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Plasmepsin I
Disulfide Linkages in Plasmodium Falciparum Plasmepsin-I Are Essential Elements for Its Processing Activity and Multi-Milligram Recombinant Production Yield
Data-Mining Approaches Reveal Hidden Families of Proteases in The
Understanding the Structural Basis of Substrate Recognition By
Hemoglobin-Degrading, Aspartic Proteases of Blood-Feeding Parasites SUBSTRATE SPECIFICITY REVEALED by HOMOLOGY MODELS*
Interactions of Ganoderiol-F with Aspartic Proteases of Hiv and Plasmepsin for Anti-Hiv and Anti-Malaria Discovery
Research Journal of Pharmaceutical, Biological and Chemical Sciences
Computational Analysis of Plasmepsin IV Bound to an Allophenylnorstatine Inhibitor
Structure-Assisted Design of Drugs Towards HIV-1 and Malaria Targets
Peptidomimetic Plasmepsin Inhibitors with Potent Anti-Malarial Activity
High Level Expression and Characterisation of Plasmepsin II, an Aspartic Proteinase from Plasmodium Falciparum
All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
Biochemical and Cellular Characterisation of the Plasmodium Falciparum M1 Alanyl Aminopeptidase (Pfm1aap) and M17 Leucyl Aminope
Modenza: Accurate Identification of Metabolic Enzymes Using Function
Identification and Characterization of Falcilysin, a Metallopeptidase Involved in Hemoglobin Catabolism Within the Malaria Parasite Plasmodium Falciparum*
Ahmad Haniff Jaafar
Trafficked Proteins—Druggable in Plasmodium Falciparum?
Plasmepsin Inhibitors: A
A Unique Structural and Dynamic Feature of Aspartic Protease
Top View
Computational Study of Triterpenoids of Ganoderma Lucidum with Aspartic Protease Enzymes for Discovering HIV-1 and Plasmepsin Inhibitors
Plasmodium Falciparum Plasmepsins IX and X: Structure- Function Analysis and the Discovery of New Lead Antimalarial Drugs
ALEXANDER WLODAWER, Ph.D
Structural Investigation and In-Silico Characterization of Plasmepsins from Plasmodium Falciparum Divya N
WO 2016/197190 Al 15 December 2016 (15.12.2016) P O P C T
Determination of Ligand Position in Aspartic Proteases by Correlating Tanimoto Coefficient and Binding Affinity with Root Mean Square Deviation
Biochemical and Structural Insi
Structure and Inhibition of Plasmepsin II, a Hemoglobin-Degrading Enzyme
Proceedings of the International Beilstein Workshop 2002
Protein Science ~1999!, 8:2001–2009
A Distinct Member of the Aspartic Proteinase Gene Family from the Human Malaria Parasite Plasmodium Falciparum
Plasmodium Falciparum Ensures Its Amino Acid Supply with Multiple Acquisition Pathways and Redundant Proteolytic Enzyme Systems
Crystal Structures of the Free and Inhibited Forms of Plasmepsin I (PMI) from Plasmodium Falciparum
Intramembrane Proteolytic Cleavage by Human Signal Peptide Peptidase Like 3 and Malaria Signal Peptide Peptidase
Digestomics: Elucidating Protein Catabolism Through the Quantitative Mapping of in Vivo, Endogenous Peptides to the Proteome at an Amino Acid Level of Resolution
S41598-020-59477-3.Pdf
Comparative Genome-Wide Analysis and Evolutionary History Of
CHARACTERIZATION of NOVEL PLASMEPSINS from the MALARIA PARASITE Plasmodium Falcipaurm