Two novel asparaginyl endopeptidase-like cysteine proteinases from the protist Trichomonas vaginalis: their evolutionary relationship within the clan CD cysteine proteinases
- 11 June 2004
- Vol. 335, 25-35
- https://doi.org/10.1016/j.gene.2004.03.002
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Cysteine proteases of parasitic organismsPublished by Elsevier ,2002
- Soluble GPI8 restores glycosylphosphatidylinositol anchoring in a trypanosome cell-free system depleted of lumenal endoplasmic reticulum proteinsBiochemical Journal, 2000
- CP30, a Cysteine Proteinase Involved in Trichomonas vaginalis CytoadherenceInfection and Immunity, 2000
- Cloning, Isolation, and Characterization of Mammalian Legumain, an Asparaginyl EndopeptidaseJournal of Biological Chemistry, 1997
- Quartet Puzzling: A Quartet Maximum-Likelihood Method for Reconstructing Tree TopologiesMolecular Biology and Evolution, 1996
- A Putative Vacuolar Processing Protease Is Regulated by Ethylene and also during Fruit Ripening in Citrus FruitPlant Physiology, 1995
- Asparaginyl endopeptidase activity in adultSchistosoma mansoniParasitology, 1995
- Identification and molecular cloning of four cysteine proteinase genes from the pathogenic protozoon Trichomonas vaginalisMicrobiology, 1994
- A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature formsFEBS Letters, 1991
- Characterization ofTrichomonas vaginalishaemolysisParasitology, 1990