On the public citation graph
Identification of Novel Malarial Cysteine Protease Inhibitors Using Structure-Based Virtual Screening of a Focused Cysteine Protease Inhibitor Library
0 signed · 138 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/cmdc.200800050openalex-snapshot
Nonpeptidic Vinyl and Allyl Phosphonates as Falcipain‐2 Inhibitors
inferredcites →https://doi.org/10.1002/cmdc.201000265openalex-snapshot
α‐Ketoheterocycles as Inhibitors of Leishmania mexicana Cysteine Protease CPB
inferredcites →https://doi.org/10.1007/bf00554788openalex-snapshot
Estimating the hessian for gradient-type geometry optimizations
inferredcites →https://doi.org/10.1016/j.bbrc.2004.08.130openalex-snapshot
Homology modeling and mutagenesis analyses of Plasmodium falciparum falcipain 2A: implications for rational drug design
inferredcites →https://doi.org/10.1016/j.bmcl.2006.11.044openalex-snapshot
A generally applicable method for assessing the electrophilicity and reactivity of diverse nitrile-containing compounds
inferredcites →https://doi.org/10.1016/j.bmcl.2007.12.047openalex-snapshot
The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K
inferredcites →https://doi.org/10.1016/j.bmcl.2008.05.068openalex-snapshot
Design and synthesis of novel 2-pyridone peptidomimetic falcipain 2/3 inhibitors
inferredcites →https://doi.org/10.1016/j.cbpa.2004.06.002openalex-snapshot
Target-biased scoring approaches and expert systems in structure-based virtual screening
inferredcites →https://doi.org/10.1016/j.cbpa.2004.06.008openalex-snapshot
Integrating virtual screening in lead discovery
inferredcites →https://doi.org/10.1016/j.molbiopara.2006.06.013openalex-snapshot
Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum
inferredcites →https://doi.org/10.1016/s0009-2614(99)00325-5openalex-snapshot
A direct evaluation of regional Fukui functions in molecules
inferredcites →https://doi.org/10.1016/s0014-5793(98)00964-8openalex-snapshot
Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions1
inferredcites →https://doi.org/10.1016/s0960-894x(03)00304-4openalex-snapshot
3,4-Disubstituted azetidinones as selective inhibitors of the cysteine protease cathepsin K. Exploring P2 elements for selectivity
inferredcites →https://doi.org/10.1016/s0968-0896(99)00007-3openalex-snapshot
Cyclopropenone-containing cysteine proteinase inhibitors. Synthesis and enzyme inhibitory activities
inferredcites →https://doi.org/10.1016/s0968-0896(99)00011-5openalex-snapshot
Potent dipeptidylketone inhibitors of the cysteine protease cathepsin K
inferredcites →https://doi.org/10.1016/s0969-2126(00)00173-8openalex-snapshot
A target within the target: probing cruzain’s P1′ site to define structural determinants for the Chagas’ disease protease
inferredcites →https://doi.org/10.1021/ci1000373openalex-snapshot
Targeting the BH3 Domain Mediated Protein−Protein Interaction of Bcl-xL through Virtual Screening
inferredcites →https://doi.org/10.1021/ci800386vopenalex-snapshot
Hybrid Structure-Based Virtual Screening Protocol for the Identification of Novel BACE1 Inhibitors
inferredcites →https://doi.org/10.1021/jm00017a002openalex-snapshot
Vinyl Sulfones as Mechanism-Based Cysteine Protease Inhibitors
inferredcites →https://doi.org/10.1021/jm00026a010openalex-snapshot
In Vitro Antimalarial Activity of Chalcones and Their Derivatives
inferredcites →https://doi.org/10.1021/jm000320topenalex-snapshot
Cyclic Ketone Inhibitors of the Cysteine Protease Cathepsin K
inferredcites →https://doi.org/10.1021/jm00074a031openalex-snapshot
Peptide .alpha.-keto ester, .alpha.-keto amide, and .alpha.-keto acid inhibitors of calpains and other cysteine proteases
inferredcites →https://doi.org/10.1021/jm001044lopenalex-snapshot
Protein-Based Virtual Screening of Chemical Databases. 1. Evaluation of Different Docking/Scoring Combinations
inferredcites →https://doi.org/10.1021/jm0493717openalex-snapshot
Identification of Novel Parasitic Cysteine Protease Inhibitors Using Virtual Screening. 1. The ChemBridge Database
inferredcites →https://doi.org/10.1021/jm0505765openalex-snapshot
Identification of Novel Parasitic Cysteine Protease Inhibitors by Use of Virtual Screening. 2. The Available Chemical Directory
inferredcites →https://doi.org/10.1021/jm0608356openalex-snapshot
Benchmarking Sets for Molecular Docking
inferredcites →https://doi.org/10.1021/jm100556bopenalex-snapshot
Falcipain Inhibitors: Optimization Studies of the 2-Pyrimidinecarbonitrile Lead Series
inferredcites →https://doi.org/10.1021/jm8008597openalex-snapshot
Covalent Modifiers: An Orthogonal Approach to Drug Design
inferredcites →https://doi.org/10.1021/jm8013663openalex-snapshot
Structures of Falcipain-2 and Falcipain-3 Bound to Small Molecule Inhibitors: Implications for Substrate Specificity
inferredcites →https://doi.org/10.1021/jm801622xopenalex-snapshot
Identification of Novel Falcipain-2 Inhibitors as Potential Antimalarial Agents through Structure-Based Virtual Screening
inferredcites →https://doi.org/10.1021/jm901633vopenalex-snapshot
Nonpeptidic Tetrafluorophenoxymethyl Ketone Cruzain Inhibitors as Promising New Leads for Chagas Disease Chemotherapy
inferredcites →https://doi.org/10.1021/jm970266popenalex-snapshot
Synthesis and Antimalarial Effects of Phenothiazine Inhibitors of a Plasmodium falciparum Cysteine Protease
inferredcites →https://doi.org/10.1021/jm980249fopenalex-snapshot
Use of Papain as a Model for the Structure-Based Design of Cathepsin K Inhibitors: Crystal Structures of Two Papain−Inhibitor Complexes Demonstrate Binding to S‘-Subsites
inferredcites →https://doi.org/10.1021/jp036416ropenalex-snapshot
Condensation of Frontier Molecular Orbital Fukui Functions
inferredcites →https://doi.org/10.1021/tx00046a001openalex-snapshot
Quantitative Structure-Activity Relationships Based on Computer Calculated Parameters for the Overall Rate of Glutathione S-Transferase Catalyzed Conjugation of a Series of Fluoronitrobenzenes
inferredcites →https://doi.org/10.1038/415680aopenalex-snapshot
The economic and social burden of malaria
inferredcites →https://doi.org/10.1038/nature09099openalex-snapshot
Chemical genetics of Plasmodium falciparum
inferredcites →https://doi.org/10.1038/nature09107openalex-snapshot
Thousands of chemical starting points for antimalarial lead identification
inferredcites →https://doi.org/10.1042/0264-6021:3600481openalex-snapshot
Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3
inferredcites →https://doi.org/10.1042/bj20060422openalex-snapshot
Substrate mapping and inhibitor profiling of falcipain-2, falcipain-3 and berghepain-2: implications for peptidase anti-malarial drug discovery
inferredcites →https://doi.org/10.1073/pnas.0307720101openalex-snapshot
Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
inferredcites →https://doi.org/10.1073/pnas.0402738101openalex-snapshot
Plasmodium falciparum cysteine protease falcipain-1 is not essential in erythrocytic stage malaria parasites
inferredcites →https://doi.org/10.1074/jbc.m004459200openalex-snapshot
Characterization of Native and Recombinant Falcipain-2, a Principal Trophozoite Cysteine Protease and Essential Hemoglobinase ofPlasmodium falciparum
inferredcites →https://doi.org/10.1074/jbc.m109.014340openalex-snapshot
Vinyl Sulfones as Antiparasitic Agents and a Structural Basis for Drug Design
inferredcites →https://doi.org/10.1074/jbc.m603776200openalex-snapshot
Structural and Functional Characterization of Falcipain-2, a Hemoglobinase from the Malarial Parasite Plasmodium falciparum
inferredcites →https://doi.org/10.1093/bioinformatics/16.6.566openalex-snapshot
DaliLite workbench for protein structure comparison
inferredcites →https://doi.org/10.1103/physrevb.37.785openalex-snapshot
Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
inferredcites →https://doi.org/10.1110/ps.0228103openalex-snapshot
Probing the structure of falcipain‐3, a cysteine protease from Plasmodium falciparum: Comparative protein modeling and docking studies
inferredcites →https://doi.org/10.1111/j.1365-2958.2004.04108.xopenalex-snapshot
Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth
inferredcites →https://doi.org/10.1126/science.1077426openalex-snapshot
A Role for the Protease Falcipain 1 in Host Cell Invasion by the Human Malaria Parasite
inferredcites →https://doi.org/10.1128/aac.40.7.1600openalex-snapshot
Antimalarial effects of vinyl sulfone cysteine proteinase inhibitors
inferredcites →https://doi.org/10.1128/aac.47.1.154-160.2003openalex-snapshot
Structure-Activity Relationships for Inhibition of Cysteine Protease Activity and Development of Plasmodium falciparum by Peptidyl Vinyl Sulfones
inferredcites →https://doi.org/10.1128/aac.47.12.3810-3814.2003openalex-snapshot
Antimalarial Activities of Novel SyntheticCysteine ProteaseInhibitors
inferredcites →https://doi.org/10.1128/aem.57.7.2101-2103.1991openalex-snapshot
Cytotoxicity of T-2 toxin and its metabolites determined with the neutral red cell viability assay
inferredcites →https://doi.org/10.1172/jci113766openalex-snapshot
A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum.
inferredcites →https://doi.org/10.1172/jci115456openalex-snapshot
Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase.
inferredcites →https://doi.org/10.1172/jci116262openalex-snapshot
Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria.
inferredcites →https://doi.org/10.1182/blood.v87.10.4448.bloodjournal87104448openalex-snapshot
Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites
inferredcites →https://doi.org/10.1371/journal.pone.0005156openalex-snapshot
Hemoglobin Cleavage Site-Specificity of the Plasmodium falciparum Cysteine Proteases Falcipain-2 and Falcipain-3
inferredcites →https://doi.org/10.2174/092986706776055733openalex-snapshot
Thiol Proteases: Inhibitors and Potential Therapeutic Targets
inferredcites →https://doi.org/10.2174/092986707780090927openalex-snapshot
Recent Advances in Antimalarial Compounds and their Patents
inferredcites →https://doi.org/10.2174/1381612023394197openalex-snapshot
Cysteine Proteases of Malaria Parasites: Targets for Chemotherapy
inferredcites →https://doi.org/10.2174/157340910790980142openalex-snapshot
Computational Approaches for the Discovery of Cysteine Protease Inhibitors Against Malaria and SARS
inferredcites →https://doi.org/10.2307/3280287openalex-snapshot
Synchronization of Plasmodium falciparum Erythrocytic Stages in Culture
inferredcites →https://doi.org/10.3390/molecules14114570openalex-snapshot
The Trypanocidal Activity of Naphthoquinones: A Review
inferredcites →https://doi.org/10.4155/fmc.10.21openalex-snapshot
Strategies for Discovering and Derisking Covalent, Irreversible Enzyme Inhibitors
inferredcites →https://doi.org/10.4269/ajtmh.2004.71.179openalex-snapshot
ANTIMALARIAL DRUG RESISTANCE, ARTEMISININ-BASED COMBINATION THERAPY, AND THE CONTRIBUTION OF MODELING TO ELUCIDATING POLICY CHOICES
inferredcites →https://doi.org/10.4269/ajtmh.2007.77.181openalex-snapshot
Artemisinin-Based Combination Treatment of Falciparum Malaria
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/ange.201610042openalex-snapshot
Highly Site Selective Formal [5+2] and [4+2] Annulations of Isoxazoles with Heterosubstituted Alkynes by Platinum Catalysis: Rapid Access to Functionalized 1,3‐Oxazepines and 2,5‐Dihydropyridines
inferred← citeshttps://doi.org/10.1002/anie.201610042openalex-snapshot
Highly Site Selective Formal [5+2] and [4+2] Annulations of Isoxazoles with Heterosubstituted Alkynes by Platinum Catalysis: Rapid Access to Functionalized 1,3‐Oxazepines and 2,5‐Dihydropyridines
inferred← citeshttps://doi.org/10.1002/cbdv.201700037openalex-snapshot
Design, Synthesis, and Biological Evaluation of Peptidomimetic N‐Substituted Cbz‐4‐Hyp‐Hpa‐Amides as Novel Inhibitors of Plasmodium falciparum
inferred← citeshttps://doi.org/10.1002/chem.201904139openalex-snapshot
α‐Unsaturated 3‐Amino‐1‐carboxymethyl‐β‐lactams as Bacterial PBP Inhibitors: Synthesis and Biochemical Assessment
inferred← citeshttps://doi.org/10.1002/minf.201500113openalex-snapshot
Machine Learning Estimation of Atom Condensed Fukui Functions
inferred← citeshttps://doi.org/10.1002/minf.202000028openalex-snapshot
Rapid Identification of Potential Inhibitors of SARS‐CoV‐2 Main Protease by Deep Docking of 1.3 Billion Compounds
inferred← citeshttps://doi.org/10.1002/qua.24481openalex-snapshot
Jaguar: A high‐performance quantum chemistry software program with strengths in life and materials sciences
inferred← citeshttps://doi.org/10.1002/wcms.1535openalex-snapshot
Expanding the boundaries of ligand–target modeling by exascale calculations
inferred← citeshttps://doi.org/10.1007/978-94-007-4497-4_7openalex-snapshot
Advanced Screening to Identify Novel Pesticides
inferred← citeshttps://doi.org/10.1007/s00894-014-2386-2openalex-snapshot
Methyl-methoxylpyrrolinone and flavinium nucleus binding signatures on falcipain-2 active site
inferred← citeshttps://doi.org/10.1007/s10822-013-9685-zopenalex-snapshot
Novel anti-Plasmodial hits identified by virtual screening of the ZINC database
inferred← citeshttps://doi.org/10.1007/s10822-014-9789-0openalex-snapshot
Creating and virtually screening databases of fluorescently-labelled compounds for the discovery of target-specific molecular probes
inferred← citeshttps://doi.org/10.1007/s11172-018-2073-zopenalex-snapshot
New quinoline- and isoquinoline-based multicomponent methods for the synthesis of 1,1(3,3)-dicyanotetrahydrobenzoindolizines
inferred← citeshttps://doi.org/10.1016/b978-0-08-101210-9.00008-1openalex-snapshot
Falcipains as drug targets in antimalarial therapy
inferred← citeshttps://doi.org/10.1016/j.bbagen.2018.09.015openalex-snapshot
Identification of (4-(9H-fluoren-9-yl) piperazin-1-yl) methanone derivatives as falcipain 2 inhibitors active against Plasmodium falciparum cultures
inferred← citeshttps://doi.org/10.1016/j.bmc.2013.04.047openalex-snapshot
Falcipain-2 inhibition by suramin and suramin analogues
inferred← citeshttps://doi.org/10.1016/j.bmc.2017.10.017openalex-snapshot
Discovery of new antimalarial agents: Second-generation dual inhibitors against FP-2 and PfDHFR via fragments assembely
inferred← citeshttps://doi.org/10.1016/j.bmcl.2014.01.062openalex-snapshot
Synthesis, biological evaluation, hydration site thermodynamics, and chemical reactivity analysis of α-keto substituted peptidomimetics for the inhibition of Plasmodium falciparum
inferred← citeshttps://doi.org/10.1016/j.cdc.2020.100524openalex-snapshot
Synthesis and characterization of indolizine and 5,6-benzo-fused indolizine derivatives with their pharmacological applications
inferred← citeshttps://doi.org/10.1016/j.ejmech.2014.11.061openalex-snapshot
Synthesis and structure–activity-relationship studies of thiazolidinediones as antiplasmodial inhibitors of the Plasmodium falciparum cysteine protease falcipain-2
inferred← citeshttps://doi.org/10.1016/j.ejmech.2019.111983openalex-snapshot
Current progress in antimalarial pharmacotherapy and multi-target drug discovery
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e25077openalex-snapshot
Biological evaluation of novel side chain containing CQTrICh-analogs as antimalarials and their development as PfCDPK1 kinase inhibitors
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.142817openalex-snapshot
Falcipain-2: A review on structurally diverse non-peptide inhibitors
inferred← citeshttps://doi.org/10.1016/j.jmgm.2017.05.014openalex-snapshot
Identification of potent inhibitors of DNA methyltransferase 1 (DNMT1) through a pharmacophore-based virtual screening approach
inferred← citeshttps://doi.org/10.1016/j.jpba.2016.02.056openalex-snapshot
Serum albumin as a probe for testing the selectivity of irreversible cysteine protease inhibitors: The case of vinyl sulfones
inferred← citeshttps://doi.org/10.1016/j.ymeth.2014.07.007openalex-snapshot
Hierarchical virtual screening approaches in small molecule drug discovery
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.5b01013openalex-snapshot
Cyanohydrin as an Anchoring Group for Potent and Selective Inhibitors of Enterovirus 71 3C Protease
inferred← citeshttps://doi.org/10.1021/acs.joc.2c02729openalex-snapshot
Switchable Regioselective 7-endo or 6-exo Iodocyclization of O-Homoallyl Benzimidates
inferred← citeshttps://doi.org/10.1021/acs.jproteome.0c00836openalex-snapshot
Structure-Based Screening to Discover New Inhibitors for Papain-like Proteinase of SARS-CoV-2: An In Silico Study
inferred← citeshttps://doi.org/10.1021/acs.orglett.5b03535openalex-snapshot
Total Synthesis of K777: Successful Application of Transition-Metal-Catalyzed Alkyne Hydrothiolation toward the Modular Synthesis of a Potent Cysteine Protease Inhibitor
inferred← citeshttps://doi.org/10.1021/acsinfecdis.5b00093openalex-snapshot
Computer-Aided Drug Discovery Approaches against the Tropical Infectious Diseases Malaria, Tuberculosis, Trypanosomiasis, and Leishmaniasis
inferred← citeshttps://doi.org/10.1021/ci2005516openalex-snapshot
Computer-Aided Drug Design of Falcipain Inhibitors: Virtual Screening, Structure–Activity Relationships, Hydration Site Thermodynamics, and Reactivity Analysis
inferred← citeshttps://doi.org/10.1021/jm501439wopenalex-snapshot
Synthesis of Gallinamide A Analogues as Potent Falcipain Inhibitors and Antimalarials
inferred← citeshttps://doi.org/10.1038/s41598-017-16887-0openalex-snapshot
A Copper-Catalyzed Tandem Cyclization Reaction of Aminoalkynes with Alkynes for the Construction of Tetrahydropyrrolo[1,2-a]quinolines Scaffold
inferred← citeshttps://doi.org/10.1038/srep23690openalex-snapshot
Structure Based Docking and Molecular Dynamic Studies of Plasmodial Cysteine Proteases against a South African Natural Compound and its Analogs
inferred← citeshttps://doi.org/10.1039/9781788010016-00067openalex-snapshot
Molecular Mechanisms of Drug Action: X-ray Crystallography at the Basis of Structure-based and Ligand-based Drug Design
inferred← citeshttps://doi.org/10.1039/c1md00129aopenalex-snapshot
Design, synthesis and biological evaluation of novel benzothiazole and triazole analogs as falcipain inhibitors
inferred← citeshttps://doi.org/10.1039/c3mb70105kopenalex-snapshot
Structural features of falcipain-3 inhibitors: an in silico study
inferred← citeshttps://doi.org/10.1039/c7ob01895aopenalex-snapshot
Recent advances in transition-metal-catalyzed reactions of alkynes with isoxazoles
inferred← citeshttps://doi.org/10.1039/c9ra06571gopenalex-snapshot
Quinoline-triazole hybrids inhibit falcipain-2 and arrest the development of Plasmodium falciparum at the trophozoite stage
inferred← citeshttps://doi.org/10.1080/07391102.2014.924878openalex-snapshot
Dynamical footprint of falcipain-2 catalytic triad in hemoglobin-β-bound state
inferred← citeshttps://doi.org/10.1080/17460441.2016.1195945openalex-snapshot
Drug target identification in protozoan parasites
inferred← citeshttps://doi.org/10.1080/17568919.2025.2515819openalex-snapshot
Repurposing sulfonamide-scaffolds for enhanced and sustainable malaria therapy
inferred← citeshttps://doi.org/10.1111/cbdd.12621openalex-snapshot
Discovery of Novel Peptidomimetics as Irreversible CHIKV Ns P 2 Protease Inhibitors Using Quantum Mechanical‐Based Ligand Descriptors
inferred← citeshttps://doi.org/10.1111/cbdd.12968openalex-snapshot
Synthesis, antimalarial activity in vitro, and docking studies of novel neolignan derivatives
inferred← citeshttps://doi.org/10.1111/fcp.12974openalex-snapshot
Antimalarial activities of benzothiazole analogs: A systematic review
inferred← citeshttps://doi.org/10.1128/aac.00298-17openalex-snapshot
Structure of the Enterovirus 71 3C Protease in Complex with NK-1.8k and Indications for the Development of Antienterovirus Protease Inhibitor
inferred← citeshttps://doi.org/10.1186/1471-2164-12-s5-s9openalex-snapshot
Protease-associated cellular networks in malaria parasite Plasmodium falciparum
inferred← citeshttps://doi.org/10.1371/journal.pone.0075992openalex-snapshot
Ligand Pose and Orientational Sampling in Molecular Docking
inferred← citeshttps://doi.org/10.1515/psr-2018-0119openalex-snapshot
Case studies on computer-based identification of natural products as lead molecules
inferred← citeshttps://doi.org/10.1590/s0074-02762012000700001openalex-snapshot
New approaches in antimalarial drug discovery and development: a review
inferred← citeshttps://doi.org/10.21608/puj.2019.14599.1049openalex-snapshot
Expression of cysteine proteinases and cystatins in parasites and use of cysteine proteinase inhibitors in parasitic diseases. Part III: Protozoa (2): Plasmodium spp.
inferred← citeshttps://doi.org/10.2174/0929867311320250003openalex-snapshot
Development of Plasmodium falciparum Protease Inhibitors in the Past Decade (2002–2012)
inferred← citeshttps://doi.org/10.2174/0929867324666170810165302openalex-snapshot
Structure-based Approaches Targeting Parasite Cysteine Proteases
inferred← citeshttps://doi.org/10.2174/0929867327666200730215316openalex-snapshot
Falcipain-2 and Falcipain-3 Inhibitors as Promising Antimalarial Agents
inferred← citeshttps://doi.org/10.2174/0929867331666230913165219openalex-snapshot
Three Decades of Targeting Falcipains to Develop Antiplasmodial Agents: What have we Learned and What can be Done Next?
inferred← citeshttps://doi.org/10.2174/138161212799436386openalex-snapshot
From Laptop to Benchtop to Bedside: Structure-based Drug Design on Protein Targets
inferred← citeshttps://doi.org/10.2174/138920211797248565openalex-snapshot
Proteases in Malaria Parasites - A Phylogenomic Perspective
inferred← citeshttps://doi.org/10.2174/1389450117666161221122432openalex-snapshot
Targeting Cysteine Proteases from Plasmodium falciparum: A General Overview, Rational Drug Design and Computational Approaches for Drug Discovery
inferred← citeshttps://doi.org/10.2174/157489312803900965openalex-snapshot
Comparative Genomics and Systems Biology of Malaria Parasites Plasmodium
inferred← citeshttps://doi.org/10.3389/fchem.2019.00534openalex-snapshot
In silico Guided Drug Repurposing: Discovery of New Competitive and Non-competitive Inhibitors of Falcipain-2
inferred← citeshttps://doi.org/10.3389/fmicb.2019.00394openalex-snapshot
Structural Insights Into Key Plasmodium Proteases as Therapeutic Drug Targets
inferred← citeshttps://doi.org/10.3390/ijms12129236openalex-snapshot
3D QSAR Pharmacophore Modeling, in Silico Screening, and Density Functional Theory (DFT) Approaches for Identification of Human Chymase Inhibitors
inferred← citeshttps://doi.org/10.3390/molecules23051174openalex-snapshot
Synthesis and Evaluation of Antiplasmodial Activity of 2,2,2-Trifluoroethoxychalcones and 2-Fluoroethoxy Chalcones against Plasmodium falciparum in Culture
inferred← citeshttps://doi.org/10.3390/molecules25194485openalex-snapshot
A Novel Series of [1,2,4]Triazolo[4,3-a]Pyridine Sulfonamides as Potential Antimalarial Agents: In Silico Studies, Synthesis and In Vitro Evaluation
inferred← citeshttps://doi.org/10.3390/molecules27061845openalex-snapshot
QSAR and Molecular Docking Studies of Pyrimidine-Coumarin-Triazole Conjugates as Prospective Anti-Breast Cancer Agents
inferred← citeshttps://doi.org/10.3390/ph4050681openalex-snapshot
Expanding the Antimalarial Drug Arsenal—Now, But How?
inferred← citeshttps://doi.org/10.3390/scipharm89040044openalex-snapshot
Computer-Aided Design of Peptidomimetic Inhibitors of Falcipain-3: QSAR and Pharmacophore Models
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.