Literature for peptidase C02.007: calpain-8

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Literature Substrates

(Topics flags: K Knockout, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

    2024
  1. Carroll,S.H., Schafer,S., Kawasaki,K., Tsimbal,C., Jule,A.M., Hallett,S.A., Li,E. and Liao,E.C.
    Genetic requirement of dact1/2 to regulate noncanonical Wnt signaling and calpain 8 during embryonic convergent extension and craniofacial morphogenesis
    elife13, PubMed  Europe PubMed DOI
  2. Pandey,A., Cousin,H., Kumar,S., Taylor,L., Chander,A., Coppenrath,K., Shaidani,N.I., Horb,M. and Alfandari,D.
    ADAM interact with large protein complexes to regulate Histone modification, gene expression and splicing
    bioRxiv PubMed  Europe PubMed DOI
  3. 2016
  4. Hata,S., Kitamura,F., Yamaguchi,M., Shitara,H., Murakami,M. and Sorimachi,H.
    A gastrointestinal calpain complex, G-calpain, is a heterodimer of CAPN8 and CAPN9 calpain isoforms, which play catalytic and regulatory roles, respectively
    J Biol Chem291, 27313-27322. PubMed  Europe PubMed DOI
  5. 2012
  6. Sorimachi,H., Hata,S. and Ono,Y.
    Gastrointestinal calpain
    [ISSN:978-0-12-407743-0]3, 2018-2022. DOI
  7. 2011
  8. Cousin,H., Abbruzzese,G., Kerdavid,E., Gaultier,A. and Alfandari,D.
    Translocation of the cytoplasmic domain of ADAM13 to the nucleus is essential for Calpain8-a expression and cranial neural crest cell migration
    Dev Cell20, 256-263. PubMed  Europe PubMed DOI
  9. 2010
  10. Hata,S., Abe,M., Suzuki,H., Kitamura,F., Toyama-Sorimachi,N., Abe,K., Sakimura,K. and Sorimachi,H.
    Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense
    PLoS Genet6, e1001040-e1001040. PubMed  Europe PubMed DOI  K
  11. 2007
  12. Hata,S., Doi,N., Kitamura,F. and Sorimachi,H.
    Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains
    J Biol Chem282, 27847-27856. PubMed  Europe PubMed DOI
  13. 2006
  14. [YEAR:13-2-2006]Hata,S., Koyama,S., Kawahara,H., Doi,N., Maeda,T., Toyama-Sorimachi,N., Abe,K., Suzuki,K. and Sorimachi,H.
    Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP
    J Biol Chem281, 11214-11224. PubMed  Europe PubMed DOI
  15. 2004
  16. Sorimachi,H.
    Other calpains
    [ISSN:0-12-079610-4]2, 1217-1225.  V
  17. 2001
  18. Hata,S., Nishi,K., Kawamoto,T., Lee,H.J., Kawahara,H., Maeda,T., Shintani,Y., Sorimachi,H. and Suzuki,K.
    Both the conserved and the unique gene structure of stomach-specific calpains reveal processes of calpain gene evolution
    J Mol Evol53, 191-203. PubMed  Europe PubMed DOI
  19. 1994
  20. [YEAR:18-4-1994]Sorimachi,H., Saido,T.C. and Suzuki,K.
    New era of calpain research. Discovery of tissue-specific calpains
    FEBS Lett343, 1-5. PubMed  Europe PubMed DOI
  21. 1993
  22. [YEAR:15-9-1993]Sorimachi,H., Ishiura,S. and Suzuki,K.
    A novel tissue-specific calpain species expressed predominantly in the stomach comprises two alternative splicing products with and without Ca(2+)-binding domain
    J Biol Chem268, 19476-19482. PubMed  Europe PubMed