Two cysteine proteinases respond to bacterial and WSSV challenge in Chinese white shrimp Fenneropenaeus chinensis.

[1]  Shicui Zhang,et al.  Identification and functional characterization of legumain in amphioxus Branchiostoma belcheri. , 2009, Bioscience reports.

[2]  Xiao-Fan Zhao,et al.  Molecular cloning and characterization of the translationally controlled tumor protein from Fenneropenaeus chinensis , 2009, Molecular Biology Reports.

[3]  Zhenming Xu,et al.  Clip domain serine protease and its homolog respond to Vibrio challenge in Chinese white shrimp, Fenneropenaeus chinensis. , 2009, Fish & shellfish immunology.

[4]  Xiao-Fan Zhao,et al.  Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis. , 2008, Fish & shellfish immunology.

[5]  Xiu-xia Zhou,et al.  Identification of differentially expressed immune-relevant genes in Chinese soft-shelled turtle (Trionyx sinensis) infected with Aeromonas hydrophila. , 2008, Veterinary immunology and immunopathology.

[6]  Joel Dudley,et al.  MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences , 2008, Briefings Bioinform..

[7]  L. Qiu,et al.  Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon). , 2008, Comparative biochemistry and physiology. Part A, Molecular & integrative physiology.

[8]  Xiaohong Huang,et al.  HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion. , 2008, Journal of insect physiology.

[9]  M. Bogyo,et al.  IrAE: an asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus. , 2007, International journal for parasitology.

[10]  S. Weng,et al.  Profiling of differentially expressed genes in hepatopancreas of white spot syndrome virus-resistant shrimp (Litopenaeus vannamei) by suppression subtractive hybridisation. , 2007, Fish & shellfish immunology.

[11]  Robert W Chapman,et al.  Insights into the immune transcriptome of the shrimp Litopenaeus vannamei: tissue-specific expression profiles and transcriptomic responses to immune challenge. , 2007, Physiological genomics.

[12]  B. Buddle,et al.  Differences of gene expression in bovine alveolar macrophages infected with virulent and attenuated isogenic strains of Mycobacterium bovis. , 2006, International immunopharmacology.

[13]  R. Dutch,et al.  Cathepsin L Is Involved in Proteolytic Processing of the Hendra Virus Fusion Protein , 2005, Journal of Virology.

[14]  W. Terra,et al.  The cathepsin L-like proteinases from the midgut of Tenebrio molitor larvae: sequence, properties, immunocytochemical localization and function. , 2005, Insect biochemistry and molecular biology.

[15]  H. Volk,et al.  The expression of legumain, an asparaginyl endopeptidase that controls antigen processing, is reduced in endotoxin-tolerant monocytes , 2005, Genes and Immunity.

[16]  R. Maizels,et al.  Bm-CPI-2, a cystatin from Brugia malayi nematode parasites, differs from Caenorhabditis elegans cystatins in a specific site mediating inhibition of the antigen-processing enzyme AEP. , 2005, Molecular and biochemical parasitology.

[17]  R. Arroyo,et al.  Two novel asparaginyl endopeptidase-like cysteine proteinases from the protist Trichomonas vaginalis: their evolutionary relationship within the clan CD cysteine proteinases. , 2004, Gene.

[18]  D. Brömme,et al.  Thiol-dependent cathepsins: pathophysiological implications and recent advances in inhibitor design. , 2002, Current pharmaceutical design.

[19]  M. Sajid,et al.  Cysteine proteases of parasitic organisms. , 2002, Molecular and biochemical parasitology.

[20]  N. Rawlings,et al.  Evolutionary Lines of Cysteine Peptidases , 2001, Biological chemistry.

[21]  A. Barrett,et al.  Activation of human prolegumain by cleavage at a C-terminal asparagine residue. , 2000, Biochemical Journal.

[22]  H. Ploegh Viral strategies of immune evasion. , 1998, Science.

[23]  M. Scott,et al.  The Role of Proteolysis in the Processing and Assembly of 11S Seed Globulins , 1998, Plant Cell.

[24]  D. Turk,et al.  Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. , 1997, Biological chemistry.

[25]  V. Turk,et al.  The preparation of catalytically active human cathepsin B from its precursor expressed in Escherichia coli in the form of inclusion bodies. , 1995, European journal of biochemistry.

[26]  K. Karrer,et al.  Two distinct gene subfamilies within the family of cysteine protease genes. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[27]  M. Nishimura,et al.  A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms , 1991, FEBS letters.

[28]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[29]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[30]  Alberto Smith,et al.  Legumain and cathepsin-L expression in human unstable carotid plaque. , 2010, Atherosclerosis.

[31]  M. Lavric,et al.  Gene expression modulation in chicken macrophages exposed to Mycoplasma synoviae or Escherichia coli. , 2008, Veterinary microbiology.

[32]  Kejin Hu,et al.  Food digestion by cathepsin L and digestion-related rapid cell differentiation in shrimp hepatopancreas. , 2007, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.

[33]  D. Sellos,et al.  Cloning and expression of cathepsinl-like proteinases in the hepatopancreas of the shrimpPenaeus vannamei during the intermolt cycle , 2006, Journal of Comparative Physiology B.

[34]  Xiao-Fan Zhao,et al.  Expression of the Helicoverpa cathepsin B-like proteinase during embryonic development. , 2005, Archives of insect biochemistry and physiology.