Cysteine protease inhibitor E64 reduces the rate of formation of selenite cataract in the whole animal.
暂无分享,去创建一个
[1] L. David,et al. Amelioration of cataracts and proteolysis in cultured lenses by cysteine protease inhibitor E64. , 1991, Investigative ophthalmology & visual science.
[2] T. Shearer,et al. Calpain II in two in vivo models of sugar cataract. , 1990, Experimental eye research.
[3] M. Maki,et al. Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. , 1989, The Journal of biological chemistry.
[4] T. Shearer,et al. Calpain II in human lens. , 1989, Investigative ophthalmology & visual science.
[5] I. Guggenmoos‐Holzmann,et al. Cell density of human lens epithelium in women higher than in men. , 1989, Investigative Ophthalmology and Visual Science.
[6] T. Murachi. Intracellular regulatory system involving calpain and calpastatin. , 1989, Biochemistry international.
[7] J. Wiseman,et al. Inhibition of the proteolysis of rat erythrocyte membrane proteins by a synthetic inhibitor of calpain. , 1988, Biochemical and biophysical research communications.
[8] T. Tsujinaka,et al. Synthesis of a new cell penetrating calpain inhibitor (calpeptin). , 1988, Biochemical and biophysical research communications.
[9] R. Mellgren,et al. Calcium‐dependent proteases: an enzyme system active at cellular membranes? , 1987, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[10] M. Tamai,et al. In vitro and in vivo inhibition of cysteine proteinases by EST, a new analog of E-64. , 1986, Journal of pharmacobio-dynamics.
[11] H. Kawasaki,et al. The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. , 1986, Journal of biochemistry.
[12] T. Shearer,et al. Purification of calpain II from rat lens and determination of endogenous substrates. , 1986, Experimental eye research.
[13] B. Horecker,et al. Role of phospholipids in the activation of the Ca2+-dependent neutral proteinase of human erythrocytes. , 1985, Biochemical and biophysical research communications.
[14] T. Shearer,et al. Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis. , 1984, Investigative ophthalmology & visual science.
[15] J. L. Britton,et al. Early development of selenium-induced cataract: slit lamp evaluation. , 1983, Experimental eye research.
[16] K. Suzuki. Reaction of calcium-activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid. , 1983, Journal of biochemistry.
[17] J. L. Britton,et al. Influence of selenite and fourteen trace elements on cataractogenesis in the rat. , 1983, Investigative ophthalmology & visual science.
[18] K. Kakinuma,et al. Evidence that NADPH is the actual substrate of the oxidase responsible for the "respiratory burst" of phagocytosing polymorphonuclear leukocytes. , 1983, Journal of biochemistry.
[19] H. Towbin,et al. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[20] S. Iwata. Process of Lens Opacification and Membrane Function: A Review , 1974 .
[21] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[22] T. Shearer,et al. Selenite cataract: a review. , 1987, Current eye research.
[23] T. Murachi,et al. Age-related changes of calpain II and alpha-crystallin in the lens of hereditary cataract (Nakano) mouse. , 1985, Current eye research.
[24] A. Barrett,et al. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. , 1982, The Biochemical journal.
[25] K. Imahori,et al. Inhibition of epoxide derivatives on chicken calcium-activated neutral protease (CANP) in vitro and in vivo. , 1980, Journal of biochemistry.