Folding of the Plasmodium falciparum Cysteine Protease Falcipain-2 Is Mediated by a Chaperone-like Peptide and Not the Prodomain
Open Access
- 1 April 2002
- journal article
- Published by Elsevier
- Vol. 277 (17) , 14910-14915
- https://doi.org/10.1074/jbc.m109680200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Systematic Optimization of Expression and Refolding of the Plasmodium falciparum Cysteine Protease Falcipain-2Protein Expression and Purification, 2001
- Folding of Newly Translated Proteins In Vivo: The Role of Molecular ChaperonesAnnual Review of Biochemistry, 2001
- Expression of rat chymotrypsinogen in yeast: a study on the structural and functional significance of the chymotrypsinogen propeptideFEBS Letters, 1996
- Functional Analysis of the Propeptide of Subtilisin E as an Intramolecular Chaperone for Protein FoldingPublished by Elsevier ,1995
- The Propeptide Is Nonessential for the Expression of Human Cathepsin DPublished by Elsevier ,1995
- Alignment/Phylogeny of the Papain Superfamily of Cysteine ProteasesJournal of Molecular Biology, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Introduction of a cysteine protease active site into trypsinBiochemistry, 1989
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976