Affinage · Plasmodium

GAPDH

PF3D7_1462800 · glyceraldehyde-3-phosphate dehydrogenase

Annotated
2026-09-08
41 papers in source corpus 18 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1462800 (GAPDH) is the P. falciparum glyceraldehyde-3-phosphate dehydrogenase, an NAD+-specific (not NADP+-dependent) homotetrameric glycolytic oxidoreductase whose catalytic cysteine and quaternary assembly are central to both its metabolic and moonlighting functions (PMID:10767547, PMID:16131754, PMID:26341815). Its active-site groove carries a unique -KG- dipeptide insertion in the S loop that distinguishes it structurally from human GAPDH and underlies its exceptional sensitivity to inhibition by free heme (ferriprotoporphyrin IX, Ki ~0.2 µM) (PMID:12748176, PMID:16131754). The enzyme's catalytic cysteine is a hub for reversible redox regulation: S-glutathionylation and S-nitrosylation each inhibit activity, with glutaredoxin 1, thioredoxin 1, and plasmoredoxin reversing glutathionylation and the thioredoxin system modulating nitrosylation (PMID:21595565, PMID:24256207, PMID:20307687). This same reactive cysteine is exploited by covalent antimalarial chemotypes — 3-bromo-isoxazolines and phenoxynaphthoquinones alkylate it, with selectivity over human GAPDH arising because all four parasite subunits are alkylated whereas partial alkylation of human GAPDH triggers a protective conformational rearrangement (PMID:25137375, PMID:27137361, PMID:28079302). Beyond glycolysis, GAPDH is recruited to parasite membranes during schizogony via an N-terminal, Rab2-dependent mechanism and accumulates at the merozoite apical region, binds cytoplasmic tails of RH and DBL invasion ligands, and localizes to the sporozoite surface where its C-terminal domain engages Kupffer-cell CD68 to mediate liver-stage traversal and hepatocyte infection (PMID:12974391, PMID:22991428, PMID:27551151, PMID:30456380). Its oligomerization state also governs antimalarial susceptibility: fosmidomycin-resistance alleles reduce tetramer assembly, alter cooperativity, and blunt heme inhibition, linking GAPDH quaternary structure to MEP pathway flux (PMID:36103572).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2000 Medium

    Establishing that the parasite enzyme is a bona fide NAD+-dependent oxidoreductase defined its basic catalytic identity and cofactor specificity.

    Evidence Recombinant expression in E. coli with NAD+ versus NADP+ activity assays

    PMID:10767547

    Open questions at the time
    • No kinetic constants or quaternary structure defined at this stage
    • No cellular localization or in vivo role addressed
  2. 2003 High

    Discovery that heme binds and potently inhibits the enzyme (Ki ~0.2 µM), far more than red-cell GAPDH, identified glycolysis as a heme-vulnerable node unique to the parasite.

    Evidence FP-agarose affinity pulldown plus in vitro inhibition assay with Ki determination

    PMID:12748176

    Open questions at the time
    • Structural basis of selectivity over host GAPDH not yet resolved
    • Physiological relevance of heme inhibition in intact parasite not established
  3. 2003 High

    Membrane recruitment via the N-terminal domain in a Rab2-dependent manner during schizogony revealed a non-glycolytic role in vesicular transport and apical organelle biogenesis.

    Evidence IFA, subcellular fractionation, and competitive microsomal binding with recombinant N-terminal fragment

    PMID:12974391

    Open questions at the time
    • Direct Rab2–GAPDH interaction interface not defined
    • Functional consequence of membrane recruitment not tested by loss-of-function
  4. 2005 High

    The crystal structure showed a homotetramer with one NAD+ per subunit and a unique S-loop -KG- insertion, providing the structural rationale for selective heme inhibition.

    Evidence X-ray crystallography at ~2.25 Å with comparison to human GAPDH

    PMID:16131754

    Open questions at the time
    • Direct structural evidence of heme bound in the groove not obtained
    • Link between S-loop insertion and inhibitor selectivity remained inferred
  5. 2006 Medium

    A second structure revealed an exploitable ligand-binding pocket in the active site near NAD+, framing the enzyme as an inhibitor-design target.

    Evidence X-ray crystallography with extra active-site electron density

    PMID:16345073

    Open questions at the time
    • Identity of the bound ligand only inferred (likely AEBSF)
    • No demonstrated antimalarial compound occupying this pocket
  6. 2011 High

    Identification of reversible S-glutathionylation reversed by glutaredoxin 1, thioredoxin 1, and plasmoredoxin established redox modification of the catalytic cysteine as a physiological activity switch.

    Evidence Biotin-maleimide affinity purification, proteomics, and enzyme activity assays before/after deglutathionylation

    PMID:21595565

    Open questions at the time
    • In vivo trigger and dynamics of glutathionylation not defined
    • Fraction of cellular GAPDH modified under physiological stress unknown
  7. 2010 Medium

    Capture as a thioredoxin 1 substrate that enhances its activity connected the enzyme to the parasite thiol-redox network.

    Evidence Trx-affinity chromatography with PfTrx-1(C33S) mixed-disulfide trap, LC-MS, and activity assay

    PMID:20307687

    Open questions at the time
    • Specific cysteine(s) targeted by Trx-1 not mapped
    • Single-lab affinity capture without reciprocal validation
  8. 2014 Medium

    Detection of active-site S-nitrosylation as an inhibitory modification, with Trx1 acting as both trans- and de-nitrosylase, extended redox control to nitric-oxide signaling.

    Evidence Biotin-switch/MS S-nitrosoproteome screen plus mechanistic Trx1 assays

    PMID:24256207

    Open questions at the time
    • Direct reversal of GAPDH inhibition by Trx1 not explicitly demonstrated
    • Physiological nitrosylation stoichiometry unknown
  9. 2012 Medium

    Binding to cytoplasmic tails of RH and DBL invasion ligands via an aromatic/charged motif positioned the enzyme as a possible connector between merozoite surface ligands and the actin motor.

    Evidence Peptide pulldown and surface plasmon resonance

    PMID:22991428

    Open questions at the time
    • Interaction not validated in intact merozoites
    • Functional requirement for invasion not tested genetically
  10. 2016 High

    Surface localization on sporozoites and direct binding to Kupffer-cell CD68 defined a moonlighting adhesin role in liver-stage invasion, with an anti-mimotope antibody blocking invasion without host cross-reactivity.

    Evidence Phage display, PfGAPDH–CD68 binding assay, and antibody inhibition of liver invasion

    PMID:27551151

    Open questions at the time
    • Mechanism of surface trafficking of a cytosolic enzyme unresolved
    • Downstream signaling in Kupffer cells not defined
  11. 2018 Medium

    Mapping the CD68-binding interface to two C-terminal epitopes localized the adhesive determinant required for Kupffer-cell traversal.

    Evidence Epitope mapping and antibody inhibition of infection

    PMID:30456380

    Open questions at the time
    • Structure of the C-terminal–CD68 complex not determined
    • Epitope-level mapping from a single lab
  12. 2014 High

    Covalent inhibition by 3-bromo-isoxazolines alkylating the catalytic cysteine, tunable by ring substituents, validated the active-site thiol as a druggable target.

    Evidence In vitro inhibition, MS confirmation of adduct, computational electrostatics

    PMID:25137375

    Open questions at the time
    • Selectivity over human GAPDH not yet explained at this stage
    • Whole-cell antiparasitic efficacy not addressed
  13. 2016 High

    Demonstration that full alkylation of all four parasite subunits (versus a protective conformational block in human GAPDH after single-site alkylation) provided a structural basis for inhibitor selectivity.

    Evidence In vitro inhibition, MS quantification of alkylation across subunits, conformational analysis

    PMID:27137361

    Open questions at the time
    • Structural snapshot of the conformational rearrangement not captured
    • Selectivity not confirmed against other host homologs
  14. 2017 Medium

    A second covalent chemotype (phenoxynaphthoquinone) engaging the catalytic cysteine via phenolate displacement, with rate differences among homologs, reinforced active-site electrostatics as a selectivity handle.

    Evidence In vitro covalent inhibition and biochemical adduct characterization with analogs

    PMID:28079302

    Open questions at the time
    • Mechanism partly inferred from analog series
    • No cellular or in vivo validation
  15. 2019 Medium

    Assigning GAPDH as the source of the damaged metabolite 4-phosphoerythronate placed it within a metabolite-damage pathway whose product, when unrepaired by PGP, dysregulates upper glycolysis and the pentose phosphate pathway.

    Evidence pgp genetic knockout, metabolite profiling, and pathway epistasis

    PMID:31822583

    Open questions at the time
    • GAPDH as the 4-PE source is inferred, not directly demonstrated
    • Rate of side-product formation in vivo unquantified
  16. 2022 High

    Convergent genetic screens linking GAPDH oligomerization state to fosmidomycin resistance showed that reduced tetramer assembly, altered cooperativity, and diminished heme inhibition control MEP pathway sensitivity, unifying quaternary structure with drug susceptibility.

    Evidence Parallel resistance screens, metabolic profiling, and biochemical assays of oligomerization, cooperativity, and heme inhibition

    PMID:36103572

    Open questions at the time
    • Mechanistic link between GAPDH oligomer state and MEP flux not fully resolved
    • Structural basis of assembly-defective variants not determined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a cytosolic glycolytic enzyme is trafficked to and displayed on the sporozoite surface and merozoite membranes, and how its moonlighting adhesin and redox-regulatory roles are coordinated with glycolytic flux in vivo, remains unresolved.
  • No secretion/surface-trafficking mechanism identified for the cytosolic enzyme
  • No genetic dissection separating glycolytic from moonlighting functions
  • In vivo contribution of redox modifications to parasite physiology unquantified

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
CYTOPLASMIC TAILS OF RH AND DBL MEROZOITE INVASION LIGANDSFERRIPROTOPORPHYRIN IX / FREE HEME (INHIBITOR, KI ~0.2 ΜM)GLUTAREDOXIN 1 (DEGLUTATHIONYLATION)KUPFFER-CELL CD68 RECEPTOR (C-TERMINAL DOMAIN)PLASMOREDOXIN (DEGLUTATHIONYLATION)RAB2 GTPASE (N-TERMINAL-DEPENDENT MEMBRANE RECRUITMENT)THIOREDOXIN 1 (PFTRX-1; ACTIVITY ENHANCEMENT, DENITROSYLATION/TRANSNITROSYLATION)
Complex memberships
Homotetramer (each subunit binds one NAD+)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 P. falciparum GAPDH (PfGAPDH) was recombinantly expressed in E. coli and shown to exhibit enzymatic (oxidoreductase) activity with NAD+ but not NADP+ as cofactor, establishing cofactor specificity. The gene contains 1 intron and the predicted ORF codes for 337 amino acids (36.6 kDa). Recombinant protein expression in E. coli, enzymatic activity assay with NAD+ vs NADP+ Gene Medium 10767547
2003 PfGAPDH binds to ferriprotoporphyrin IX (FP/heme) immobilized on agarose (pulldown), and FP inhibits PfGAPDH enzymatic activity with a Ki of 0.2 µM — far more potently than red blood cell GAPDH — suggesting the glycolytic pathway is particularly susceptible to heme-mediated inhibition in the parasite. Affinity pulldown on FP-agarose; in vitro enzyme inhibition assay with Ki determination The Journal of biological chemistry High 12748176
2003 PfGAPDH localizes to both membrane-containing pellet and cytosolic supernatant fractions (whereas aldolase is cytosol-only), and is recruited to membranes in a GTPase Rab2-dependent manner. The N-terminal domain (residues 1–192) of PfGAPDH mediates this Rab2-dependent membrane recruitment, as demonstrated by competitive inhibition with the N-terminal fragment. During schizogony, PfGAPDH accumulates at the parasite periphery and apical region of merozoites, suggesting a non-glycolytic role in vesicular transport and apical organelle biogenesis. Indirect immunofluorescence; subcellular fractionation; quantitative microsomal binding assay with recombinant fragments; competitive inhibition assay Biological chemistry High 12974391
2005 Crystal structure of PfGAPDH determined at ~2.25 Å resolution shows a homotetrameric enzyme with one NAD+ per subunit. A unique dipeptide insertion (-KG-) in the S loop, together with characteristic single amino acid substitutions, distinguishes the PfGAPDH active-site groove from human GAPDH and may account for the selective inhibition by ferriprotoporphyrin IX. X-ray crystallography of recombinant His-tagged protein; structural comparison Acta crystallographica. Section D, Biological crystallography High 16131754
2006 Crystal structure of PfGAPDH solved at 2.25 Å reveals unexpected extra electron density in the active site (likely the protease inhibitor AEBSF) near the nicotinamide ribose of bound NAD+, identifying a ligand-binding pocket in the active site that can be exploited for inhibitor design. X-ray crystallography Proteins Medium 16345073
2006 PfGAPDH enzymatic activity is abolished by treatment with 2.5 mM dihydroxyacetone within 6 h in vitro; methylglyoxal at 2.5 mM did not affect PfGAPDH activity over 20 h, distinguishing the two substrates of PfAQP in their ability to inhibit GAPDH. In vitro enzyme activity assay with recombinant PfGAPDH; compound treatment Biochimica et biophysica acta Medium 16427024
2010 PfGAPDH is captured as a substrate/target of cytosolic thioredoxin 1 (PfTrx-1) via a Trx-affinity chromatography approach using a cysteine mutant (C33S) that forms a stable mixed disulfide intermediate. PfTrx-1 was shown to enhance PfGAPDH enzymatic activity, establishing a redox-regulatory interaction. Trx-affinity chromatography with cysteine mutant PfTrx-1(C33S); LC-MS identification; enzyme activity assay Parasitology international Medium 20307687
2011 PfGAPDH is a target of S-glutathionylation in P. falciparum, and this modification reversibly inhibits its enzymatic activity. P. falciparum glutaredoxin 1, thioredoxin 1, and plasmoredoxin are each able to catalyze deglutathionylation and thereby restore PfGAPDH activity. Enzymatic deglutathionylation; affinity purification with biotin-maleimide; proteomics; enzyme activity assay confirming reversible inhibition Antioxidants & redox signaling High 21595565
2012 PfGAPDH binds in a peptide pulldown/SPR assay to the cytoplasmic tails of certain P. falciparum merozoite Reticulocyte Homology (RH) and Duffy Binding-Like (DBL) ligands in a manner dependent on an aromatic amino acid (phenylalanine or tyrosine) in the context of negatively charged residues. This places PfGAPDH as a potential connector between merozoite surface ligands and the actin motor during invasion. Peptide pulldown binding assay; surface plasmon resonance (SPR) mBio Medium 22991428
2014 PfGAPDH is strongly inhibited by S-nitrosylation of its active-site cysteine; this was identified in a systematic biotin-switch/MS screen of the P. falciparum S-nitrosoproteome. Additionally, PfTrx1 was shown to possess transnitrosylating activity at its Cys43 and denitrosylating activity via its active-site cysteines, indicating the thioredoxin system modulates this modification on PfGAPDH. Biotin-switch assay coupled to mass spectrometry; mechanistic studies of PfTrx1 denitrosylating/transnitrosylating activities Antioxidants & redox signaling Medium 24256207
2014 3-Bromo-isoxazoline derivatives covalently inhibit PfGAPDH by selectively alkylating the catalytic cysteine, as confirmed by mass spectrometry. Substituents on the isoxazolinic ring modulate potency up to 20-fold, predominantly through an electrostatic effect. In vitro enzyme inhibition assay; mass spectrometry confirmation of covalent adduct; computational analysis Journal of medicinal chemistry High 25137375
2015 Recombinant PfGAPDH is a homotetramer with optimal pH ~9; kinetic measurements gave KmNAD = 0.28 mM and KmG3P = 0.25 mM. P. yoelii GAPDH was detected in all four subcellular fractions (cytosol, nucleus, cytoskeleton, membranes) by differential detergent fractionation, with multiple molecular species suggesting post-translational modifications. Recombinant protein expression and purification; enzyme kinetics; differential detergent fractionation; 2D gel electrophoresis; Western blot; LC-ESI-MS Protein expression and purification Medium 26341815
2016 3-Bromo-isoxazoline compounds fully inhibit PfGAPDH by alkylating all four catalytic cysteines of the tetramer, whereas under identical conditions human GAPDH was only 25% inhibited with alkylation of a single cysteine. Partial alkylation of human GAPDH produces a conformational rearrangement that restricts access of bulky 3-Br-isoxazoline inhibitors to the remaining active sites, explaining the selectivity. In vitro enzyme inhibition assay; mass spectrometry of alkylation; structural/conformational analysis Bioorganic & medicinal chemistry High 27137361
2016 PfGAPDH is present on the surface of Plasmodium sporozoites and directly interacts with CD68 on the Kupffer cell surface, mediating sporozoite traversal of Kupffer cells and subsequent hepatocyte infection. A P39 mimotope peptide identified by phage display was shown to be a structural mimic of PfGAPDH, and an anti-P39 antibody inhibits sporozoite liver invasion without cross-reacting with mammalian GAPDH. Phage display library screening; direct binding assay (PfGAPDH–CD68 interaction); antibody inhibition assay of liver invasion The Journal of experimental medicine High 27551151
2017 2-Phenoxy-1,4-naphthoquinone forms a covalent adduct with the PfGAPDH catalytic cysteine through a phenolate displacement mechanism, demonstrated by chemical/biochemical studies. Up to fivefold differences in inactivation rates among GAPDH homologs indicate structural/electrostatic differences in the active sites. In vitro covalent inhibition assay; analog design; biochemical characterization of adduct formation Chemical biology & drug design Medium 28079302
2018 The C-terminal end of Plasmodium GAPDH interacts with the Kupffer cell CD68 receptor, and two epitopes within this C-terminal region were identified as the ligand-binding interface required for sporozoite traversal of Kupffer cells. Epitope mapping; antibody inhibition assay of Plasmodium infection Life science alliance Medium 30456380
2019 PfGAPDH is implicated as a side-product-generating enzyme: its activity produces 4-phosphoerythronate (4-PE) as a damaged metabolite by-product. Accumulation of 4-PE (caused by loss of phosphoglycolate phosphatase PGP) inhibits 6-phosphogluconate dehydrogenase, causing metabolic dysregulation including partial inhibition of upper glycolysis — placing PfGAPDH in a metabolite damage pathway. Genetic disruption of pgp (KO); metabolite profiling; epistasis/metabolic pathway analysis mBio Medium 31822583
2022 Two independent genetic screens in P. falciparum converged on resistance alleles in GAPDH that confer fosmidomycin (FSM) resistance. FSM-resistant GAPDH variant proteins are catalytically active but show reduced assembly into the homotetrameric state, altered enzymatic cooperativity, and reduced susceptibility to inhibition by free heme. These data establish that GAPDH oligomerization state controls MEP pathway sensitivity and antimalarial susceptibility. Parallel genetic resistance screens; metabolic profiling; biochemical characterization of oligomerization; enzyme cooperativity and heme inhibition assays PLoS pathogens High 36103572

Source papers

Stage 0 corpus · 41 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Protein S-glutathionylation in malaria parasites. Antioxidants & redox signaling 87 21595565
2001 Determining liver stage parasite burden by real time quantitative PCR as a method for evaluating pre-erythrocytic malaria vaccine efficacy. Molecular and biochemical parasitology 61 11738713
2003 Identification and characterization of heme-interacting proteins in the malaria parasite, Plasmodium falciparum. The Journal of biological chemistry 58 12748176
2003 The N'-terminal domain of glyceraldehyde-3-phosphate dehydrogenase of the apicomplexan Plasmodium falciparum mediates GTPase Rab2-dependent recruitment to membranes. Biological chemistry 57 12974391
1994 Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage. European journal of biochemistry 56 8125109
2016 Identification of GAPDH on the surface of Plasmodium sporozoites as a new candidate for targeting malaria liver invasion. The Journal of experimental medicine 47 27551151
2006 Dihydroxyacetone and methylglyoxal as permeants of the Plasmodium aquaglyceroporin inhibit parasite proliferation. Biochimica et biophysica acta 45 16427024
2016 Rapid Generation of Marker-Free P. falciparum Fluorescent Reporter Lines Using Modified CRISPR/Cas9 Constructs and Selection Protocol. PloS one 42 27997583
2014 Discovery of covalent inhibitors of glyceraldehyde-3-phosphate dehydrogenase, a target for the treatment of malaria. Journal of medicinal chemistry 37 25137375
2003 The treatment of Plasmodium falciparum-infected erythrocytes with chloroquine leads to accumulation of ferriprotoporphyrin IX bound to particular parasite proteins and to the inhibition of the parasite's 6-phosphogluconate dehydrogenase. Parasite (Paris, France) 37 12669348
2005 Structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum. Acta crystallographica. Section D, Biological crystallography 30 16131754
2006 Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 A resolution reveals intriguing extra electron density in the active site. Proteins 28 16345073
2000 Identification and recombinant expression of glyceraldehyde-3-phosphate dehydrogenase of Plasmodium falciparum. Gene 27 10767547
2014 Protein S-nitrosylation in Plasmodium falciparum. Antioxidants & redox signaling 25 24256207
2017 Plasmodium glyceraldehyde-3-phosphate dehydrogenase: A potential malaria diagnostic target. Experimental parasitology 24 28552792
2008 The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro. Malaria journal 21 18721457
1982 Specific inactivation of glucose metabolism from eucaryotic cells by pentalenolactone. Biochimica et biophysica acta 21 7034785
2023 Multi-omics dissection of stage-specific artemisinin tolerance mechanisms in Kelch13-mutant Plasmodium falciparum. Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy 20 37385107
2019 The Metabolite Repair Enzyme Phosphoglycolate Phosphatase Regulates Central Carbon Metabolism and Fosmidomycin Sensitivity in Plasmodium falciparum. mBio 18 31822583
2019 A P. falciparum NF54 Reporter Line Expressing mCherry-Luciferase in Gametocytes, Sporozoites, and Liver-Stages. Frontiers in cellular and infection microbiology 16 31058097
2016 Selectivity of 3-bromo-isoxazoline inhibitors between human and Plasmodium falciparum glyceraldehyde-3-phosphate dehydrogenases. Bioorganic & medicinal chemistry 15 27137361
2017 Molecular basis for covalent inhibition of glyceraldehyde-3-phosphate dehydrogenase by a 2-phenoxy-1,4-naphthoquinone small molecule. Chemical biology & drug design 14 28079302
2012 Binding of aldolase and glyceraldehyde-3-phosphate dehydrogenase to the cytoplasmic tails of Plasmodium falciparum merozoite duffy binding-like and reticulocyte homology ligands. mBio 13 22991428
2010 Target proteins of the cytosolic thioredoxin in Plasmodium falciparum. Parasitology international 12 20307687
2018 Identification of Plasmodium GAPDH epitopes for generation of antibodies that inhibit malaria infection. Life science alliance 11 30456380
2015 Cloning, expression, purification and characterization of Plasmodium spp. glyceraldehyde-3-phosphate dehydrogenase. Protein expression and purification 11 26341815
2023 Role of Stereochemistry on the Biological Activity of Nature-Inspired 3-Br-Acivicin Isomers and Derivatives. Molecules (Basel, Switzerland) 9 37049935
2022 GAPDH mediates drug resistance and metabolism in Plasmodium falciparum malaria parasites. PLoS pathogens 9 36103572
2019 Covalent Inhibitors of Plasmodium falciparum Glyceraldehyde 3-Phosphate Dehydrogenase with Antimalarial Activity in Vitro. ACS medicinal chemistry letters 9 30996801
2015 Comparing Antibody Responses in Chickens Against Plasmodium falciparum Lactate Dehydrogenase and Glyceraldehyde-3-phosphate Dehydrogenase with Freund's and Pheroid® Adjuvants. Immunological investigations 8 26436851
2012 Direct loop-mediated isothermal amplification from Plasmodium chabaudi infected blood samples: inability to discriminate genomic and cDNA sequences. Experimental parasitology 8 22417971
2008 Phylogenetic and structural information on glyceraldehyde-3-phosphate dehydrogenase (G3PDH) in Plasmodium provides functional insights. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases 8 18472435
1991 Is Plasmodium falciparum aldolase useful for rational drug design? Acta Leidensia 6 1820702
2022 A Dual, Systematic Approach to Malaria Diagnostic Biomarker Discovery. Clinical infectious diseases : an official publication of the Infectious Diseases Society of America 5 34718455
2014 Proteomics analysis of antimalarial targets of Garcinia mangostana Linn. Asian Pacific journal of tropical biomedicine 4 25183269
2025 Congenital malaria in newborns of mothers living in highly endemic parts of Kinshasa, Democratic Republic of Congo. Paediatrics and international child health 1 39992706
2026 Multifunctional glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of parasites. Molecular and biochemical parasitology 0 41581767
2025 The impact of Iso-mukaadial acetate on Plasmodium falciparum transcriptional gene regulation. Scientific reports 0 41309744
2023 Comparative analyses of functional antibody-mediated inhibition with anti-circumsporozoite monoclonal antibodies against transgenic Plasmodium berghei. Malaria journal 0 37936181
2009 [Inhibition of CpG oligodeoxynucleotide on the development of pre-erythrocytic stage of Plasmodium]. Zhongguo ji sheng chong xue yu ji sheng chong bing za zhi = Chinese journal of parasitology & parasitic diseases 0 19459490
2002 [Sequencing of the glyceraldehyde-3-phosphate dehydrogenase gene from Plasmodium falciparum strain FCC1/HN]. Zhongguo ji sheng chong xue yu ji sheng chong bing za zhi = Chinese journal of parasitology & parasitic diseases 0 12567551