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Archives of Biochemistry and Biophysics|August 1, 1985
Structural characterization of the calcium binding protein s100 from adipose tissueD R Marshak, H Umekawa, D M Watterson, et al.
Biochemical Pharmacology|December 24, 1996
Cellular events involved in the sensitization of etoposide-resistant cells by inhibitors of calcium-calmodulin-dependent processes. Role for effects on apoptosis, DNA cleavable complex, and phosphorylationK Kawamura, D Grabowski, K Krivacic, et al.
Clinical and Experimental Pharmacology & Physiology|March 1, 1991
Inhibition of cyclic GMP phosphodiesterase by xanthine derivatives relaxes guinea-pig trachealis smooth muscleH Tanaka, K Ogawa, K Takagi, et al.
Biochemical and Biophysical Research Communications|June 25, 1996
Isoform-specific intracellular vesicle formation by recombinant annexin XI-A in Sf9 cellsT Sudo, N Mamiya, M Goto, et al.
The Journal of Biological Chemistry|May 5, 1992
A calcyclin-associated protein is a newly identified member of the Ca2+/phospholipid-binding proteins, annexin familyH Tokumitsu, A Mizutani, H Minami, et al.
Archives of Biochemistry and Biophysics|April 1, 1995
The long amino-terminal tail domain of annexin XI is necessary for its nuclear localizationA Mizutani, N Watanabe, T Kitao, et al.
Molecular Pharmacology|June 1, 1989
Thyroid hormones directly interact with vascular smooth muscle stripsT Ishikawa, T Chijiwa, M Hagiwara, et al.
Biochemical and Biophysical Research Communications|December 16, 1991
Molecular cloning and sequencing of a cDNA clone encoding a new calcium binding protein, named calgizzarin, from rabbit lungM Watanabe, Y Ando, H Todoroki, et al.
Biochemical and Biophysical Research Communications|June 30, 1987
The Ca2+ -activated protease (calpain) modulates Ca2+/calmodulin dependent activity of smooth muscle myosin light chain kinaseM Ito, T Tanaka, K Nunoki, et al.
Cancer Letters|March 1, 1982
Antitumor effect of dicyclohexylammonium sulfate, a potent inhibitor of spermidine synthase against P388 leukemiaH Ito, H Hibasami, K Shimura, et al.
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