Affinage · Plasmodium

PF3D7_1443900

heat shock protein 90, putative

Audit flag: identity unverified
Annotated
2026-09-08
55 papers in source corpus 20 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1443900 (PfHsp90) is an essential cytosolic molecular chaperone of Plasmodium falciparum that supports parasite survival and stage progression, and its inhibition arrests development at the ring-to-trophozoite transition (PMID:12584193, PMID:15339915). It is an ATP-driven chaperone: its N-terminal domain binds and hydrolyzes ATP, displaying the highest ATPase activity of any known Hsp90 (~6-fold above human Hsp90), and a crystal structure of this domain in apo and ADP-bound states reveals the principal drug-binding pocket (PMID:14514358, PMID:20837488, PMID:20635416). PfHsp90 assembles into ~300 kDa hetero-oligomeric complexes together with PfHsp70, the co-chaperone PfHop (whose TPR2A motif binds the PfHsp90 C-terminus), PfPP5, PfFKBP35, and calcineurin, with the ATPase cycle tuned by co-chaperones — Pfp23 suppresses ATPase activity via defined contact residues, and an acetylation site overlapping the Aha1/p23 binding surface modulates complex integrity (PMID:15339915, PMID:11737864, PMID:15811524, PMID:15850699, PMID:22005844, PMID:20140477, PMID:26267894). Through these complexes PfHsp90 chaperones specific clients: it maintains the stability and histone deacetylase activity of PfSir2A, so its inhibition derepresses var genes and disrupts ribosomal silencing, and it promotes the hydrolytic activity of the 26S proteasome (PMID:36121150, PMID:38492573). PfHsp90 is a validated antimalarial target inhibited by geldanamycin and structurally diverse compounds acting at the N-terminal ATP site, with activity across blood and liver stages (PMID:12584193, PMID:26711771, PMID:29339390). Its distinctive extended charged linker further modulates ATPase activity and co-chaperone interaction, contributing to functional divergence from human Hsp90 (PMID:22315411).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1994 Medium

    Establishing the gene structure and expression pattern was the first step in defining PfHsp90 as a stress-responsive, developmentally expressed chaperone gene.

    Evidence Gene sequencing, Northern blot, and phylogenetic analysis of pfhsp86 across parasite stages

    PMID:3060854 PMID:7838176

    Open questions at the time
    • No protein-level function assayed
    • Charged-region and phylogenetic observations were sequence-based, not functional
  2. 2001 Medium

    Native co-IP identified PfPP5 as the first physical binding partner of PfHsp90, opening the question of what larger complex PfHsp90 forms.

    Evidence Co-immunoprecipitation of native proteins from parasite lysate

    PMID:11737864

    Open questions at the time
    • Single co-IP without reciprocal validation at the time
    • Functional consequence of the PfPP5 interaction not established
  3. 2003 High

    Fractionation and inhibitor studies defined PfHsp90 as an ATP-binding chaperone in a ~300 kDa PfHsp70-containing complex whose inhibition arrests specific developmental stages.

    Evidence Sedimentation/gel filtration, recombinant ATP-binding assay with geldanamycin competition, stage-specific growth assays

    PMID:12584193 PMID:14514358

    Open questions at the time
    • ATPase turnover (not just binding) not yet quantified
    • Client proteins unidentified
    • Mechanistic basis of stage arrest unclear
  4. 2004 High

    Co-IP mapping of the multi-chaperone complex linked PfHsp90 function to heat shock-dependent cytoprotection during febrile temperature stress.

    Evidence Co-immunoprecipitation identifying PfHsp70/PfPP5/tubulin, temperature-dependent geldanamycin disruption and stage-progression assays

    PMID:15339915

    Open questions at the time
    • Direct client substrates of the complex not defined
    • Role of tubulin association unresolved
  5. 2005 Medium

    Identification of calcineurin and PfFKBP35 (via TPR domain) as PfHsp90 associates expanded the interactome and revealed pharmacological synergy exploitable against the parasite.

    Evidence Native co-IP, TPR domain interaction analysis, geldanamycin/ascomycin synergy growth assays

    PMID:15811524 PMID:15850699

    Open questions at the time
    • Whether these interactions are direct or bridged by other co-chaperones not resolved
    • Functional output of calcineurin/FKBP35 association unclear
  6. 2010 High

    Enzymology, structure, and co-chaperone mapping converged to define the PfHsp90 ATPase cycle and its regulation, distinguishing it from human Hsp90.

    Evidence In vitro ATPase assays on recombinant protein, MS identification of an acetylation site in the Aha1/p23 domain, HDAC-inhibitor complex dissociation, N-domain crystal structure (apo/ADP), and Pfp23 mutagenesis defining binding residues

    PMID:20140477 PMID:20635416 PMID:20837488

    Open questions at the time
    • Full-length conformational cycle not structurally resolved
    • Enzyme(s) writing/erasing the acetylation mark not identified
  7. 2012 Medium

    Chimeric and mutagenesis studies showed the parasite-specific charged linker and defined residues tune PfHsp90 activity and inhibitor selectivity, motivating selective drug design.

    Evidence Yeast Hsp90 linker-swap chimeras with ATPase/biophysical readout; SPR and mutagenesis defining Arg98 for harmine selectivity

    PMID:22315411 PMID:22615284

    Open questions at the time
    • Linker function inferred through a heterologous yeast system rather than in parasite
    • Harmine affinity (Kd 40 µM) is modest
  8. 2015 High

    Subdomain mapping of PfHop and identification of ATP-site-binding chemotypes clarified how PfHsp90 is bridged to PfHsp70 and how it can be drugged at the N-terminus.

    Evidence Far Western, SPR, co-IP, split-GFP TPR mapping of PfHop; binding partner identification and structural analysis of imidazopyridazine compounds at the ATP site

    PMID:26267894 PMID:26711771

    Open questions at the time
    • Stoichiometry and dynamics of the PfHsp70–PfHop–PfHsp90 relay not defined
    • Whether ATP-site inhibitors act identically in vivo not fully resolved
  9. 2018 Medium

    Cross-stage inhibitor profiling established PfHsp90 as a target relevant beyond blood stages, including late liver-stage development.

    Evidence Target-based binding screens, liver- and blood-stage cell assays, time-course inhibition, SNX-0723/PIK-75 synergy

    PMID:29339390

    Open questions at the time
    • On-target versus off-target contribution of inhibitors not genetically confirmed
    • Liver-stage clients unidentified
  10. 2022 High

    Identification of PfSir2A as a stability-dependent client connected PfHsp90 chaperone function directly to epigenetic regulation of var genes and rRNA silencing.

    Evidence Co-IP of PfHsp90–PfSir2A, inhibitor-induced PfSir2A depletion (17-AAG, radicicol), HDAC activity assay, var gene expression analysis

    PMID:36121150

    Open questions at the time
    • Whether PfSir2A folding/maturation requires the full co-chaperone cycle not dissected
    • Breadth of epigenetic clients beyond PfSir2A unknown
  11. 2024 High

    Unbiased thermal proteome profiling expanded the PfHsp90 client set to the 26S proteasome, linking the chaperone to regulated protein degradation.

    Evidence Thermal proteome profiling under selective inhibition plus biochemical proteasome activity assays (BX-2819, XL888, Tropane 1)

    PMID:38492573

    Open questions at the time
    • Direct contact surface between PfHsp90 and proteasome subunits not mapped
    • Whether chaperoning is constitutive or stress-dependent unresolved
  12. 2025 Medium

    Detection of a selective C-terminal nucleotide-binding site indicated PfHsp90 has a second regulatory ATP interaction beyond the canonical N-domain.

    Evidence Affinity experiments with lysine-reactive nucleotide analog and ATP resin, limited proteolysis, mutagenesis on C-terminal construct

    PMID:40907219

    Open questions at the time
    • Functional/catalytic role of C-terminal nucleotide binding not established
    • No structure of the C-terminal site

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the PfHsp90 ATPase cycle and its full co-chaperone network select and mature the complete client repertoire in vivo remains to be defined.
  • Comprehensive client census is incomplete beyond PfSir2A and the proteasome
  • No full-length or complex structure defining the working conformational cycle
  • Genetic (rather than pharmacological) dissection of essentiality and client dependence is lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
26S PROTEASOME (CLIENT)CALCINEURIN (PP2B)PFFKBP35PFHOP (TPR2A BINDS PFHSP90 C-TERMINUS)PFHSP70 / PFHSP70-1PFP23 (CO-CHAPERONE, ATPASE SUPPRESSOR)PFPP5PFSIR2A (CLIENT)TUBULIN
Complex memberships
PfHsp90–26S proteasomePfHsp90–PfHsp70–PfHop–PfPP5–PfFKBP35–calcineurin assemblyPfHsp90–PfPP5 complexPfHsp90–PfSir2A complex~300 kDa PfHsp90 multi-chaperone complex (PfHsp90–PfHsp70–PfHop)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 PfHsp90 exists in ~300 kDa, 11S complexes that contain PfHsp70; geldanamycin (GA) inhibits PfHsp90 and arrests parasite development at ring-to-trophozoite transition; GA selectively inhibits PfHsp90 phosphorylation; pre-exposure to heat shock attenuates GA-mediated growth inhibition, consistent with a role for PfHsp90 in cytoprotection. Sedimentation analysis, size exclusion chromatography, homology modeling of GA-binding pocket, flow cytometry of parasite stages, metabolic labeling The Journal of biological chemistry High 12584193
2003 Recombinant PfHsp90 exhibits ATP-binding activity that is specifically inhibited by geldanamycin in vitro; mRNA is mainly expressed in ring and trophozoite stages but protein is present in all erythrocytic stages. Recombinant protein expression, in vitro ATP-binding assay, geldanamycin competition, stage-specific Western blot Malaria journal Medium 14514358
2004 PfHsp90 multi-chaperone complex (containing PfHsp70, PfPP5, and tubulin) mediates heat shock-dependent cytoprotection and growth promotion during febrile episodes; geldanamycin disrupts this complex and inhibits ring-to-trophozoite progression in a temperature-dependent manner. Co-immunoprecipitation identifying complex components, flow cytometry of parasite stage progression, geldanamycin-mediated complex disruption The Journal of biological chemistry High 15339915
2001 Native PfHsp90 co-immunoprecipitates with PfPP5 (a tetratricopeptide repeat-containing serine/threonine phosphatase) in P. falciparum parasite extracts, establishing PfPP5 as a binding partner of PfHsp90. Co-immunoprecipitation of native proteins from parasite lysate BMC microbiology Medium 11737864
2005 Plasmodial calcineurin (protein phosphatase 2B) associates with PfHsp90 in vivo; geldanamycin inhibits this association; PfFKBP35 associates with PfHsp90 via its TPR domain; geldanamycin and ascomycin act synergistically to inhibit P. falciparum growth. Co-immunoprecipitation of native proteins, pharmacological disruption with geldanamycin, TPR domain interaction analysis Molecular and biochemical parasitology Medium 15811524 15850699
2010 Full-length recombinant PfHsp90 has the highest ATPase activity of all known Hsp90s (6-fold higher than human Hsp90); geldanamycin inhibits PfHsp90 ATPase activity more robustly than human Hsp90; a site of acetylation overlapping with the Aha1 and p23 binding domain was identified by mass spectrometry, and histone deacetylase inhibitor treatment causes partial dissociation of the PfHsp90 complex. In vitro ATPase assay on recombinant protein, geldanamycin competition, mass spectrometric identification of acetylation site, histone deacetylase inhibitor treatment with complex analysis The Journal of biological chemistry High 20837488
2010 Crystal structure of the N-terminal ATP-binding domain of PfHsp90 was solved in apo and ADP-bound states at 2.3 Å resolution, showing the principal drug-binding pocket and high structural similarity to human Hsp90. X-ray crystallography Proteins High 20635416
2011 PfHop co-localises with PfHsp70 and PfHsp90 in trophozoite-stage parasites; gel filtration and co-immunoprecipitation demonstrate PfHop is present in a complex with both PfHsp70 and PfHsp90, suggesting PfHop mediates their functional interaction. Immunofluorescence co-localization, gel filtration, co-immunoprecipitation Cell stress & chaperones Medium 22005844
2010 Recombinant Pfp23 suppresses citrate synthase aggregation (chaperone activity) and interacts with PfHsp90 to suppress its ATPase activity; site-directed mutagenesis identified residues K91, H93, W94, and K96 in Pfp23 as crucial for binding PfHsp90. In vitro aggregation suppression assay, ATPase inhibition assay, site-directed mutagenesis, modeling of protein complex Cellular and molecular life sciences High 20140477
2012 The unusually extended charged linker of PfHsp90 was introduced into yeast Hsp90 and shown to affect ATPase activity, cochaperone interaction, and conformation, establishing that the linker sequence (not just length) modulates chaperone function. Chimeric yeast Hsp90 constructs with native/artificial linkers, in vitro ATPase assay, biophysical characterization, in vivo yeast complementation Proceedings of the National Academy of Sciences of the United States of America Medium 22315411
2012 Site-directed mutagenesis identified Arg98 in PfHsp90 as essential for selective binding of harmine (a beta-carboline alkaloid) to PfHsp90 over human Hsp90; harmine binding was confirmed by surface plasmon resonance (Kd = 40 µM). Surface plasmon resonance binding assay, site-directed mutagenesis Antimicrobial agents and chemotherapy Medium 22615284
2015 PfHsp90 was identified as a binding partner for class 2 imidazopyridazine compounds at its ATP-binding N-terminal domain; a representative compound bound the ATP-binding site as shown by structural and biochemical analysis, and these compounds inhibit trophozoite-stage parasite growth. Binding partner identification, structural/biochemical analysis of compound-PfHsp90 interaction, stage-specific parasite growth inhibition assay Antimicrobial agents and chemotherapy Medium 26711771
2015 PfHop directly associates with PfHsp70-1 in a nucleotide-dependent fashion (ADP promotes the interaction more than ATP); TPR1 and TPR2B subdomains of PfHop preferentially bind the C-terminus of PfHsp70-1, while the TPR2A motif preferentially interacts with the C-terminus of PfHsp90. Far Western analysis, surface plasmon resonance, co-immunoprecipitation, split-GFP approach for TPR subdomain interaction mapping PloS one High 26267894
2018 PfHsp90 inhibitors exhibit anti-Plasmodium activity at both liver and blood stages; time-course inhibition studies support a role for PfHsp90 in late liver-stage parasite development; PfHsp90 inhibitor SNX-0723 synergizes with PIK-75 to reduce liver-stage parasite load. Target-based compound binding screens, cell-based liver-stage and blood-stage malaria assays, time-course inhibition studies, expression analysis Antimicrobial agents and chemotherapy Medium 29339390
2022 PfHsp90 physically interacts with PfSir2A (a histone deacetylase); inhibition of PfHsp90 by 17-AAG or radicicol results in depletion of PfSir2A protein and loss of its histone deacetylase activity, causing derepression of var genes and loss of ribosomal silencing. PfHsp90 thus acts as a chaperone required for PfSir2A stability. Co-immunoprecipitation of PfHsp90-PfSir2A complex, pharmacological inhibition (17-AAG, radicicol) with Western blot for PfSir2A levels, histone deacetylase activity assay, var gene expression analysis mSphere High 36121150
2024 Thermal proteome profiling following selective PfHsp90 inhibition identified the 26S proteasome as enriched among proteins with perturbed stability; subsequent biochemical and cellular studies support that PfHsp90 directly promotes proteasome hydrolysis by chaperoning the active 26S complex. Thermal proteome profiling, biochemical proteasome activity assays, cellular studies with selective PfHsp90 inhibitors (BX-2819, XL888, Tropane 1) Cell chemical biology High 38492573
2025 The C-terminus of PfHsp90 contains a specific nucleotide-binding site that interacts with ATP, dATP, and ADP (but not AMP or GTP), as shown by affinity experiments with a lysine-reactive nucleotide analog and an ATP resin; limited proteolysis and mutagenesis support this interaction at the C-terminal domain. Affinity experiments with lysine-reactive nucleotide analog and ATP resin, limited proteolysis, site-directed mutagenesis, computational analysis Bioorganic & medicinal chemistry Medium 40907219
1994 The PfHsp90 gene (pfhsp86) is constitutively expressed in both trophozoite and gametocyte stages; transcription is enhanced 2–4-fold at elevated temperatures (39–41°C); the protein is encoded by a single gene with two exons separated by an intron; the sequence contains an unusually large charged amino acid region homologous to the calreticulin calcium-binding domain; phylogenetic analysis places PfHsp90 closer to plant Hsp90 than to vertebrate or other parasite Hsp90s. Gene sequencing, Northern blot (stage-specific expression), phylogenetic analysis, sequence homology analysis Molecular and biochemical parasitology / Gene Medium 3060854 7838176

Source papers

Stage 0 corpus · 55 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Molecular and biochemical parasitology 198 17125854
2003 Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. The Journal of biological chemistry 189 12584193
2010 Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug. The Journal of biological chemistry 139 20837488
2012 Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity. Proceedings of the National Academy of Sciences of the United States of America 105 22315411
2011 Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis. Protein and peptide letters 90 20955165
2009 Plasmodial heat shock proteins: targets for chemotherapy. FEMS immunology and medical microbiology 85 20041948
2003 The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin. Malaria journal 82 14514358
2004 Recurrent fever promotes Plasmodium falciparum development in human erythrocytes. The Journal of biological chemistry 70 15339915
2010 A repurposing strategy identifies novel synergistic inhibitors of Plasmodium falciparum heat shock protein 90. Journal of medicinal chemistry 64 20349996
2011 Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop). Cell stress & chaperones 58 22005844
2005 The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity. Molecular and biochemical parasitology 56 15850699
1994 Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falciparum. Molecular and biochemical parasitology 56 7838176
2012 Harmine is a potent antimalarial targeting Hsp90 and synergizes with chloroquine and artemisinin. Antimicrobial agents and chemotherapy 52 22615284
2010 Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins 52 20635416
2005 Plasmodium falciparum calcineurin and its association with heat shock protein 90: mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin. Molecular and biochemical parasitology 51 15811524
2015 Imidazopyridazine Inhibitors of Plasmodium falciparum Calcium-Dependent Protein Kinase 1 Also Target Cyclic GMP-Dependent Protein Kinase and Heat Shock Protein 90 To Kill the Parasite at Different Stages of Intracellular Development. Antimicrobial agents and chemotherapy 47 26711771
2015 Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity. PloS one 38 26267894
1994 Sequence, transcript characterization and polymorphisms of a Plasmodium falciparum gene belonging to the heat-shock protein (HSP) 90 family. Gene 38 7828879
2011 Post-transcriptional repair of a split heat shock protein 90 gene by mRNA trans-splicing. The Journal of biological chemistry 35 21209094
2010 Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients. Malaria journal 35 20719001
2001 A novel tetratricopeptide repeat (TPR) containing PP5 serine/threonine protein phosphatase in the malaria parasite, Plasmodium falciparum. BMC microbiology 35 11737864
2018 Identification of Hsp90 Inhibitors with Anti-Plasmodium Activity. Antimicrobial agents and chemotherapy 34 29339390
2016 In vitro and in vivo anti-malarial activity of novel harmine-analog heat shock protein 90 inhibitors: a possible partner for artemisinin. Malaria journal 33 27903279
2007 Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: molecular modelling approach to rational drug design against malaria. Journal of biosciences 32 17536172
2013 Targeting Plasmodium falciparum Hsp90: Towards Reversing Antimalarial Resistance. Pathogens (Basel, Switzerland) 30 25436880
1988 Identification of a heat shock-like antigen in P. falciparum, related to the heat shock protein 90 family. Nucleic acids research 27 3060854
2022 Design and synthesis of harmiquins, harmine and chloroquine hybrids as potent antiplasmodial agents. European journal of medicinal chemistry 26 35551033
1994 Immunogenicity and antigenicity of a Plasmodium falciparum protein fraction (90-110 kDa) able to protect squirrel monkeys against asexual blood stages. Vaccine 26 8303938
2013 Heat shock protein 90 inhibitors as broad spectrum anti-infectives. Current pharmaceutical design 23 22920905
2021 Inhibitors of the Plasmodium falciparum Hsp90 towards Selective Antimalarial Drug Design: The Past, Present and Future. Cells 18 34831072
2011 Target highlights in CASP9: Experimental target structures for the critical assessment of techniques for protein structure prediction. Proteins 17 22020785
2010 Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90. Cellular and molecular life sciences : CMLS 17 20140477
2022 Hsp90 and Associated Co-Chaperones of the Malaria Parasite. Biomolecules 16 35892329
2019 Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function. Biophysical reviews 16 31734827
2014 Co-chaperones of Hsp90 in Plasmodium falciparum and their concerted roles in cellular regulation. Parasitology 16 24560171
2024 Selective targeting of Plasmodium falciparum Hsp90 disrupts the 26S proteasome. Cell chemical biology 15 38492573
2023 Pharmacophore Model-Based Virtual Screening Workflow for Discovery of Inhibitors Targeting Hsp90. ACS omega 15 37867657
2021 Further investigation of harmicines as novel antiplasmodial agents: Synthesis, structure-activity relationship and insight into the mechanism of action. European journal of medicinal chemistry 15 34274829
2021 Plasmodium berghei Hsp90 contains a natural immunogenic I-Ab-restricted antigen common to rodent and human Plasmodium species. Current research in immunology 15 35492393
2018 Novobiocin-ferrocene conjugates possessing anticancer and antiplasmodial activity independent of HSP90 inhibition. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 15 30542925
2018 In silico identification and evaluation of potential interaction of Azadirachta indica phytochemicals with Plasmodium falciparum heat shock protein 90. Journal of molecular graphics & modelling 15 30544005
2023 The Plasmodium falciparum exported J domain proteins fine-tune human and malarial Hsp70s: pathological exploitation of proteostasis machinery. Frontiers in molecular biosciences 11 37457831
2013 Targeting heat shock protein 90 for malaria. Mini reviews in medicinal chemistry 11 24070209
2021 Molecular docking and molecular dynamics simulation identify a novel Radicicol derivative that predicts exclusive binding to Plasmodium falciparum Topoisomerase VIB. Journal of biomolecular structure & dynamics 10 33650468
2024 Characterization and Inhibition of the Chaperone Function of Plasmodium falciparum Glucose-Regulated Protein 94 kDa (Pf Grp94). Proteins 7 39670568
1999 Stage-specific expression of heat shock protein 90 in murine malaria parasite Plasmodium yoelii. Experimental parasitology 7 10502467
2021 Role of Hsp90 in Plasmodium falciparum Malaria. Advances in experimental medicine and biology 6 34569023
2024 Ursolic acid acetate and iso-mukaadial acetate bind to Plasmodium falciparum Hsp90, abrogating its chaperone function in vitro. Naunyn-Schmiedeberg's archives of pharmacology 5 38252299
2022 Heat Shock Protein 90 Regulates the Activity of Histone Deacetylase Sir2 in Plasmodium falciparum. mSphere 5 36121150
2024 Auto QSAR-based active learning docking for hit identification of potential inhibitors of Plasmodium falciparum Hsp90 as antimalarial agents. PloS one 4 39585817
2023 In silico prediction and in vitro assessment of novel heterocyclics with antimalarial activity. Parasitology research 4 38155300
2018 Structure-activity relationship of new antimalarial 1-aryl-3-susbtituted propanol derivatives: Synthesis, preliminary toxicity profiling, parasite life cycle stage studies, target exploration, and targeted delivery. European journal of medicinal chemistry 4 29754074
2025 The possibilities and challenges associated with selective targeting Plasmodium falciparum Hsp90 for Malaria. Transactions of the Royal Society of South Africa. Royal Society of South Africa 1 41836916
2026 Synthetic quinolone-tethered aminoguanidine derivatives exhibit potent anti-plasmodial activity. International journal of antimicrobial agents 0 41921671
2025 Investigation of a cryptic ligand binding site on Plasmodium falciparum Hsp90. Bioorganic & medicinal chemistry 0 40907219