Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum - Test2 - elhamkhani - TriplyDB

Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum

Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum

http://www.wikidata.org/entity/Q24597864

about

Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides Recombinant Plasmepsin 1 from the Human Malaria Parasite Plasmodium falciparum : Enzymatic Characterization, Active Site Inhibitor Design, and Structural Analysis Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum Conformational switching in an aspartic proteinase The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes Disulfide linkages in Plasmodium falciparum plasmepsin-i are essential elements for its processing activity and multi-milligram recombinant production yield Constraining cyclic peptides to mimic protein structure motifs.Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite Computational analysis of plasmepsin IV bound to an allophenylnorstatine inhibitor.Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations.Integration and mining of malaria molecular, functional and pharmacological data: how far are we from a chemogenomic knowledge space?Active site contribution to specificity of the aspartic proteases plasmepsins I and II.Characterisation of hydrazides and hydrazine derivatives as novel aspartic protease inhibitors.Identification of Tight-Binding Plasmepsin II and Falcipain 2 Inhibitors in Aqueous Extracts of Marine Invertebrates by the Combination of Enzymatic and Interaction-Based Assays.Antimalarial synergy of cysteine and aspartic protease inhibitors.Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursors Folding funnels and binding mechanisms.Computational perspectives into plasmepsins structure-function relationship: implications to inhibitors design.New class of small nonpeptidyl compounds blocks Plasmodium falciparum development in vitro by inhibiting plasmepsins Crystallization and preliminary X-ray analysis of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae Emerging targets for antimalarial drugs.Structural studies of vacuolar plasmepsins Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin.Inhibitory effects of pepstatin A and mefloquine on the growth of Babesia parasites Comparative genome-wide analysis and evolutionary history of haemoglobin-processing and haem detoxification enzymes in malarial parasites Molecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani.Proteases of malaria parasites: new targets for chemotherapy.Proteases as regulators of pathogenesis: examples from the Apicomplexa.Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum.A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum.Expression and characterisation of plasmepsin I from Plasmodium falciparum.New directions for protease inhibitors directed drug discovery.Novel Plasmodium falciparum metabolic network reconstruction identifies shifts associated with clinical antimalarial resistance.Exploring the subsite specificity of Schistosoma mansoni aspartyl hemoglobinase through comparative molecular modelling.Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors.Flap flexibility amongst plasmepsins I, II, III, IV, and V: Sequence, structural, and molecular dynamics analyses.An Ab Initio Method for Designing Multi-Target Specific Pharmacophores using Complementary Interaction Field of Aspartic Proteases.Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum.

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P2860

Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum

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1996 nî lūn-bûn

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Structure and inhibition of pl ...... yme from Plasmodium falciparum

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P2860

Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design

Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain

Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution

High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme

On the size of the active site in proteases. I. Papain

Pepstatin, a new pepsin inhibitor produced by Actinomycetes

The structure and function of the aspartic proteinases

Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer

The plasmodium digestive vacuole: metabolic headquarters and choice drug target.

Order and specificity of the Plasmodium falciparum hemoglobin degradation pathway

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