{"gene":"PF3D7_0818200","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2013,"finding":"Recombinant PF3D7_0818200 (Pf14-3-3I) protein binds purified parasite histones, and using a battery of H3-specific phosphopeptides, was shown to preferentially bind histone H3S28ph over H3S10ph, independent of modification of neighbouring residues (H3S10phK14ac and H3S28phS32ph), identifying it as a histone H3 phosphorylation reader.","method":"Recombinant protein binding assay with purified parasite histones; phosphopeptide binding assays with H3-specific phosphopeptides; in silico structural analysis confirming conservation of binding residues","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 1–2 / Weak — in vitro biochemical binding with multiple phosphopeptides and structural analysis, but single lab, no mutagenesis validation of binding residues","pmids":["23308157"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"finding":"PF3D7_0818200 (Pf14-3-3I) binds phosphorylated PfPKAr and PfCDPK1 to mediate assembly of a multiprotein signaling complex in P. falciparum merozoites; disruption of this complex with a phospho-peptide (P1) based on Ca2+-dependent phosphosites of PKAr inhibits microneme secretion and RBC invasion.","method":"Coimmunoprecipitation, gel filtration chromatography, competitive phospho-peptide displacement, microneme secretion assay, RBC invasion assay","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP plus gel filtration plus functional disruption assay (microneme secretion and invasion), multiple orthogonal methods in one study","pmids":["32817103"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"finding":"PF3D7_0818200 (Pf14-3-3I) interacts with PfCDPK1 in a phosphorylation-dependent manner via a canonical Mode I-type (RXXpS/pT) binding motif (CDPK1 sequence 61KLGpS64), with a binding affinity constant of 670 ± 3.6 nM, and this interaction marginally enhances CDPK1 kinase activity.","method":"Molecular dynamics simulation, ELISA, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), kinase activity assay; peptidomimetic antagonists showing parasite growth inhibition","journal":"The Biochemical journal","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — multiple orthogonal biophysical methods (SPR, ITC, ELISA) plus MD simulation and functional kinase assay in a single study","pmids":["32484216"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2016,"finding":"PF3D7_0818200 (Pf14-3-3I) binds and colocalizes with PfAKAL (an AKAP-like protein), and in turn interacts with PfPKA-R; PF3D7_0818200 is phosphorylated in vitro by PKA, whereas PfAKAL is not, suggesting phosphorylation-regulated assembly of the PfAKAL–Pf14-3-3I–PfPKA-R complex.","method":"Pull-down experiments with recombinant proteins and parasite extracts, immunofluorescence colocalization, radiolabel kinase activity assay (in vitro PKA phosphorylation), proteomic approaches","journal":"Malaria journal","confidence":"Medium","confidence_rationale":"Tier 2–3 / Weak — pull-down plus colocalization plus in vitro phosphorylation assay, but single lab and limited mechanistic follow-up","pmids":["27129434"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]}],"current_model":"PF3D7_0818200 (14-3-3I) functions as a phosphorylation-dependent scaffold protein in P. falciparum that reads histone H3S28ph to regulate nuclear processes, and assembles a merozoite signaling complex by binding phosphorylated PfCDPK1 (via a Mode I RXXpS motif, Kd ~670 nM) and phosphorylated PfPKAr, with disruption of this complex blocking microneme secretion and red blood cell invasion; it is itself phosphorylated by PKA and mediates indirect association between PfAKAL and PfPKA-R."},"narrative":{"mechanistic_narrative":"PF3D7_0818200 (14-3-3I) is a phosphorylation-dependent scaffold protein of P. falciparum that reads phosphorylated ligands to organize both nuclear and merozoite signaling processes [PMID:23308157, PMID:32817103]. In the nucleus it acts as a histone modification reader, binding recombinant parasite histones and preferentially recognizing histone H3S28ph over H3S10ph independent of neighboring modifications [PMID:23308157]. At the invasive stage it assembles a multiprotein merozoite signaling complex by binding phosphorylated PfCDPK1 and phosphorylated PfPKAr, and disruption of this complex with a phosphopeptide based on the Ca2+-dependent phosphosites of PKAr blocks microneme secretion and red blood cell invasion [PMID:32817103]. Its interaction with PfCDPK1 is a canonical Mode I (RXXpS/pT) engagement of the CDPK1 phosphosite 61KLGpS64 with an affinity of ~670 nM, and this binding marginally enhances CDPK1 kinase activity [PMID:32484216]. PF3D7_0818200 also binds and colocalizes with the AKAP-like protein PfAKAL and bridges it to PfPKA-R; it is itself phosphorylated in vitro by PKA whereas PfAKAL is not, implying phosphorylation-regulated assembly of the PfAKAL–PF3D7_0818200–PfPKA-R complex [PMID:27129434]. Beyond these scaffolding and reader roles, no further mechanistic detail has been characterized in the available corpus.","teleology":[{"year":2013,"claim":"Established that PF3D7_0818200 is a nuclear phosphorylation reader, addressing whether a parasite 14-3-3 protein could decode histone phosphomarks.","evidence":"Recombinant protein binding to purified parasite histones and a panel of H3 phosphopeptides, with in silico analysis of binding residues","pmids":["23308157"],"confidence":"Medium","gaps":["Binding residues were not validated by mutagenesis","The downstream chromatin or transcriptional consequence of H3S28ph reading was not defined","Shown only in vitro; nuclear recruitment in living parasites not demonstrated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"claim":"Identified PF3D7_0818200 as a bridge in a PKA-associated complex, answering how an AKAP-like anchoring protein connects to the PKA regulatory subunit.","evidence":"Pull-downs with recombinant proteins and parasite extracts, immunofluorescence colocalization, and in vitro radiolabel PKA phosphorylation assay","pmids":["27129434"],"confidence":"Medium","gaps":["Single-lab pull-down with limited mechanistic follow-up","Functional consequence of the PfAKAL–PF3D7_0818200–PfPKA-R complex not established","Whether PKA phosphorylation of PF3D7_0818200 gates complex assembly was not directly tested"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2020,"claim":"Defined PF3D7_0818200 as the organizer of a merozoite invasion-signaling complex, showing that its scaffolding of phospho-PfPKAr and phospho-PfCDPK1 is functionally required for invasion.","evidence":"Reciprocal co-immunoprecipitation, gel filtration, competitive phosphopeptide displacement, and microneme secretion and RBC invasion assays","pmids":["32817103"],"confidence":"High","gaps":["The phosphopeptide disruption is pharmacological; genetic ablation of PF3D7_0818200 binding not shown","Temporal ordering of complex assembly during invasion not resolved","Full composition of the merozoite complex beyond the named partners not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"claim":"Resolved the molecular grammar and affinity of the PF3D7_0818200–PfCDPK1 interaction and its effect on kinase activity, providing a druggable interface.","evidence":"Molecular dynamics simulation with SPR, ITC and ELISA affinity measurements, kinase activity assay, and peptidomimetic antagonist growth-inhibition tests","pmids":["32484216"],"confidence":"High","gaps":["The mechanism by which binding enhances CDPK1 activity is only marginal and mechanistically undefined","Cellular relevance of the 670 nM affinity during native signaling not established","Selectivity of peptidomimetic antagonists over sibling 14-3-3 members not characterized"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":null,"claim":"It remains unknown how the nuclear histone-reading role and the cytoplasmic merozoite signaling-scaffold role of PF3D7_0818200 are coordinated across the parasite life cycle.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No genetic loss-of-function study connecting the two functional modules","No structural model of PF3D7_0818200 bound to its native partners in the parasite","Regulation of PF3D7_0818200 phosphorylation state in vivo not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PfAKAL–PF3D7_0818200–PfPKA-R complex [#3]","Merozoite signaling complex with phospho-PfPKAr and phospho-PfCDPK1 [#1]"],"partners":["HISTONE H3 (H3S28PH) [#0]","PFCDPK1 (VIA 61KLGPS64 MODE I MOTIF, KD ~670 NM) [#2]","PFPKAR / PFPKA-R [#1, #3]","PFAKAL (AKAP-LIKE PROTEIN) [#3]"],"other_free_text":["Interaction with PfCDPK1 uses a canonical Mode I (RXXpS/pT) phosphopeptide-binding mode [#2]","PF3D7_0818200 is itself a PKA substrate in vitro, whereas its partner PfAKAL is not [#3]","Phosphopeptide (P1) and peptidomimetic antagonists disrupting its complexes inhibit microneme secretion, invasion, and parasite growth [#1, #2]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"23308157","id":"PMC_23308157","title":"Comprehensive histone phosphorylation analysis and identification of Pf14-3-3 protein as a histone H3 phosphorylation reader in malaria parasites.","date":"2013","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/23308157","citation_count":31,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32817103","id":"PMC_32817103","title":"Phosphorylation-Dependent Assembly of a 14-3-3 Mediated Signaling Complex during Red Blood Cell Invasion by Plasmodium falciparum Merozoites.","date":"2020","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/32817103","citation_count":12,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32484216","id":"PMC_32484216","title":"Molecular dynamics simulations and biochemical characterization of Pf14-3-3 and PfCDPK1 interaction towards its role in growth of human malaria parasite.","date":"2020","source":"The Biochemical journal","url":"https://pubmed.ncbi.nlm.nih.gov/32484216","citation_count":10,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["14-3-3I"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"27129434","id":"PMC_27129434","title":"Characterization of an A-kinase anchoring protein-like suggests an alternative way of PKA anchoring in Plasmodium falciparum.","date":"2016","source":"Malaria journal","url":"https://pubmed.ncbi.nlm.nih.gov/27129434","citation_count":6,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["14-3-3 protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5772,"output_tokens":1406,"usd":0.019203,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6270,"output_tokens":2848,"usd":0.051275,"stage2_stop_reason":"end_turn"},"total_usd":0.070478,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"Recombinant PF3D7_0818200 (Pf14-3-3I) protein binds purified parasite histones, and using a battery of H3-specific phosphopeptides, was shown to preferentially bind histone H3S28ph over H3S10ph, independent of modification of neighbouring residues (H3S10phK14ac and H3S28phS32ph), identifying it as a histone H3 phosphorylation reader.\",\n      \"method\": \"Recombinant protein binding assay with purified parasite histones; phosphopeptide binding assays with H3-specific phosphopeptides; in silico structural analysis confirming conservation of binding residues\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1–2 / Weak — in vitro biochemical binding with multiple phosphopeptides and structural analysis, but single lab, no mutagenesis validation of binding residues\",\n      \"pmids\": [\"23308157\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"PF3D7_0818200 (Pf14-3-3I) binds phosphorylated PfPKAr and PfCDPK1 to mediate assembly of a multiprotein signaling complex in P. falciparum merozoites; disruption of this complex with a phospho-peptide (P1) based on Ca2+-dependent phosphosites of PKAr inhibits microneme secretion and RBC invasion.\",\n      \"method\": \"Coimmunoprecipitation, gel filtration chromatography, competitive phospho-peptide displacement, microneme secretion assay, RBC invasion assay\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus gel filtration plus functional disruption assay (microneme secretion and invasion), multiple orthogonal methods in one study\",\n      \"pmids\": [\"32817103\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"PF3D7_0818200 (Pf14-3-3I) interacts with PfCDPK1 in a phosphorylation-dependent manner via a canonical Mode I-type (RXXpS/pT) binding motif (CDPK1 sequence 61KLGpS64), with a binding affinity constant of 670 ± 3.6 nM, and this interaction marginally enhances CDPK1 kinase activity.\",\n      \"method\": \"Molecular dynamics simulation, ELISA, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), kinase activity assay; peptidomimetic antagonists showing parasite growth inhibition\",\n      \"journal\": \"The Biochemical journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — multiple orthogonal biophysical methods (SPR, ITC, ELISA) plus MD simulation and functional kinase assay in a single study\",\n      \"pmids\": [\"32484216\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"PF3D7_0818200 (Pf14-3-3I) binds and colocalizes with PfAKAL (an AKAP-like protein), and in turn interacts with PfPKA-R; PF3D7_0818200 is phosphorylated in vitro by PKA, whereas PfAKAL is not, suggesting phosphorylation-regulated assembly of the PfAKAL–Pf14-3-3I–PfPKA-R complex.\",\n      \"method\": \"Pull-down experiments with recombinant proteins and parasite extracts, immunofluorescence colocalization, radiolabel kinase activity assay (in vitro PKA phosphorylation), proteomic approaches\",\n      \"journal\": \"Malaria journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Weak — pull-down plus colocalization plus in vitro phosphorylation assay, but single lab and limited mechanistic follow-up\",\n      \"pmids\": [\"27129434\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0818200 (14-3-3I) functions as a phosphorylation-dependent scaffold protein in P. falciparum that reads histone H3S28ph to regulate nuclear processes, and assembles a merozoite signaling complex by binding phosphorylated PfCDPK1 (via a Mode I RXXpS motif, Kd ~670 nM) and phosphorylated PfPKAr, with disruption of this complex blocking microneme secretion and red blood cell invasion; it is itself phosphorylated by PKA and mediates indirect association between PfAKAL and PfPKA-R.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"PF3D7_0818200 (14-3-3I) is a phosphorylation-dependent scaffold protein of P. falciparum that reads phosphorylated ligands to organize both nuclear and merozoite signaling processes [#0, #1]. In the nucleus it acts as a histone modification reader, binding recombinant parasite histones and preferentially recognizing histone H3S28ph over H3S10ph independent of neighboring modifications [#0]. At the invasive stage it assembles a multiprotein merozoite signaling complex by binding phosphorylated PfCDPK1 and phosphorylated PfPKAr, and disruption of this complex with a phosphopeptide based on the Ca2+-dependent phosphosites of PKAr blocks microneme secretion and red blood cell invasion [#1]. Its interaction with PfCDPK1 is a canonical Mode I (RXXpS/pT) engagement of the CDPK1 phosphosite 61KLGpS64 with an affinity of ~670 nM, and this binding marginally enhances CDPK1 kinase activity [#2]. PF3D7_0818200 also binds and colocalizes with the AKAP-like protein PfAKAL and bridges it to PfPKA-R; it is itself phosphorylated in vitro by PKA whereas PfAKAL is not, implying phosphorylation-regulated assembly of the PfAKAL\\u2013PF3D7_0818200\\u2013PfPKA-R complex [#3]. Beyond these scaffolding and reader roles, no further mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Established that PF3D7_0818200 is a nuclear phosphorylation reader, addressing whether a parasite 14-3-3 protein could decode histone phosphomarks.\",\n      \"evidence\": \"Recombinant protein binding to purified parasite histones and a panel of H3 phosphopeptides, with in silico analysis of binding residues\",\n      \"pmids\": [\"23308157\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Binding residues were not validated by mutagenesis\",\n        \"The downstream chromatin or transcriptional consequence of H3S28ph reading was not defined\",\n        \"Shown only in vitro; nuclear recruitment in living parasites not demonstrated\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Identified PF3D7_0818200 as a bridge in a PKA-associated complex, answering how an AKAP-like anchoring protein connects to the PKA regulatory subunit.\",\n      \"evidence\": \"Pull-downs with recombinant proteins and parasite extracts, immunofluorescence colocalization, and in vitro radiolabel PKA phosphorylation assay\",\n      \"pmids\": [\"27129434\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single-lab pull-down with limited mechanistic follow-up\",\n        \"Functional consequence of the PfAKAL\\u2013PF3D7_0818200\\u2013PfPKA-R complex not established\",\n        \"Whether PKA phosphorylation of PF3D7_0818200 gates complex assembly was not directly tested\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Defined PF3D7_0818200 as the organizer of a merozoite invasion-signaling complex, showing that its scaffolding of phospho-PfPKAr and phospho-PfCDPK1 is functionally required for invasion.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation, gel filtration, competitive phosphopeptide displacement, and microneme secretion and RBC invasion assays\",\n      \"pmids\": [\"32817103\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"The phosphopeptide disruption is pharmacological; genetic ablation of PF3D7_0818200 binding not shown\",\n        \"Temporal ordering of complex assembly during invasion not resolved\",\n        \"Full composition of the merozoite complex beyond the named partners not defined\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Resolved the molecular grammar and affinity of the PF3D7_0818200\\u2013PfCDPK1 interaction and its effect on kinase activity, providing a druggable interface.\",\n      \"evidence\": \"Molecular dynamics simulation with SPR, ITC and ELISA affinity measurements, kinase activity assay, and peptidomimetic antagonist growth-inhibition tests\",\n      \"pmids\": [\"32484216\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"The mechanism by which binding enhances CDPK1 activity is only marginal and mechanistically undefined\",\n        \"Cellular relevance of the 670 nM affinity during native signaling not established\",\n        \"Selectivity of peptidomimetic antagonists over sibling 14-3-3 members not characterized\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown how the nuclear histone-reading role and the cytoplasmic merozoite signaling-scaffold role of PF3D7_0818200 are coordinated across the parasite life cycle.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No genetic loss-of-function study connecting the two functional modules\",\n        \"No structural model of PF3D7_0818200 bound to its native partners in the parasite\",\n        \"Regulation of PF3D7_0818200 phosphorylation state in vivo not defined\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0035175\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0050815\", \"supporting_discovery_ids\": [1, 2, 3]},\n      {\"term_id\": \"GO:0019901\", \"supporting_discovery_ids\": [1, 2, 3]},\n      {\"term_id\": \"GO:0030674\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0020009\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0044409\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0002020\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"complexes\": [\n      \"PfAKAL\\u2013PF3D7_0818200\\u2013PfPKA-R complex [#3]\",\n      \"Merozoite signaling complex with phospho-PfPKAr and phospho-PfCDPK1 [#1]\"\n    ],\n    \"partners\": [\n      \"Histone H3 (H3S28ph) [#0]\",\n      \"PfCDPK1 (via 61KLGpS64 Mode I motif, Kd ~670 nM) [#2]\",\n      \"PfPKAr / PfPKA-R [#1, #3]\",\n      \"PfAKAL (AKAP-like protein) [#3]\"\n    ],\n    \"other_free_text\": [\n      \"Interaction with PfCDPK1 uses a canonical Mode I (RXXpS/pT) phosphopeptide-binding mode [#2]\",\n      \"PF3D7_0818200 is itself a PKA substrate in vitro, whereas its partner PfAKAL is not [#3]\",\n      \"Phosphopeptide (P1) and peptidomimetic antagonists disrupting its complexes inhibit microneme secretion, invasion, and parasite growth [#1, #2]\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0818200","name":null,"product":"14-3-3 protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0712600","name":null,"product":"14-3-3 protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0501800","name":null,"product":"14-3-3 protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}