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Lin, G.D., Chattopadhyay, D., Maki, M., Wang, K.K., Carson, M., Jin, L., Yuen, P.W., Takano, E., Hatanaka, M., DeLucas, L.J. and Narayana, S.V. (1997) Crystal Structure of Calcium Bound Domain VI of Calpain at 1.9 A Resolution and Its Role in Enzyme Assembly, Regulation, and Inhibitor Binding. Nature Structural Molecular Biology, 4, 539-547.
http://dx.doi.org/10.1038/nsb0797-539

has been cited by the following article:

• TITLE: Phylogenetic Analysis and Taste Cell Expression of Calpain 9 in Catfish (Ictalurus punctatus)

  AUTHORS: Tetsuya Ookura, Eiki Koyama, Anne Hansen, John H. Teeter, Yukio Kawamura, Joseph G. Brand

  KEYWORDS: Gene Evolution, Taste, Novel Type

  JOURNAL NAME: Natural Science, Vol.7 No.3, March 13, 2015

  ABSTRACT: The calpains, calcium-activated neutral proteases, play important roles in calcium-regulated intra-cellular signal transduction cascades. Here we report the isolation and initial characterization of a cDNA encoding a calpain 9, digestive tract specific calpain, from catfish taste epithelium. This calpain 9 (Ip-CAPN9a) shares 61% identity with human calpain 9. Phylogenetic analysis provides evidence that catfish calpain 9 and the related enzymes from Oncorhynchus mykiss, Danio rerio, Xenopus laevis, Mus musculus, Rattus norvegicus and Homo sapiens make up a distinct clade within the tissue-specific calpain family. Northern blot analysis reveals that Ip-CAPN9a is predominantly expressed in barbell and digestive tract, but not expressed in brain. An antibody against the N-terminal segment of Ip-CAPN9a recognizes cells within the taste buds in catfish barbells.