Characterization of a functional domain of human calpastatin.

[1]  M. Maki,et al.  Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. , 1988, The Journal of biological chemistry.

[2]  K. Titani,et al.  Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis. , 1988, Biochemistry.

[3]  H. Kawasaki,et al.  All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. , 1988, The Journal of biological chemistry.

[4]  B. Horecker,et al.  Effects of a monoclonal anti-calpain antibody on responses of stimulated human neutrophils. Evidence for a role for proteolytically modified protein kinase C. , 1988, The Journal of biological chemistry.

[5]  M. Maki,et al.  All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II , 1987, FEBS letters.

[6]  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.

[7]  R. Kannagi,et al.  Repetitive region of calpastatin is a functional unit of the proteinase inhibitor. , 1987, Biochemical and biophysical research communications.

[8]  K. Titani,et al.  Evidence for the repetitive domain structure of pig calpastatin as demonstrated by cloning of complementary DNA , 1986, FEBS letters.

[9]  Y Masui,et al.  Secretion cloning vectors in Escherichia coli. , 1984, The EMBO journal.

[10]  P. Leder,et al.  Antibodies to human c-myc oncogene product: evidence of an evolutionarily conserved protein induced during cell proliferation. , 1984, Science.

[11]  T. Murachi,et al.  [Calpain and calpastatin]. , 1983, Rinsho byori. The Japanese journal of clinical pathology.

[12]  T. Curran,et al.  Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that viral and cellular fos gene products have different carboxy termini , 1983, Cell.

[13]  K. Suzuki,et al.  Purification of an endogenous 68,000-dalton inhibitor of Ca2+-activated neutral protease from chicken skeletal muscle. , 1982, Biochimica et biophysica acta.

[14]  M. Inouye,et al.  DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an extremely AT-rich promoter , 1979, Cell.

[15]  A. van der Eb,et al.  The nucleotide sequence of the transforming HpaI-E fragment of adenovirus type 5 DNA. , 1978, Gene.

[16]  S. Weissman,et al.  The genome of simian virus 40. , 1978, Science.

[17]  Y. Ishino,et al.  cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. , 1989, Journal of enzyme inhibition.

[18]  K. Suzuki.  Calcium activated neutral protease: domain structure and activity regulation , 1987 .

[19]  A. W. Murray,et al.  Proteolytic activation of protein kinase C: a physiological reaction? , 1987 .

[20]  C. Yanisch-Perron,et al.  Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. , 1985, Gene.

[21]  K. Tanaka,et al.  Intracellular Ca2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin). , 1980, Advances in enzyme regulation.