S. Yamada

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Activation of the 20S Proteasome of Xenopus Oocytes by SDS: Evidence for the Substrate-Induced Conformational Change Characteristic of Trypsin-Like Peptidase

T. Tokumoto, K. Ishikawa, J. Yamada, 1998, Zoological science.

Reaction mechanism of calcium-ATPase of sarcoplasmic reticulum. Substrates for phosphorylation reaction and back reaction, and further resolution of phosphorylated intermediates.

N. Ikemoto, S. Yamada, 1980, The Journal of biological chemistry.

Irreversible Potent Activation and Reversible Inhibition of Trypsin-Like Activity of 20S Proteasome Purified from Xenopus Oocytes by Fatty Acid

T. Tokumoto, K. Ishikawa, K. Sato, 1998, Zoological science.

Formation of the dermal chromatophore unit (DCU) in the tree frog Hyla arborea.

S. Yamada, M. Yasutomi, 1998, Pigment cell research.

Reaction of 20S proteasome: shift of SDS-dependent activation profile by divalent cations.

K. Ishikawa, H. Yoshimura, S. Yamada, 1995, Journal of biochemistry.

Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1

H. Dohra, T. Ushimaru, T. Tokumoto, 2008, BMC Biochemistry.

Disappearance of a novel protein component of the 26S proteasome during Xenopus oocyte maturation.

M. Lohka, R. Horiguchi, Y. Nagahama, 1999, Experimental cell research.

High affinity Zn2+ inhibitory site(s) for the trypsin-like peptidase of the 20S proteasome.

M. Yamazaki, Takafumi Shimizu, T. Tokumoto, 2008, Archives of biochemistry and biophysics.

Reaction mechanism of the Ca 2+ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. VII. Recognition and release of Ca 2+ ions.

Y. Tonomura, S. Yamada, 1972, Journal of biochemistry.

Ca2+-controlled conformational states of the Ca2+ transport enzyme of sarcoplasmic reticulum.

N. Ikemoto, J. F. Morgan, S. Yamada, 1978, The Journal of biological chemistry.

Distinction of thiols involved in the specific reaction steps of the Ca2+-ATPase of the sarcoplasmic reticulum.

N. Ikemoto, S. Yamada, 1978, The Journal of biological chemistry.

Reaction mechanism of the Ca2+-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. 8. Molecular mechanism of the conversion of osmotic energy to chemical energy in the sarcoplasmic reticulum.

Y. Tonomura, M. Sumida, S. Yamada, 1970, Journal of biochemistry.

Reaction mechanism of the Ca2 plus-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. 3. Ca plus-uptake and ATP-splitting.

Y. Tonomura, T. Yamamoto, S. Yamada, 1970, Journal of biochemistry.

ATP inactivates hydrolysis of the K+-sensitive phosphoenzyme of kidney Na+,K+-transport ATPase and activates that of muscle sarcoplasmic reticulum Ca2+-transport ATPase.

M. Nakao, Y. Fukushima, S. Yamada, 1984, Journal of biochemistry.

Sarcoplasmic reticulum Ca-ATPase: distinction of phosphoenzymes formed from MgATP and CaATP as substrates and interconversion of the phosphoenzymes by Mg2+ and Ca2+.

J. Fujii, H. Katayama, S. Yamada, 1986, Journal of biochemistry.

ATP formation from ADP and a phosphorylated intermediate of Ca2+-dependent ATPase in fragmented sarcoplasmic reticulum.

Y. Tonomura, T. Kanazawa, S. Yamada, 1970, Journal of biochemistry.

Activation of the 20S proteasome of Xenopus oocytes by cardiolipin: blockage of the activation of trypsin-like activity by the substrate.

T. Tokumoto, K. Ishikawa, M. Uritani, 1998, Bioscience, biotechnology, and biochemistry.

Atomic force microscopy studies of interaction of the 20S proteasome with supported lipid bilayers.

J. Hirokawa, M. Yamazaki, S. Yamada, 2003, Biochimica et biophysica acta.

Reaction mechanism of the Ca 2+ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. VI. Co-operative transition of ATPase activity during the initial phase.

Y. Tonomura, T. Yamamoto, T. Kanazawa, 1971, Journal of biochemistry.