Affinage · Plasmodium

PKA

PF3D7_0934800 · cAMP-dependent protein kinase catalytic subunit

Annotated
2026-09-08
48 papers in source corpus 23 papers cited in narrative 24 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PKAc (PF3D7_0934800) is the catalytic subunit of cAMP-dependent protein kinase A in Plasmodium falciparum and the central effector of cAMP signaling controlling erythrocyte invasion and blood-stage proliferation (PMID:11559352, PMID:31594816, PMID:31075098). Enzymatically active PKAc is stimulated by cAMP and, unlike the mammalian enzyme, is only weakly inhibited by H89 and PKI, indicating a divergent substrate-binding architecture (PMID:18501980); its activation requires phosphorylation of activation-loop residue T189 by PfPDK1, and cAMP binding to the regulatory subunit PfPKA-R releases the catalytic subunit to phosphorylate substrates (PMID:27738107, PMID:34879056). During merozoite invasion PKAc phosphorylates the AMA1 cytoplasmic tail at S610, a cAMP-dependent priming event that licenses subsequent GSK3-mediated phosphorylation of T613, with both steps required for efficient invasion, and it additionally targets glideosome motor components myosin A, GAP45, and CDPK1 (PMID:20532217, PMID:23025827, PMID:27698395). Beyond invasion, PKAc phosphorylates erythrocyte-associated proteins including STEVOR at S324 to regulate gametocyte-infected erythrocyte deformability (PMID:25951195, PMID:27136945). PKAc activity must be temporally bounded: conditional disruption abolishes invasion and blood-stage growth (PMID:31594816, PMID:31075098), while hyperactivation through PDEβ loss, overexpression, or membrane-permeable cAMP agonists is equally lethal (PMID:27738107, PMID:30794532, PMID:34879056). In P. berghei the kinase is dispensable for pre-erythrocytic liver-stage development despite being essential for initiating blood-stage infection (PMID:31142638).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2000 Medium

    Establishing that P. falciparum encodes a single-copy PKA catalytic subunit with stage-regulated expression defined the gene as a discrete signaling component preferentially active in asexual blood stages.

    Evidence Gene cloning and expression analysis in P. falciparum

    PMID:10960174

    Open questions at the time
    • No enzymatic activity or substrate demonstrated
    • Subcellular localization not defined
  2. 2001 Medium

    Detection of cAMP-stimulated kinase activity in schizonts, and the block of intraerythrocytic development by H89, first linked PKAc enzymatic activity to blood-stage viability.

    Evidence In vitro kinase activity assay and pharmacological inhibition (H89, PKI) in P. falciparum schizonts

    PMID:11559352

    Open questions at the time
    • Pharmacological inhibitors are not PKAc-selective
    • No molecular substrate identified
  3. 2005 Medium

    Placing PKAc downstream of melatonin and in reciprocal cross-talk with Ca2+ signaling positioned the kinase within a host-hormone-responsive cell-cycle control circuit.

    Evidence cAMP analogue treatment, PKA activity assay, and pharmacological inhibitors in infected erythrocytes

    PMID:16103224

    Open questions at the time
    • Relies on pharmacological tools rather than genetic manipulation of PKAc
    • Direct PKAc substrates in this circuit not identified
  4. 2008 High

    Recombinant reconstitution of active PfPKAc, together with regulatory-subunit modulation of anion conductance and cAMP rescue of a growth defect, provided direct biochemical evidence that PKAc activity is required for normal parasite growth and behaves differently from mammalian PKA-C.

    Evidence Wheat germ cell-free expression and purification with inhibitor profiling; patch-clamp and transgenic PfPKA-R overexpression with cAMP rescue in P. falciparum

    PMID:18248092 PMID:18501980

    Open questions at the time
    • Physiological substrates not yet defined at this stage
    • Anion-conductance effects attributed to the regulatory subunit, not directly to PKAc
  5. 2009 Medium

    Loss-of-function by dsRNA knockdown and additional recombinant characterization tied PKAc depletion to schizont cell-cycle arrest and transcriptional programs enriched for invasion and calcium signaling.

    Evidence dsRNA silencing with microarray transcriptomics and E. coli-expressed recombinant kinase assays in P. falciparum

    PMID:19159956 PMID:19779742

    Open questions at the time
    • dsRNA knockdown incomplete and prone to off-target effects
    • Transcriptional changes may be indirect consequences of arrest
  6. 2010 High

    Identification of AMA1 S610 as a PKAc-dependent phosphosite whose mutation blocks invasion connected the kinase to a specific invasion ligand and a concrete molecular function.

    Evidence Site-directed mutagenesis (S610A), in vivo phosphorylation and invasion assays in P. falciparum; melatonin/Ca2+-cAMP feedback in P. chabaudi

    PMID:20532217 PMID:20964707

    Open questions at the time
    • Direct kinase-substrate assay for AMA1 not yet shown at this stage
    • Whether PKAc is the sole S610 kinase not established
  7. 2012 Medium

    Discovery of myosin A, GAP45, and CDPK1 as PKAc substrates broadened the kinase's role from a single ligand to regulation of the glideosome invasion motor.

    Evidence In vitro kinase assay with phosphoproteomics and phospho-motif analysis in P. falciparum

    PMID:23025827

    Open questions at the time
    • Individual phosphosites not confirmed by mutagenesis
    • Functional consequence of each site on motor activity not tested
  8. 2015 Medium

    Linking PKAc-dependent phosphorylation to gametocyte-infected erythrocyte stiffness extended the kinase's substrate scope to host-cell mechanical remodeling relevant to transmission stages.

    Evidence Microsphere filtration deformability assays with PDE-inhibitor cAMP elevation and PKA activity measurement in P. falciparum

    PMID:25951195

    Open questions at the time
    • Specific PKAc substrates driving deformability not identified in this study
    • Pharmacological cAMP elevation not gene-specific
  9. 2016 High

    Resolving a hierarchical AMA1 phosphorylation cascade, identifying STEVOR S324 as a substrate, and solving the PfPKA-R:cAMP structure together defined how cAMP release of PKAc drives sequential invasion phosphorylation and host-cell modification, and revealed that hyperactivation is as damaging as inhibition.

    Evidence In vitro kinase assays, phosphosite mutagenesis and invasion assays; IP-mass spectrometry and microsphiltration; X-ray crystallography of PfPKA-R with cAMP analogues in P. falciparum

    PMID:27136945 PMID:27698395 PMID:27738107

    Open questions at the time
    • No crystal structure of the catalytic subunit itself
    • Mechanism coupling PKAc priming to GSK3 recruitment not defined
  10. 2017 Medium

    Demonstrating that CDPK1 phosphorylates the regulatory subunit PfPKA-R established a direct molecular node of cross-talk between Ca2+- and cAMP-dependent kinase signaling upstream of PKAc.

    Evidence Comparative phosphoproteomics, conditional knockdown, and in vitro kinase assay in P. falciparum

    PMID:28680058

    Open questions at the time
    • Functional impact of PfPKA-R phosphorylation on PKAc release not quantified
    • Reciprocal regulation (PKAc phosphorylating CDPK1) noted earlier but its integration unclear
  11. 2019 High

    Conditional genetic disruption across species resolved PKAc as strictly essential for erythrocyte invasion and blood-stage growth (via AMA1 S610 phosphorylation) but dispensable for liver-stage development, and defined tight temporal control of its activation as itself essential.

    Evidence DiCre conditional deletion in P. falciparum with phospho-immunoblot and invasion assays; ACβ/PKAc disruption with phosphoproteomics; PDEβ disruption showing lethal hyperactivation; sporozoite-stage KO in P. berghei

    PMID:30794532 PMID:31075098 PMID:31142638 PMID:31594816

    Open questions at the time
    • Full in vivo PKAc substrate set only partially assigned from phosphoproteomes
    • Basis of species/stage-specific dispensability in liver stages unexplained
  12. 2021 High

    Identifying PfPDK1 as the activation-loop (T189) kinase for PKAc, and confirming lethal overexpression and a gametocyte-deformability role, established the upstream activation mechanism and reinforced that PKAc dosage must be balanced.

    Evidence Conditional knockdown, PKAc overexpression selection with whole-genome sequencing, and T189 mutagenesis in P. falciparum; DiCre KO with AMA1 secretion readouts in P. yoelii

    PMID:34390881 PMID:34879056

    Open questions at the time
    • P. yoelii shows impaired AMA1 secretion whereas P. falciparum studies did not report this defect, indicating unresolved species divergence in how PKAc loss affects AMA1
    • How PfPDK1 access to PKAc is temporally controlled not defined
  13. 2024 Medium

    Placing PKAc upstream of the phosphatase PP7 in ring-stage development, and recovering PKAc/PfPDK1/PfPKA-R resistance mutations against PDE inhibitors, defined downstream signaling architecture and confirmed PKAc as the direct effector of PDEβ-regulated cAMP.

    Evidence Conditional disruption with phosphoproteomics (PP7); in vitro PDE-inhibitor resistance selection with whole-genome sequencing in P. falciparum

    PMID:39387582 PMID:39642214

    Open questions at the time
    • Direct PP7-PKAc substrate opposition not biochemically reconstituted
    • How PKAc distinguishes invasion versus ring-stage substrate programs unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How PKAc achieves substrate and temporal selectivity — the full in vivo substrate repertoire, the structural basis of its divergent inhibitor profile, and what confines its activity to invasion versus ring-stage and gametocyte programs — remains unresolved.
  • No crystal structure of the catalytic subunit
  • Complete validated in vivo substrate set not defined
  • Mechanistic basis of species/stage-specific requirements not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
ADENYLYL CYCLASE BETA / PDEΒ (CAMP-REGULATING ENZYMES UPSTREAM) [#16, #17, #23]AMA1 (SUBSTRATE, S610) [#7, #11, #15]GSK3 (DOWNSTREAM AMA1 T613 KINASE) [#11]MYOSIN A, GAP45, CDPK1 (GLIDEOSOME SUBSTRATES; CDPK1 ALSO PHOSPHORYLATES PFPKA-R) [#9, #14]PFPDK1 (ACTIVATION-LOOP T189 KINASE) [#19, #23]PFPKA-R (REGULATORY SUBUNIT) [#3, #13, #14]PP7 (DOWNSTREAM PHOSPHATASE SUBSTRATE) [#22]STEVOR (SUBSTRATE, S324) [#12]
Complex memberships
cAMP-dependent protein kinase (PKA) holoenzyme with regulatory subunit PfPKA-R [#3, #13, #14]

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 PKAc (PF3D7_0934800) gene was isolated and characterized from P. falciparum; it exists as a single copy gene and its expression is developmentally regulated, with higher levels in asexual blood stages than in sexual forms. Gene cloning, expression analysis Molecular and biochemical parasitology Medium 10960174
2001 PKAc (PF3D7_0934800) activity is detectable in P. falciparum schizonts; it can be stimulated by cAMP and inhibited by protein kinase inhibitor (PKI), and its inhibition by H89 blocks intraerythrocytic parasite development. In vitro kinase activity assay, pharmacological inhibition (H89, PKI) European journal of biochemistry Medium 11559352
2005 Melatonin induces an increase in cAMP levels and PKAc activity (~40–50%) in P. falciparum-infected erythrocytes, and PKAc activation mediates melatonin-induced cell cycle alteration; a cross-talk exists whereby cAMP/PKAc activation raises cytosolic Ca2+, and Ca2+-dependent pathways (via PLC) regulate cAMP increases. cAMP analogue treatment, PKA activity assay, pharmacological inhibitors (H89, PKI, 6-Bz-cAMP, U73122) The Journal of cell biology Medium 16103224
2008 The regulatory subunit of PKA (PfPKA-R) modulates anion conductance in P. falciparum-infected erythrocytes: addition of recombinant PfPKA-R in patch-clamp experiments or overexpression of PfPKA-R in transgenic parasites down-regulates anion channel activity, and this overexpression strain has a growth defect rescued by elevated intracellular cAMP, indicating PKAc activity is required for normal parasite growth. Patch-clamp electrophysiology, transgenic parasite overexpression, cAMP rescue experiment PLoS pathogens Medium 18248092
2008 Recombinant PKAc catalytic subunit (PfPKAc) was purified using a wheat germ cell-free expression system and shown to be enzymatically active; unlike mammalian PKA-C, PfPKAc is only weakly inhibited by H89 and slightly inhibited by PKI, indicating its substrate-binding sites differ from mammalian counterparts. Wheat germ cell-free expression, protein purification, in vitro kinase assay with inhibitors Molecular and biochemical parasitology High 18501980
2009 dsRNA-mediated knockdown of PfPKAc mRNA in P. falciparum caused morphological changes in schizonts and cell cycle arrest, accompanied by a compensatory decrease in PfPKAr mRNA; transcriptomic analysis showed altered expression of 329 genes, particularly those in merozoite invasion processes, calcium/calmodulin signaling, kinase networks, and mitochondrial functions. dsRNA gene silencing, microarray transcriptomics Parasitology research Medium 19779742
2009 Recombinant PfPKAc was overexpressed in E. coli and purified, and its enzymatic properties were determined using a fluorogenic kinase assay, establishing biochemical parameters suitable for inhibitor screening. Recombinant protein expression in E. coli, purification, fluorogenic in vitro kinase assay Parasitology research Medium 19159956
2010 PKAc activity phosphorylates the cytoplasmic tail of AMA1 at serine 610 (S610); mutation of AMA1 S610 to alanine abolishes phosphorylation in vivo and dramatically impedes erythrocyte invasion, establishing PKAc as the kinase responsible for this phosphorylation event. Site-directed mutagenesis, in vivo phosphorylation assay, invasion assay PLoS pathogens High 20532217
2010 In P. chabaudi, melatonin triggers cAMP production and PKA activation; this cAMP/PKA activation is dependent on prior Ca2+ elevation (blocked by BAPTA), and in turn cAMP application evokes Ca2+ signals, establishing bidirectional positive feedback between Ca2+ and cAMP/PKAc pathways; PKAc activation was essential for melatonin-induced increase in parasitemia. cAMP measurement, PKA activity assay, Ca2+ chelation (BAPTA), pharmacological stimulation Journal of pineal research Medium 20964707
2012 In vitro kinase assays identified three novel PKAc substrates associated with the glideosome motor complex: myosin A, GAP45, and CDPK1, establishing PKAc involvement in regulating the invasion motor complex via cAMP-dependent phosphorylation. In vitro kinase assay, phosphoproteomics, phospho-motif analysis Journal of proteome research Medium 23025827
2015 PKAc-mediated phosphorylation of gametocyte-infected erythrocyte proteins contributes to stiffness of immature gametocytes; pharmacological elevation of cAMP (mimicking PKAc hyperactivation) renders mature stage V gametocytes less deformable, establishing that parasite PKAc activity contributes to GIE mechanical properties. Microsphere filtration assay, phosphodiesterase inhibitor treatment, PKA activity measurement PLoS pathogens Medium 25951195
2016 PKAc phosphorylates AMA1 at S610 in a cAMP-dependent priming step, which then enables subsequent phosphorylation of a conserved downstream threonine (T613) by GSK3; both phosphorylation steps are required for efficient erythrocyte invasion, establishing a hierarchical, sequential phosphorylation cascade on AMA1 regulated by PKAc. In vitro kinase assay, site-directed mutagenesis, invasion assay Scientific reports High 27698395
2016 PKAc-mediated phosphorylation of the STEVOR C-terminal domain at serine S324 regulates gametocyte-infected erythrocyte deformability; this was demonstrated using immunoprecipitation and mass spectrometry, establishing STEVOR as a PKAc substrate involved in host cell mechanical modification. Immunoprecipitation, mass spectrometry, microsphiltration, phosphorylation assay Blood Medium 27136945
2016 Crystal structure of the PfPKA regulatory subunit (PfPKA-R) in complex with cAMP and (Sp)-2-Cl-cAMPS was solved; structurally, cAMP binding to PfPKA-R stabilizes a conformation that releases PKAc from inhibition, allowing it to phosphorylate substrates such as AMA1; uncontrolled induction of PKAc activity via membrane-permeable cAMP agonists is equally disruptive to parasite growth as inhibition. X-ray crystallography, cAMP analogue binding, parasite growth assay with cAMP agonists The Journal of biological chemistry High 27738107
2017 PfCDPK1 phosphorylates the PKA regulatory subunit (PfPKA-R) and thereby regulates PKAc activity in P. falciparum, establishing a cross-talk mechanism between Ca2+-dependent and cAMP-dependent kinase signaling relevant to invasion. Comparative phosphoproteomics, conditional knockdown, in vitro kinase assay Nature communications Medium 28680058
2019 Conditional disruption of PKAc (PF3D7_0934800) via DiCre-mediated excision in P. falciparum results in complete loss of PKAc protein, severe reduction in intraerythrocytic growth after one cycle, and a pronounced invasion defect; PKAc-null parasites fail to phosphorylate AMA1 at S610 in vivo, confirming PKAc as the kinase responsible for this event. CRISPR-Cas9 gene editing, DiCre conditional gene deletion, live imaging, phospho-specific immunoblot, invasion assay mBio High 31594816
2019 Conditional disruption of both adenylyl cyclase beta (ACβ) and PKAc in P. falciparum demonstrates that cAMP production and PKAc activity are critical specifically for erythrocyte invasion; PKAc-dependent phosphorylation of AMA1 cytoplasmic domain regulates invasion; numerous cAMP/PKAc-dependent phosphorylation sites were identified by phosphoproteomics. Conditional gene disruption, phosphoproteomics, invasion assay PLoS biology High 31075098
2019 Hyperactivation of PKAc caused by conditional gene disruption of PfPDEβ (leading to elevated cAMP) causes a profound reduction in erythrocyte invasion and rapid death of invaded merozoites; phosphoproteomic analysis of PDEβ-null parasites showed >2-fold increase in phosphorylation at over 200 sites, more than half conforming to PKAc substrate consensus, establishing that temporal regulation of PKAc activation by PDEβ is essential. Conditional gene disruption, phosphoproteomics, invasion and growth assay PLoS biology High 30794532
2019 PKAc (PF3D7_0934800) is dispensable for pre-erythrocytic stages in P. berghei: conditional PKAc gene disruption in sporozoites showed that mutant sporozoites can glide, invade hepatocytes, and mature into hepatic merozoites released from merosomes, but fail to initiate blood stage infection, demonstrating PKAc is not required for liver stage development. Conditional gene disruption in P. berghei sporozoites, gliding assay, hepatocyte invasion and development assay Life science alliance High 31142638
2021 PfPDK1 (3-phosphoinositide-dependent protein kinase-1) is required to activate PKAc in P. falciparum; whole-genome sequencing of parasites selected to tolerate PKAc overexpression identified missense mutations exclusively in PfPDK1; targeted mutagenesis demonstrated that PfPDK1 phosphorylates T189 in the PKAc activation loop to activate the kinase. Conditional PKAc knockdown, whole-genome sequencing, targeted mutagenesis of T189, PKAc overexpression selection PLoS biology High 34879056
2021 Conditional knockdown of PKAc in P. falciparum confirms its essential role in erythrocyte invasion by merozoites, and additionally shows that PKAc is involved in regulating gametocyte deformability; overexpression of PKAc is lethal and kills parasites at the early phase of schizogony. Conditional PKAc knockdown, PKAc overexpression, deformability assay, growth assay PLoS biology High 34879056
2021 PKAc disruption in P. yoelii (DiCre-loxP inducible KO) caused severe growth and erythrocyte invasion defects, and impaired secretion of AMA1 to the merozoite surface, while secretions of PyEBL, Py235, and RON2 were not affected by PKAc loss. DiCre-loxP conditional knockout, invasion assay, IFA for secretion of AMA1 and other ligands Parasitology international Medium 34390881
2024 PP7, identified as a high-confidence PKAc substrate by phosphoproteomics, is dispensable for erythrocyte invasion but essential for early ring-stage development; phosphoproteomic analysis of PP7-null parasites revealed that PP7 may regulate certain PKAc substrates, placing PKAc upstream of PP7 in a signaling network controlling ring-stage development. Conditional gene disruption, phosphoproteomics, invasion and ring-stage development assay mBio Medium 39387582
2024 In vitro drug resistance selection with PDE inhibitors generated P. falciparum parasites with mutations in either the catalytic or regulatory subunits of PKA, or in PfPDK1, but not in PDEβ itself, confirming that PKAc (and its upstream activator PfPDK1 and its regulatory subunit) are direct downstream effectors of PDEβ-regulated cAMP signaling. In vitro drug selection, whole-genome sequencing of resistant parasites Science advances Medium 39642214

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC genomics 421 15479470
2012 The Plasmodium falciparum schizont phosphoproteome reveals extensive phosphatidylinositol and cAMP-protein kinase A signaling. Journal of proteome research 113 23025827
2005 Cyclic AMP and calcium interplay as second messengers in melatonin-dependent regulation of Plasmodium falciparum cell cycle. The Journal of cell biology 113 16103224
2010 Protein kinase a dependent phosphorylation of apical membrane antigen 1 plays an important role in erythrocyte invasion by the malaria parasite. PLoS pathogens 112 20532217
2002 A stretch-activated anion channel is up-regulated by the malaria parasite Plasmodium falciparum. The Journal of physiology 87 12154179
2017 PfCDPK1 mediated signaling in erythrocytic stages of Plasmodium falciparum. Nature communications 84 28680058
2001 The H89 cAMP-dependent protein kinase inhibitor blocks Plasmodium falciparum development in infected erythrocytes. European journal of biochemistry 84 11559352
2015 Identification of potent phosphodiesterase inhibitors that demonstrate cyclic nucleotide-dependent functions in apicomplexan parasites. ACS chemical biology 82 25555060
2008 Plasmodium falciparum regulatory subunit of cAMP-dependent PKA and anion channel conductance. PLoS pathogens 69 18248092
2017 Cyclic nucleotide signalling in malaria parasites. Open biology 59 29263246
2019 Cyclic AMP signalling controls key components of malaria parasite host cell invasion machinery. PLoS biology 58 31075098
2015 cAMP-Signalling Regulates Gametocyte-Infected Erythrocyte Deformability Required for Malaria Parasite Transmission. PLoS pathogens 55 25951195
2019 Protein Kinase A Is Essential for Invasion of Plasmodium falciparum into Human Erythrocytes. mBio 52 31594816
2015 Extensive differential protein phosphorylation as intraerythrocytic Plasmodium falciparum schizonts develop into extracellular invasive merozoites. Proteomics 52 25886026
2011 Impairment of the Plasmodium falciparum erythrocytic cycle induced by angiotensin peptides. PloS one 52 21364758
2019 Phosphodiesterase beta is the master regulator of cAMP signalling during malaria parasite invasion. PLoS biology 40 30794532
2016 Plasmodium falciparum STEVOR phosphorylation regulates host erythrocyte deformability enabling malaria parasite transmission. Blood 40 27136945
2000 Isolation and characterisation of a cAMP-dependent protein kinase catalytic subunit gene from Plasmodium falciparum. Molecular and biochemical parasitology 37 10960174
2010 Melatonin triggers PKA activation in the rodent malaria parasite Plasmodium chabaudi. Journal of pineal research 36 20964707
2012 Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic target. Microbes and infection 35 22626931
2010 cAMP-dependent protein kinase from Plasmodium falciparum: an update. Parasitology 34 20663247
2016 Hierarchical phosphorylation of apical membrane antigen 1 is required for efficient red blood cell invasion by malaria parasites. Scientific reports 29 27698395
2013 Malaria proteomics: insights into the parasite-host interactions in the pathogenic space. Journal of proteomics 27 24140976
2017 The potential use of melatonin to treat protozoan parasitic infections: A review. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 24 29136773
2008 Susceptibility of Plasmodium falciparum cyclic AMP-dependent protein kinase and its mammalian homologue to the inhibitors. Molecular and biochemical parasitology 23 18501980
2001 Reversal of type 2 diabetes in mice by products of malaria parasites. II. Role of inositol phosphoglycans (IPGs). Molecular genetics and metabolism 23 11461192
2019 PKAc is not required for the preerythrocytic stages of Plasmodium berghei. Life science alliance 20 31142638
1995 Cloning and structural analysis of the gene for cAMP-dependent protein kinase catalytic subunit from Plasmodium yoelii. Biochimica et biophysica acta 20 7578264
2021 The 3-phosphoinositide-dependent protein kinase 1 is an essential upstream activator of protein kinase A in malaria parasites. PLoS biology 18 34879056
2020 cAMP signalling and its role in host cell invasion by malaria parasites. Current opinion in microbiology 17 33032143
2016 Plasmodiumfalciparum infection induces dynamic changes in the erythrocyte phospho-proteome. Blood cells, molecules & diseases 16 27067487
2016 Interaction between bradykinin B2 and Ang-(1-7) Mas receptors regulates erythrocyte invasion by Plasmodium falciparum. Biochimica et biophysica acta 14 27431603
2009 Phenotypic and transcriptomic analyses of Plasmodium falciparum protein kinase A catalytic subunit inhibition. Parasitology research 14 19779742
2016 Antimalarial activity of novel 4-cyano-3-methylisoquinoline inhibitors against Plasmodium falciparum: design, synthesis and biological evaluation. Organic & biomolecular chemistry 13 27105169
2016 Disrupting the Allosteric Interaction between the Plasmodium falciparum cAMP-dependent Kinase and Its Regulatory Subunit. The Journal of biological chemistry 13 27738107
2023 miR-34c-3p Regulates Protein Kinase A Activity Independent of cAMP by Dicing prkar2b Transcripts in Theileria annulata-Infected Leukocytes. mSphere 9 36847534
2016 PKA and Apicomplexan Parasite Diseases. Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme 9 27835919
2012 Correlation between structure, retention, property, and activity of biologically relevant 1,7-bis(aminoalkyl)diazachrysene derivatives. Journal of pharmaceutical and biomedical analysis 8 22985530
2022 The Potential Role of the Serotonin Transporter as a Drug Target against Parasitic Infections: A Scoping Review of the Literature. Recent advances in anti-infective drug discovery 6 35249526
2021 cAMP-Dependent Signaling Pathways as Potential Targets for Inhibition of Plasmodium falciparum Blood Stages. Frontiers in microbiology 6 34108954
2016 Characterization of an A-kinase anchoring protein-like suggests an alternative way of PKA anchoring in Plasmodium falciparum. Malaria journal 6 27129434
2020 Targeting Plasmodium with constrained peptides and peptidomimetics. IUBMB life 5 32037730
2021 Molecular basis of synchronous replication of malaria parasites in the blood stage. Current opinion in microbiology 4 34428626
2009 Expression and biochemical characterization of the Plasmodium falciparum protein kinase A catalytic subunit. Parasitology research 4 19159956
2024 Inhibitors of malaria parasite cyclic nucleotide phosphodiesterases block asexual blood-stage development and mosquito transmission. Science advances 3 39642214
2024 Plasmodium falciparum protein phosphatase PP7 is required for early ring-stage development. mBio 2 39387582
2021 cAMP-dependent protein kinase regulates secretion of apical membrane antigen 1 (AMA1) in Plasmodium yoelii. Parasitology international 1 34390881
2025 Plasmodium falciparum PP1 phosphatase is a key regulator of malaria parasite transmission. mBio 0 40823845