Advances in experimental medicine and biology.

Atomic force microscopic evidence for Z-band as a rigid disc fixing the sarcomere structure of skeletal muscle.

J. Wakayama, T. Yamada, Takenori Yamada, 2000, Cell structure and function.

Contractility of single myofibrils of rabbit skeletal muscle studied at various MgATP concentrations.

J. Wakayama, T. Yamada, 2000, The Japanese journal of physiology.

Applications of atomic force microscopy in food nanotechnology.

H. Muramatsu, S. Sugiyama, J. Wakayama, 2013 .

Karyotype Analysis of Buckwheat Using Atomic Force Microscopy

Suresh Neethirajan, S. Sugiyama, J. Wakayama, 2011, Microscopy and Microanalysis.

IRREVERSIBLE INHIBITIONS OF SERINE PROTEASES BY PEPTIDYL ALLYLIC HALIDE DERIVATIVES

E. Ikeda, J. Wakayama, H. Takei, 1996 .

Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy

N. Akiyama, D. Miyashiro, J. Wakayama, 2013, Journal of Physiological Sciences.

Isometric contractile properties of single myofibrils of rabbit skeletal muscle.

J. Wakayama, T. Yamada, K. Yuri, 1998, Journal of biochemistry.

Mechanical strength of sarcomere structures of skeletal myofibrils studied by submicromanipulation.

M. Aimi, N. Akiyama, J. Wakayama, 2006, Cell structure and function.

Direct x-ray observation of a single hexagonal myofilament lattice in native myofibrils of striated muscle.

H. Iwamoto, Y. Nishikawa, T. Fujisawa, 2002, Biophysical journal.