Recombinant Leishmania surface glycoprotein GP63 is secreted in the baculovirus expression system as a latent metalloproteinase
- 30 November 1993
- Vol. 134 (1) , 75-81
- https://doi.org/10.1016/0378-1119(93)90176-4
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Construction of an improved baculovirus insecticide containing an insect-specific toxin geneNature, 1991
- Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidaseMolecular and Biochemical Parasitology, 1989
- Species‐specific variation in signal peptide design Implications for protein secretion in foreign hostsFEBS Letters, 1989
- CELL-SURFACE ANCHORING OF PROTEINS VIA GLYCOSYL-PHOSPHATIDYLINOSITOL STRUCTURESAnnual Review of Biochemistry, 1988
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- The promastigote surface protease of leishmaniaParasitology Today, 1987
- Baculovirus Expression Vectors: the Requirements for High Level Expression of Proteins, Including GlycoproteinsJournal of General Virology, 1987
- Towards a comparative anatomy of N-terminal topogenic protein sequencesJournal of Molecular Biology, 1986
- Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomesCell, 1986
- A common major surface antigen on amastigotes and promastigotes of Leishmania species.The Journal of Experimental Medicine, 1985