Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain.
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Cysteine Proteases: Modes of Activation and Future Prospects as Pharmacological TargetsVinyl Sulfones as Antiparasitic Agents and a Structural Basis for Drug DesignStructures of Falcipain-2 and Falcipain-3 Bound to Small Molecule Inhibitors: Implications for Substrate Specificity ‡Biochemical properties of a novel cysteine protease of Plasmodium vivax, vivapain-4The Ionic and hydrophobic interactions are required for the auto activation of cysteine proteases of Plasmodium falciparumStructural basis for unique mechanisms of folding and hemoglobin binding by a malarial proteaseCritical role of amino acid 23 in mediating activity and specificity of vinckepain-2, a papain-family cysteine protease of rodent malaria parasites.Cross-talk between malarial cysteine proteases and falstatin: the BC loop as a hot-spot target.Hemoglobin cleavage site-specificity of the Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3.Regulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparumThe Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif.Centenary celebrations article: Cysteine proteases of human malaria parasites.Structure-function of falcipains: malarial cysteine proteases.Whole-genome analysis reveals molecular innovations and evolutionary transitions in chromalveolate species.Efficient expression systems for cysteine proteases of malaria parasites: too good to be true?Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli.Propeptides as modulators of functional activity of proteases.Cryptopain-1, a cysteine protease of Cryptosporidium parvum, does not require the pro-domain for folding.Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli.Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax.Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2.Structural and functional characterization of Falcipain-2, a hemoglobinase from the malarial parasite Plasmodium falciparum.Plasmodium falciparum Falcipain-2a Polymorphisms in Southeast Asia and Their Association with Artemisinin Resistance.Cysteine proteases in protozoan parasites
P2860
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P2860
Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain.
description
2002 nî lūn-bûn
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name
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@en
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@nl
type
label
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@en
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@nl
prefLabel
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@en
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@nl
P2860
P356
P1476
Folding of the Plasmodium falc ...... peptide and not the prodomain.
@en
P2093
Bhaskar R Shenai
Puran S Sijwali
P2860
P304
14910-14915
P356
10.1074/JBC.M109680200
P407
P577
2002-02-04T00:00:00Z