Affinage · Plasmodium

GCN5

PF3D7_0823300 · histone acetyltransferase GCN5

Annotated
2026-09-08
34 papers in source corpus 20 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0823300 (GCN5) is an essential histone acetyltransferase that couples chromatin acetylation to stage-specific transcriptional programs in Plasmodium falciparum (PMID:15075257, PMID:17449656, PMID:40156869). Its conserved HAT domain preferentially acetylates histone H3 at K9 and K14 (and to a lesser extent K8), a specificity retained across the divergent P. falciparum H3 N-terminus and validated by functional complementation of a yeast GCN5 deletion (PMID:15075257, PMID:16410041). Genome-wide, GCN5 occupancy tracks H3K9ac and is enriched at promoters of actively transcribed genes, where its deposition of H3K9ac activates transcription; H3K9ac peak intensity correlates positively with expression level (PMID:17449656, PMID:40558503). GCN5 is recruited to target promoters by AP2-domain transcription factors, whose binding motifs coincide with GCN5 chromatin positions, and it co-localizes with AP2-LT (PMID:40558503). It acts within a divergent SAGA-like complex containing PfADA2, the PHD-finger proteins PfPHD1/PfPHD2, and PfAP2-LT (PMID:15075257, PMID:15246536, PMID:31728527, PMID:34403450). Through its bromodomain GCN5 also acetylates the variant histone PfH2B.Z and maintains repressive heterochromatin: bromodomain loss de-represses heterochromatic and var genes, impairs erythrocyte invasion, and elevates sexual conversion (PMID:34403450, PMID:40156869). GCN5 additionally acts on non-histone substrates, acetylating and stabilizing the glycolytic enzymes PfGAPDH and PfPGM1 while also transcriptionally regulating PfPGM1 (PMID:31965989, PMID:40567037). Before nuclear function, GCN5 is proteolytically processed near the food vacuole by the cysteine protease Falcipain 3, a step essential for its promoter occupancy and H3K9ac activity, after which its poly-asparagine N-terminus reassociates with the catalytic domain to support acetyltransferase activity (PMID:31862795, PMID:38924147, PMID:42323337). GCN5 governs stress responses and artemisinin resistance and is required for blood-stage survival and mosquito transmission, making it a validated antimalarial target with a bromodomain amenable to selective inhibition (PMID:17449656, PMID:33441725, PMID:37702516, PMID:40156869).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2004 High

    Establishing that the Plasmodium enzyme was a bona fide, catalytically conserved histone acetyltransferase answered whether P. falciparum possesses functional chromatin-modifying machinery of the GCN5 type.

    Evidence In vitro HAT assay on free core histones with site-specific antibodies plus rescue of a yeast GCN5 deletion by the PfGCN5 HAT domain

    PMID:15075257

    Open questions at the time
    • Substrate mapping in vitro on free histones does not establish nucleosomal specificity
    • In vivo genomic targets not addressed
  2. 2004 Medium

    Identifying PfADA2 as a physical partner answered whether GCN5 operates within a multi-subunit adaptor complex rather than alone.

    Evidence Yeast two-hybrid and in vitro binding assays; reciprocal co-immunoprecipitation of a ~200 kDa HAT-active species from parasite lysate

    PMID:15075257 PMID:15246536

    Open questions at the time
    • Full complex composition not resolved
    • Stoichiometry and functional role of ADA2 in activity untested
  3. 2006 High

    Refining the substrate profile to H3K9 and H3K14 on the divergent P. falciparum H3 clarified the physiologically relevant acetylation marks despite the parasite's atypical H3 N-terminus.

    Evidence In vitro HAT assays with recombinant PfH3 and native PfGCN5, read out with acetylation-specific antibodies

    PMID:16410041

    Open questions at the time
    • Relative in vivo contribution of K9 vs K14 not partitioned
    • Non-histone substrates not yet examined
  4. 2008 High

    Genome-wide mapping and pharmacological inhibition established that GCN5 deposits promoter H3K9ac to activate transcription in a stage-specific manner, linking the enzyme to active euchromatin.

    Evidence ChIP-chip of GCN5 versus H3K9ac/H3K9me3, HAT inhibitor treatment with expression and ChIP readouts; anacardic acid and curcumin inhibition confirming substrate-specific hypoacetylation

    PMID:17145789 PMID:17449656 PMID:18487348 PMID:18692528

    Open questions at the time
    • Recruitment mechanism to specific promoters unresolved
    • Direct versus indirect expression effects not fully separated
  5. 2019 Medium

    Interaction proteomics resolved GCN5 into two distinct GCN5/ADA2 complexes, advancing the picture from a binary partnership to defined epigenetic assemblies.

    Evidence Histone peptide pull-downs and quantitative MS-based interaction proteomics with tagging

    PMID:31728527

    Open questions at the time
    • Functional distinction between the two complexes not tested
    • Subunit-specific roles unresolved
  6. 2020 Medium

    Discovery of essential proteolytic processing near the digestive vacuole before nuclear entry revealed an unexpected post-translational maturation step required for chromatin function.

    Evidence IFA, immuno-EM, cysteine protease inhibitor treatment and ChIP showing reduced promoter occupancy and H3K9ac when processing is blocked

    PMID:31862795

    Open questions at the time
    • Protease identity not established in this study
    • Cleavage sites and trafficking route mechanism unresolved
  7. 2020 Medium

    Detection of non-histone acetylation (PfGAPDH) and metabolic-enzyme interactions extended GCN5's role beyond chromatin into metabolic regulation.

    Evidence IP-MS interactome and in vitro acetylation assay

    PMID:31965989

    Open questions at the time
    • Physiological consequence of GAPDH acetylation untested
    • In vivo acetylation sites not mapped
  8. 2021 High

    Genetic domain deletions defined a divergent GCN5 HAT complex with PHD proteins and AP2-LT and demonstrated the bromodomain's requirement for invasion, sexual conversion control, and var gene regulation.

    Evidence CRISPR bromodomain/PHD deletions with invasion, sexual-conversion, RNA-seq, ChIP-seq and interaction proteomics readouts; ChIP-seq of poised stress-gene binding with inhibitor drug-sensitivity assays

    PMID:33441725 PMID:34403450

    Open questions at the time
    • Bromodomain reader ligand at heterochromatin not defined here
    • Direct AP2-LT recruitment mechanism not yet shown
  9. 2017 Low

    Structural and biophysical characterization of the bromodomain, including inhibitor co-crystallography, established it as a druggable acetyl-lysine reader module.

    Evidence X-ray co-crystal structure with inhibitor L-45; NMR binding to diacetylated H2A.Z

    PMID:27966810 PMID:28771339

    Open questions at the time
    • H2A.Z binding is very low affinity (~650 µM) with no parasite functional validation
    • In vivo bromodomain ligand not confirmed by these assays
  10. 2023 High

    Conditional knockdown established GCN5 as a controller of stress-response transcription and a modifier of artemisinin resistance, giving direct causal genetic evidence for its role.

    Evidence TetR-DOZI knockdown to ~50% with RNA-seq, ring-stage survival assays under heat/glucose/DHA stress and pharmacological inhibition

    PMID:37702516

    Open questions at the time
    • Partial knockdown may underestimate essential functions
    • Direct GCN5 targets among stress genes not fully separated from downstream effects
  11. 2024 Medium

    Identification of Falcipain 3 as the processing protease closed the mechanistic gap on GCN5's essential proteolytic maturation.

    Evidence Co-IP/LC-MS/MS, in vitro pull-down, E64d inhibition blocking processing, and confocal/EM co-localization at the food vacuole

    PMID:38924147

    Open questions at the time
    • Precise cleavage sites not mapped
    • Reconstitution of cleavage with purified FP3 not shown
  12. 2025 High

    Combined genetic deletion, chromatin mapping, and chemical phenocopy established that GCN5 both activates euchromatic promoters and maintains repressive heterochromatin through its bromodomain, and is required across blood and transmission stages.

    Evidence Conditional deletion, ChIP-seq/CUT&Tag-seq, histone-modification profiling of PfH2B.Z, AP2-motif overlap and AP2-LT co-localization, transmission assays, and L-45 phenocopy

    PMID:40156869 PMID:40558503

    Open questions at the time
    • Direct biochemical demonstration that AP2 TFs recruit GCN5 not fully resolved
    • Mechanism coupling bromodomain to heterochromatin repression not defined
  13. 2025 Medium

    Dual regulation of the glycolytic enzyme PfPGM1 (acetylation at catalytic K100 plus promoter occupancy) demonstrated that GCN5 integrates protein-level and transcriptional control of metabolism.

    Evidence In vitro acetylation, cycloheximide-chase stability, ChIP and RT-PCR/transcriptomics

    PMID:40567037

    Open questions at the time
    • Physiological impact on glycolytic flux not measured
    • In vivo K100 acetylation stoichiometry unknown
  14. 2026 Medium

    Demonstrating that the poly-asparagine N-terminus reassociates with the catalytic domain after cleavage and supports activity clarified the functional purpose of GCN5's processing and its low-complexity region.

    Evidence Genetic deletion of the poly-asparagine repeat with high-resolution MS histone profiling, western blotting and growth/stress assays

    PMID:42323337

    Open questions at the time
    • Structural basis of N-/C-domain reassociation not resolved
    • How the repeat enhances catalysis mechanistically unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How AP2-domain transcription factors physically recruit GCN5 to specific promoters, and how a single bromodomain simultaneously drives euchromatic activation and heterochromatic repression, remain unresolved.
  • No direct biochemical reconstitution of AP2-mediated GCN5 recruitment
  • Dual euchromatin/heterochromatin bromodomain mechanism undefined
  • In vivo acetyl-lysine ligand of the bromodomain not conclusively established

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
FALCIPAIN 3 (FP3, FOOD VACUOLAR CYSTEINE PROTEASE)PFADA2PFAP2-LT (AP2-DOMAIN TRANSCRIPTION FACTOR)PFGAPDH (ACETYLATION SUBSTRATE)PFPGM1 (ACETYLATION SUBSTRATE, K100)PFPHD1PFPHD2
Complex memberships
Divergent SAGA-like GCN5/ADA2 HAT complex (PfADA2)GCN5-PfPHD1/PfPHD2-PfAP2-LT complexTwo distinct GCN5/ADA2 complexes resolved by interaction proteomics

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 PfGCN5 encodes a histone acetyltransferase with conserved HAT activity that preferentially acetylates histone H3, specifically at K8 and K14, as determined using recombinant PfGCN5 and substrate-specific antibodies. The HAT domain of PfGCN5 can partially complement a yeast GCN5 deletion mutant, and a chimera containing the PfGCN5 HAT domain fused to the remainder of yeast GCN5 fully rescues the yGCN5 deletion. In vitro HAT assay with free core histones; substrate-specific antibody detection; yeast complementation assay Eukaryotic cell High 15075257
2004 PfGCN5 physically interacts with PfADA2 (the P. falciparum ADA2 homologue), as shown by yeast two-hybrid and in vitro binding assays, suggesting they associate in a complex in vivo. Yeast two-hybrid assay; in vitro binding assay Eukaryotic cell Medium 15075257
2004 Anti-GCN5 antibodies immunoprecipitate a ~200 kDa protein from parasite lysate with HAT activity similar to recombinant GCN5, and this HAT activity is also immunoprecipitated by anti-PfADA2 antibodies, demonstrating that PfADA2 is associated with PfGCN5 in vivo. Co-immunoprecipitation with HAT activity assay Gene Medium 15246536
2006 Recombinant PfGCN5 efficiently acetylates recombinant PfH3 at K9 and K14, despite divergence in the PfH3 N-terminus from mammalian homologues, and native PfGCN5 does likewise, establishing H3K9 and H3K14 as the primary in vitro substrates. In vitro HAT assay with recombinant substrates; acetylation-specific antibody detection; native PfGCN5 from parasite extracts Gene High 16410041
2006 Curcumin inhibits the HAT activity of recombinant PfGCN5 in vitro and reduces nuclear HAT activity in parasite culture, causing hypoacetylation of histone H3 at K9 and K14 but not H4 at K5, K8, K12, or K16, indicating substrate-specific inhibition of PfGCN5. In vitro HAT assay with recombinant PfGCN5; nuclear HAT activity assay from parasite extracts; acetylation-specific antibodies Antimicrobial agents and chemotherapy High 17145789
2007 Genome-wide ChIP-chip analysis shows that PfGCN5 is distributed across the P. falciparum genome with a chromosomal distribution similar to H3K9ac but distinct from H3K9me3. PfGCN5 occupancy is enriched at promoter regions of actively expressed genes in a stage-specific manner, and treatment with a PfGCN5 inhibitor reduces promoter H3K9ac and gene expression, establishing that PfGCN5 mediates H3K9ac at promoters to activate transcription. Chromatin immunoprecipitation (ChIP) coupled with DNA microarray (ChIP-chip); real-time PCR; HAT inhibitor treatment Eukaryotic cell High 17449656
2008 Anacardic acid reversibly and non-competitively inhibits HAT activity of recombinant PfGCN5 and to a lesser extent PfGCN5 in parasite nuclear extracts, without affecting histone deacetylase activity. This causes hypoacetylation of H3K9 and H3K14 (but not H4K5/K8/K12/K16) and ChIP shows reduced acetylation near promoters of downregulated genes. In vitro HAT assay; nuclear extract HAT assay; ChIP with real-time PCR; acetylation-specific antibodies; microarray Eukaryotic cell High 18487348
2008 PfGCN5 is recruited to the enhancer region of the pf1-cys-prx gene specifically during trophozoite/schizont stages, as shown by ChIP, correlating with elevated histone acetylation and stage-specific transcriptional activity. Chromatin immunoprecipitation (ChIP); reporter assay; electrophoretic mobility shift assay (EMSA); DNase I footprinting Molecular and biochemical parasitology Medium 18692528
2019 Quantitative proteomic interaction studies identify two distinct GCN5/ADA2 complexes in P. falciparum, revealing the composition of PfGCN5-containing epigenetic complexes and their interactions with other epigenetic regulatory complexes. Histone peptide pull-downs; quantitative proteomics (mass spectrometry); tagging and interaction proteomics Nucleic acids research Medium 31728527
2020 PfGCN5 undergoes novel proteolytic processing by a cysteine protease-like enzyme that is essential for its activity in vivo. The processing occurs near the digestive vacuole following trafficking through the ER-Golgi secretory pathway before PfGCN5 reaches the nucleus. Blocking processing reduces PfGCN5 occupancy at gene promoters and lowers H3K9ac at those promoters. Immunofluorescence; immuno-electron microscopy; cysteine protease inhibitor treatment; ChIP; fractionation Journal of cell science Medium 31862795
2021 PfGCN5 forms a divergent HAT complex in P. falciparum that includes two plant homeodomain (PHD) proteins (PfPHD1 and PfPHD2) and an AP2-domain transcription factor (PfAP2-LT). Deletion of the bromodomain of PfGCN5 or the PHD domain of PfPHD1 reduces merozoite invasion of erythrocytes, elevates sexual conversion, decreases H3K9 acetylation and H3K4 trimethylation, and disrupts global transcription including mutually exclusive var gene expression. CRISPR-based domain deletion; phenotypic assays (invasion, sexual conversion); RNA-seq; ChIP-seq; immunoprecipitation/proteomics PLoS pathogens High 34403450
2021 ChIP-seq shows PfGCN5 binds to stress-responsive genes (including those involved in artemisinin resistance such as BiP and TRiC chaperone) in a poised state under normal conditions, and genome-wide PfGCN5 binding sites increase upon artemisinin exposure. Inhibition of PfGCN5 increases sensitivity of artemisinin-resistant parasites to artemisinin. ChIP-seq; pharmacological inhibition of PfGCN5; growth assay/drug sensitivity assay Scientific reports Medium 33441725
2020 PfGCN5 interacts with and acetylates PfGAPDH (glyceraldehyde-3-phosphate dehydrogenase) in vitro. Immunoprecipitation coupled with mass spectrometry identifies various metabolic enzymes as PfGCN5 interacting partners, suggesting a role beyond histone acetylation. Immunoprecipitation coupled with mass spectrometry; in vitro acetylation assay Journal of biosciences Medium 31965989
2016 A co-crystal structure of the bromodomain inhibitor L-45 (L-Moses) with the PfGCN5 bromodomain was solved, rationalizing the high selectivity of the compound for PCAF and GCN5 bromodomains. X-ray co-crystallography; biophysical characterization Angewandte Chemie (International ed. in English) Medium 27966810
2017 PfGCN5 bromodomain directly binds diacetylated histone H2A.Z (at K4 and K11) with a Kd of ~650 µM, as determined by NMR-based biophysical assays. Protein-observed 19F NMR (PrOF NMR); Carr-Purcell-Meiboom-Gill NMR; photo-cross-linking Biochemistry Low 28771339
2023 Conditional knockdown of PfGCN5 to ~50% sensitizes P. falciparum to heat shock, glucose starvation, and dihydroartemisinin. RNA-seq identifies ~300-400 PfGCN5-dependent genes involved in stress responses, including ART-resistance-related genes K13 and coronin. KD or inhibition of PfGCN5 sensitizes ART-resistant parasites to DHA treatment. TetR-DOZI conditional knockdown; RNA-seq; ring-stage survival assay; pharmacological inhibition Antimicrobial agents and chemotherapy High 37702516
2024 Falcipain 3 (FP3), a food vacuolar cysteine protease, directly interacts with PfGCN5 as shown by co-immunoprecipitation and in vitro pull-down assay. Use of the cysteine protease inhibitor E64d blocks proteolytic processing of PfGCN5 and causes co-localization of PfGCN5 and FP3 around the food vacuole, identifying FP3 as the protease responsible for PfGCN5 processing. Co-immunoprecipitation followed by LC-MS/MS; in vitro pull-down assay; cysteine protease inhibitor treatment; confocal and electron microscopy Biotechnology and applied biochemistry Medium 38924147
2025 PfGCN5 is essential for parasite survival in human blood and transmission to mosquitoes. Its bromodomain (BRD) is required at euchromatic gene promoters for proper expression and for acetylation of the variant histone PfH2B.Z. Loss of the BRD de-represses heterochromatic genes and increases acetylated PfH2B.Z in heterochromatin, indicating PfGCN5 maintains repressive heterochromatin structure. The BRD-binding compound L-45 phenocopies BRD deletion. Conditional genetic knockdown/deletion; ChIP-seq; histone modification profiling; drug treatment phenocopy; gametocyte/mosquito transmission assay Nucleic acids research High 40156869
2025 PfGCN5 acetylates PfPGM1 (phosphoglycerate mutase 1) at K100, a residue critical for PfPGM1 catalytic activity, stabilizing the protein. Additionally, PfGCN5 occupies the PfPGM1 promoter in a stage-specific manner, and knockdown of PfGCN5 reduces PfPGM1 transcript levels, demonstrating dual regulation of a glycolytic enzyme at both the protein and transcriptional levels. In vitro acetylation assay; knockdown with cycloheximide treatment; ChIP; RT-PCR/transcriptomics The FEBS journal Medium 40567037
2025 Conditional knockdown of PfGCN5 phenotypically recapitulates bromodomain deletion growth defects. CUT&Tag-seq shows PfGCN5 co-localizes with H3K9ac at gene promoters, and the H3K9ac peak intensity positively correlates with levels of gene expression. PfGCN5 chromatin positions overlap with DNA sequence motifs recognized by multiple AP2 transcription factors, indicating AP2-domain TFs recruit PfGCN5 to target promoters. PfGCN5 co-localizes with AP2-LT, confirming AP2-LT as a component of the PfGCN5 complex. TetR-DOZI conditional knockdown; CUT&Tag-seq; motif analysis; colocalization analysis Cells High 40558503
2026 The poly-asparagine repeat-containing N-terminus of PfGCN5 associates with its C-terminal catalytic domain after proteolytic cleavage in the nucleus. Deletion of the poly-asparagine repeat destabilizes the N-terminal polypeptide, impairs parasite development and growth (especially under stress), and profoundly reduces acetylation of histones H3, H3.3, and H4, demonstrating that the poly-asparagine repeat contributes to PfGCN5 acetyltransferase activity in vivo. Genetic deletion; high-resolution mass spectrometry; western blotting; growth and stress assays Nature communications Medium 42323337

Source papers

Stage 0 corpus · 34 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Cytotoxic effect of curcumin on malaria parasite Plasmodium falciparum: inhibition of histone acetylation and generation of reactive oxygen species. Antimicrobial agents and chemotherapy 187 17145789
2006 The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation. Gene 155 16410041
2007 PfGCN5-mediated histone H3 acetylation plays a key role in gene expression in Plasmodium falciparum. Eukaryotic cell 97 17449656
2004 Plasmodium falciparum histone acetyltransferase, a yeast GCN5 homologue involved in chromatin remodeling. Eukaryotic cell 92 15075257
2008 Histone acetyltransferase inhibitor anacardic acid causes changes in global gene expression during in vitro Plasmodium falciparum development. Eukaryotic cell 81 18487348
2016 Discovery of a PCAF Bromodomain Chemical Probe. Angewandte Chemie (International ed. in English) 65 27966810
2019 Epigenetic reader complexes of the human malaria parasite, Plasmodium falciparum. Nucleic acids research 48 31728527
2020 Targeting histone acetylation/deacetylation in parasites: an update (2017-2020). Current opinion in chemical biology 47 32615359
2021 A unique GCN5 histone acetyltransferase complex controls erythrocyte invasion and virulence in the malaria parasite Plasmodium falciparum. PLoS pathogens 44 34403450
2004 PfADA2, a Plasmodium falciparum homologue of the transcriptional coactivator ADA2 and its in vivo association with the histone acetyltransferase PfGCN5. Gene 33 15246536
2021 Histone acetyltransferase PfGCN5 regulates stress responsive and artemisinin resistance related genes in Plasmodium falciparum. Scientific reports 23 33441725
2014 Histone H3K9 acetylation level modulates gene expression and may affect parasite growth in human malaria parasite Plasmodium falciparum. The FEBS journal 23 25252094
2017 Designing novel inhibitors against histone acetyltransferase (HAT: GCN5) of Plasmodium falciparum. European journal of medicinal chemistry 21 28644986
2017 Specific Acetylation Patterns of H2A.Z Form Transient Interactions with the BPTF Bromodomain. Biochemistry 20 28771339
2018 Activity of bromodomain protein inhibitors/binders against asexual-stage Plasmodium falciparum parasites. International journal for parasitology. Drugs and drug resistance 19 29631126
2016 Arbitrarily Accessible 3D Microfluidic Device for Combinatorial High-Throughput Drug Screening. Sensors (Basel, Switzerland) 19 27690055
2020 Plasmodium falciparum GCN5 acetyltransferase follows a novel proteolytic processing pathway that is essential for its function. Journal of cell science 15 31862795
2022 A Leak-Free Inducible CRISPRi/a System for Gene Functional Studies in Plasmodium falciparum. Microbiology spectrum 14 35510853
2020 Combined Protein- and Ligand-Observed NMR Workflow to Screen Fragment Cocktails against Multiple Proteins: A Case Study Using Bromodomains. Molecules (Basel, Switzerland) 13 32872491
2023 Plasmodium falciparum GCN5 plays a key role in regulating artemisinin resistance-related stress responses. Antimicrobial agents and chemotherapy 12 37702516
2020 Role of PfGCN5 in nutrient sensing and transcriptional regulation in Plasmodium falciparum. Journal of biosciences 12 31965989
2023 A type II protein arginine methyltransferase regulates merozoite invasion in Plasmodium falciparum. Communications biology 11 37349497
2008 5' sequence- and chromatin modification-dependent gene expression in Plasmodium falciparum erythrocytic stage. Molecular and biochemical parasitology 11 18692528
2024 PfHDAC1 is an essential regulator of P. falciparum asexual proliferation and host cell invasion genes with a dynamic genomic occupancy responsive to artemisinin stress. mBio 8 38709067
2025 PfGCN5 is essential for Plasmodium falciparum survival and transmission and regulates Pf H2B.Z acetylation and chromatin structure. Nucleic acids research 6 40156869
2022 Role of PfMYST in DNA replication in Plasmodium falciparum. Experimental parasitology 5 36228701
2024 Plasmodium falciparum cysteine protease Falcipain 3: A potential enzyme for proteolytic processing of histone acetyltransferase PfGCN5. Biotechnology and applied biochemistry 3 38924147
2025 Plasmodium falciparum acetyltransferase GCN5 acts as a dual regulator of essential glycolytic enzyme phosphoglycerate mutase. The FEBS journal 1 40567037
2026 A role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5. Nature communications 0 42323337
2026 Sense-Antisense RNA duplexes mediate stress-responsive translational control in Plasmodium falciparum. RNA (New York, N.Y.) 0 42575702
2025 Correction to 'PfGCN5 is essential for Plasmodium falciparum survival and transmission and regulates Pf H2B.Z acetylation and chromatin structure'. Nucleic acids research 0 40266688
2025 GCN5 Is a Master Regulator of Gene Expression in the Malaria Parasite Plasmodium falciparum. Cells 0 40558503
2023 Plasmodium falciparum GCN5 plays a key role in regulating artemisinin resistance-related stress responses. bioRxiv : the preprint server for biology 0 36711954
2005 Preparation and characterization of a monoclonal antibody specific to histone acetyltransferase from Plasmodium falciparum. Hybridoma (2005) 0 15857175