{"gene":"PF3D7_1145400","run_date":"2026-09-08T14:19:05","timeline":{"discoveries":[{"year":2004,"finding":"DYN1 (PfDYN1/Pfdyn1) was cloned from P. falciparum Dd2 asexual stage cDNA and shown to encode a dynamin-like GTPase containing a conserved N-terminal tripartite GTPase domain, a coiled-coil region, and a C-terminal domain; recombinant protein was Triton X-100 insoluble and expressed only in the mature sub-stage; it co-localized with the ER marker PfGRP and associated with multiple membrane structures and ~60–100 nm vesicles inside and on the surface of parasites and in the erythrocyte cytoplasm; dsRNA targeting the C-terminus markedly inhibited P. falciparum erythrocytic growth.","method":"cDNA cloning, Western blot, immunofluorescence co-localization with ER marker, dsRNA knockdown growth inhibition assay","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — multiple orthogonal methods (localization, knockdown, Western blot) in a single lab; no in vitro GTPase assay reported for DYN1 in this paper","pmids":["15240099"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"Dd2"}]},{"year":2009,"finding":"Recombinant GTPase domain of DYN1 (PfDYN1) expressed in E. coli displayed GTPase activity that was inhibited in vitro by the dynamin inhibitor dynasore; treatment of parasite cultures with dynasore at ring and early trophozoite stage reduced hemoglobin uptake (measured by FITC-dextran incorporation), decreased intracellular hemozoin accumulation, inhibited parasite growth, and caused ultrastructural changes, implicating DYN1 in the hemoglobin uptake pathway.","method":"Recombinant protein GTPase activity assay, dynasore pharmacological inhibition, FITC-dextran uptake assay, transmission electron microscopy","journal":"Chinese medical journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vitro enzymatic assay combined with pharmacological inhibition and functional readouts (hemoglobin uptake, hemozoin), but dynasore also inhibits DYN2, limiting specificity to DYN1 alone","pmids":["19719972"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"DYN1 mRNA expression is modulated by the host hormone melatonin in a stage-specific manner during the P. falciparum erythrocytic cycle; knockout of PfPK7 (protein kinase 7) abolishes melatonin-induced changes in DYN1 gene expression and alters mitochondrial morphology and oxygen consumption, placing DYN1 downstream of PfPK7 in melatonin-triggered mitochondrial fission signaling.","method":"RT-PCR/mRNA expression analysis, PfPK7 knockout genetic epistasis, MitoTracker Red CMX Ros morphology, oxygen consumption measurement, mitochondria-targeted GFP construct","journal":"Journal of pineal research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis via PfPK7 KO combined with expression analysis and organelle morphology, single lab","pmids":["29480948"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"DYN1 (PfDyn1, PF3D7_1145400) was identified as a potential proximal interactor of the Golgi/microneme-localized PIP-binding protein PfPX2 by proximity labeling (BioID or similar), suggesting DYN1 participates in vesicular trafficking between the Golgi apparatus and micronemes.","method":"Proximity labeling (BioID-type) mass spectrometry","journal":"Scientific reports","confidence":"Low","confidence_rationale":"Tier 3 / Weak — proximity labeling is a single indirect method; DYN1 is listed as a candidate interactor without direct validation","pmids":["41125830"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"DYN1 (PF3D7_1145400) is a P. falciparum dynamin-like GTPase that is expressed in mature asexual blood stages, associates with ER and vesicular membrane structures, possesses GTPase activity inhibitable by dynasore, participates in hemoglobin uptake, and is transcriptionally regulated by melatonin via a PfPK7-dependent pathway linked to mitochondrial fission; proximity labeling additionally places it near the Golgi–microneme trafficking axis."},"narrative":{"mechanistic_narrative":"DYN1 (PF3D7_1145400) is a Plasmodium falciparum dynamin-like GTPase that functions in membrane dynamics and endocytic trafficking during the asexual erythrocytic cycle [PMID:15240099, PMID:19719972]. The protein contains a conserved N-terminal tripartite GTPase domain, a coiled-coil region, and a C-terminal domain, is expressed specifically in the mature asexual sub-stage, and localizes to the endoplasmic reticulum and to multiple membrane structures and ~60–100 nm vesicles within the parasite, at its surface, and in the erythrocyte cytoplasm [PMID:15240099]. Its recombinant GTPase domain is catalytically active and inhibited in vitro by the dynamin inhibitor dynasore; pharmacological inhibition reduces hemoglobin uptake and hemozoin accumulation and arrests growth, implicating DYN1 in the hemoglobin endocytosis pathway, consistent with the growth defect caused by dsRNA targeting its C-terminus [PMID:15240099, PMID:19719972]. DYN1 transcription is regulated by the host hormone melatonin through a PfPK7-dependent pathway linked to mitochondrial fission [PMID:29480948]. Beyond these findings, its direct binding partners and role in specific trafficking routes remain uncharacterized in the available corpus; proximity labeling has only placed it as a candidate near the Golgi–microneme axis [PMID:41125830].","teleology":[{"year":2004,"claim":"Establishing that P. falciparum encodes a dynamin-like GTPase and that it is essential answered whether the parasite possesses its own membrane-remodeling machinery of this class and whether it matters for blood-stage survival.","evidence":"cDNA cloning, Western blot, immunofluorescence co-localization with the ER marker PfGRP, and dsRNA knockdown growth-inhibition assay in Dd2 asexual stages","pmids":["15240099"],"confidence":"Medium","gaps":["No in vitro GTPase activity demonstrated for DYN1 in this study","dsRNA knockdown lacks single-gene specificity controls","Exact membrane structures and vesicle identity not molecularly defined"],"attribution":[{"species":"Plasmodium falciparum","strain":"Dd2"}]},{"year":2009,"claim":"Demonstrating catalytic GTPase activity and a functional link to hemoglobin uptake moved DYN1 from a predicted dynamin-like protein to an enzyme implicated in a specific endocytic process.","evidence":"Recombinant GTPase-domain activity assay, dynasore pharmacological inhibition, FITC-dextran uptake, and transmission electron microscopy in parasite cultures","pmids":["19719972"],"confidence":"Medium","gaps":["Dynasore also inhibits DYN2, so effects cannot be attributed to DYN1 alone","No direct genetic loss-of-function tied to the hemoglobin-uptake phenotype","Mechanistic role of DYN1 at the endocytic membrane not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"Placing DYN1 transcription downstream of PfPK7 in melatonin signaling connected the protein to host-hormone-triggered mitochondrial fission, positing a regulatory input onto DYN1 expression.","evidence":"mRNA expression analysis, PfPK7 knockout epistasis, MitoTracker morphology, oxygen consumption, and mitochondria-targeted GFP","pmids":["29480948"],"confidence":"Medium","gaps":["Regulation shown at mRNA level, not DYN1 protein or activity","Direct role of DYN1 protein in mitochondrial fission not demonstrated","Whether PfPK7 acts on DYN1 directly or indirectly is unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Proximity labeling raised the possibility that DYN1 acts in Golgi-to-microneme vesicular trafficking by placing it near the PIP-binding protein PfPX2.","evidence":"Proximity labeling (BioID-type) mass spectrometry identifying DYN1 as a candidate proximal interactor of PfPX2","pmids":["41125830"],"confidence":"Low","gaps":["Single indirect method with no reciprocal or direct interaction validation","DYN1 role in Golgi–microneme trafficking not functionally tested","Proximity does not establish physical or functional partnership"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether DYN1 physically assembles into a defined complex, what membranes it directly remodels, and how its distinct roles (hemoglobin uptake, ER/vesicle association, mitochondrial fission signaling, Golgi–microneme axis) are mechanistically integrated remain open.","evidence":"","pmids":[],"confidence":"Low","gaps":["No validated direct binding partners identified","No structural model of the assembled/oligomeric protein","Direct genetic dissection separating DYN1 from DYN2 functions lacking"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["PFPK7 (TRANSCRIPTIONAL REGULATION VIA MELATONIN SIGNALING) [#2]","PFPX2 (CANDIDATE PROXIMAL INTERACTOR, UNVALIDATED) [#3]"],"other_free_text":["Contains a tripartite N-terminal GTPase domain, coiled-coil region, and C-terminal domain; recombinant protein is Triton X-100 insoluble and expressed only in the mature asexual sub-stage [#0].","GTPase activity is inhibited in vitro by dynasore; dynasore treatment reduces hemoglobin uptake and hemozoin accumulation, but dynasore is not specific to DYN1 over DYN2 [#1].","dsRNA targeting the C-terminus inhibits erythrocytic growth [#0]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"29480948","id":"PMC_29480948","title":"Melatonin activates FIS1, DYN1, and DYN2 Plasmodium falciparum related-genes for mitochondria fission: Mitoemerald-GFP as a tool to visualize mitochondria structure.","date":"2018","source":"Journal of pineal research","url":"https://pubmed.ncbi.nlm.nih.gov/29480948","citation_count":33,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["DYN1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"17533148","id":"PMC_17533148","title":"Characterization of PfDYN2, a dynamin-like protein of Plasmodium falciparum expressed in schizonts.","date":"2007","source":"Microbes and infection","url":"https://pubmed.ncbi.nlm.nih.gov/17533148","citation_count":22,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["dynamin-like protein","PfDYN1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"15240099","id":"PMC_15240099","title":"Isolation and functional characterization of a dynamin-like gene from Plasmodium falciparum.","date":"2004","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/15240099","citation_count":21,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfDYN1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19719972","id":"PMC_19719972","title":"Dynamin like protein 1 participated in the hemoglobin uptake pathway of Plasmodium falciparum.","date":"2009","source":"Chinese medical journal","url":"https://pubmed.ncbi.nlm.nih.gov/19719972","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["dynamin-like protein","PfDYN1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40157510","id":"PMC_40157510","title":"A dynamin-like protein in Plasmodium falciparum plays an essential role in parasite growth, mitochondrial development and homeostasis during asexual blood stages.","date":"2025","source":"Biochimica et biophysica acta. Molecular cell research","url":"https://pubmed.ncbi.nlm.nih.gov/40157510","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["dynamin-like protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34428626","id":"PMC_34428626","title":"Molecular basis of synchronous replication of malaria parasites in the blood stage.","date":"2021","source":"Current opinion in microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/34428626","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["DYN1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"12905715","id":"PMC_12905715","title":"[Molecular cloning of Plasmodium yoelii dynamin-like protein (PyDyn) gene and the immunological character of its domains].","date":"2003","source":"Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae","url":"https://pubmed.ncbi.nlm.nih.gov/12905715","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["dynamin-like protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41125830","id":"PMC_41125830","title":"Characterization of a phosphoinositide-binding protein containing a PHOX homology domain in the malaria parasite Plasmodium falciparum.","date":"2025","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/41125830","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfDYN1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6503,"output_tokens":1385,"usd":0.020142,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6315,"output_tokens":2555,"usd":0.047725,"stage2_stop_reason":"end_turn"},"total_usd":0.067867,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2004,\n      \"finding\": \"DYN1 (PfDYN1/Pfdyn1) was cloned from P. falciparum Dd2 asexual stage cDNA and shown to encode a dynamin-like GTPase containing a conserved N-terminal tripartite GTPase domain, a coiled-coil region, and a C-terminal domain; recombinant protein was Triton X-100 insoluble and expressed only in the mature sub-stage; it co-localized with the ER marker PfGRP and associated with multiple membrane structures and ~60–100 nm vesicles inside and on the surface of parasites and in the erythrocyte cytoplasm; dsRNA targeting the C-terminus markedly inhibited P. falciparum erythrocytic growth.\",\n      \"method\": \"cDNA cloning, Western blot, immunofluorescence co-localization with ER marker, dsRNA knockdown growth inhibition assay\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — multiple orthogonal methods (localization, knockdown, Western blot) in a single lab; no in vitro GTPase assay reported for DYN1 in this paper\",\n      \"pmids\": [\"15240099\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"Dd2\"}]\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"Recombinant GTPase domain of DYN1 (PfDYN1) expressed in E. coli displayed GTPase activity that was inhibited in vitro by the dynamin inhibitor dynasore; treatment of parasite cultures with dynasore at ring and early trophozoite stage reduced hemoglobin uptake (measured by FITC-dextran incorporation), decreased intracellular hemozoin accumulation, inhibited parasite growth, and caused ultrastructural changes, implicating DYN1 in the hemoglobin uptake pathway.\",\n      \"method\": \"Recombinant protein GTPase activity assay, dynasore pharmacological inhibition, FITC-dextran uptake assay, transmission electron microscopy\",\n      \"journal\": \"Chinese medical journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vitro enzymatic assay combined with pharmacological inhibition and functional readouts (hemoglobin uptake, hemozoin), but dynasore also inhibits DYN2, limiting specificity to DYN1 alone\",\n      \"pmids\": [\"19719972\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"DYN1 mRNA expression is modulated by the host hormone melatonin in a stage-specific manner during the P. falciparum erythrocytic cycle; knockout of PfPK7 (protein kinase 7) abolishes melatonin-induced changes in DYN1 gene expression and alters mitochondrial morphology and oxygen consumption, placing DYN1 downstream of PfPK7 in melatonin-triggered mitochondrial fission signaling.\",\n      \"method\": \"RT-PCR/mRNA expression analysis, PfPK7 knockout genetic epistasis, MitoTracker Red CMX Ros morphology, oxygen consumption measurement, mitochondria-targeted GFP construct\",\n      \"journal\": \"Journal of pineal research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis via PfPK7 KO combined with expression analysis and organelle morphology, single lab\",\n      \"pmids\": [\"29480948\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"DYN1 (PfDyn1, PF3D7_1145400) was identified as a potential proximal interactor of the Golgi/microneme-localized PIP-binding protein PfPX2 by proximity labeling (BioID or similar), suggesting DYN1 participates in vesicular trafficking between the Golgi apparatus and micronemes.\",\n      \"method\": \"Proximity labeling (BioID-type) mass spectrometry\",\n      \"journal\": \"Scientific reports\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — proximity labeling is a single indirect method; DYN1 is listed as a candidate interactor without direct validation\",\n      \"pmids\": [\"41125830\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"DYN1 (PF3D7_1145400) is a P. falciparum dynamin-like GTPase that is expressed in mature asexual blood stages, associates with ER and vesicular membrane structures, possesses GTPase activity inhibitable by dynasore, participates in hemoglobin uptake, and is transcriptionally regulated by melatonin via a PfPK7-dependent pathway linked to mitochondrial fission; proximity labeling additionally places it near the Golgi–microneme trafficking axis.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"DYN1 (PF3D7_1145400) is a Plasmodium falciparum dynamin-like GTPase that functions in membrane dynamics and endocytic trafficking during the asexual erythrocytic cycle [#0, #1]. The protein contains a conserved N-terminal tripartite GTPase domain, a coiled-coil region, and a C-terminal domain, is expressed specifically in the mature asexual sub-stage, and localizes to the endoplasmic reticulum and to multiple membrane structures and ~60–100 nm vesicles within the parasite, at its surface, and in the erythrocyte cytoplasm [#0]. Its recombinant GTPase domain is catalytically active and inhibited in vitro by the dynamin inhibitor dynasore; pharmacological inhibition reduces hemoglobin uptake and hemozoin accumulation and arrests growth, implicating DYN1 in the hemoglobin endocytosis pathway, consistent with the growth defect caused by dsRNA targeting its C-terminus [#0, #1]. DYN1 transcription is regulated by the host hormone melatonin through a PfPK7-dependent pathway linked to mitochondrial fission [#2]. Beyond these findings, its direct binding partners and role in specific trafficking routes remain uncharacterized in the available corpus; proximity labeling has only placed it as a candidate near the Golgi–microneme axis [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2004,\n      \"claim\": \"Establishing that P. falciparum encodes a dynamin-like GTPase and that it is essential answered whether the parasite possesses its own membrane-remodeling machinery of this class and whether it matters for blood-stage survival.\",\n      \"evidence\": \"cDNA cloning, Western blot, immunofluorescence co-localization with the ER marker PfGRP, and dsRNA knockdown growth-inhibition assay in Dd2 asexual stages\",\n      \"pmids\": [\"15240099\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No in vitro GTPase activity demonstrated for DYN1 in this study\", \"dsRNA knockdown lacks single-gene specificity controls\", \"Exact membrane structures and vesicle identity not molecularly defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"Dd2\"}]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Demonstrating catalytic GTPase activity and a functional link to hemoglobin uptake moved DYN1 from a predicted dynamin-like protein to an enzyme implicated in a specific endocytic process.\",\n      \"evidence\": \"Recombinant GTPase-domain activity assay, dynasore pharmacological inhibition, FITC-dextran uptake, and transmission electron microscopy in parasite cultures\",\n      \"pmids\": [\"19719972\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Dynasore also inhibits DYN2, so effects cannot be attributed to DYN1 alone\", \"No direct genetic loss-of-function tied to the hemoglobin-uptake phenotype\", \"Mechanistic role of DYN1 at the endocytic membrane not resolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Placing DYN1 transcription downstream of PfPK7 in melatonin signaling connected the protein to host-hormone-triggered mitochondrial fission, positing a regulatory input onto DYN1 expression.\",\n      \"evidence\": \"mRNA expression analysis, PfPK7 knockout epistasis, MitoTracker morphology, oxygen consumption, and mitochondria-targeted GFP\",\n      \"pmids\": [\"29480948\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Regulation shown at mRNA level, not DYN1 protein or activity\", \"Direct role of DYN1 protein in mitochondrial fission not demonstrated\", \"Whether PfPK7 acts on DYN1 directly or indirectly is unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Proximity labeling raised the possibility that DYN1 acts in Golgi-to-microneme vesicular trafficking by placing it near the PIP-binding protein PfPX2.\",\n      \"evidence\": \"Proximity labeling (BioID-type) mass spectrometry identifying DYN1 as a candidate proximal interactor of PfPX2\",\n      \"pmids\": [\"41125830\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single indirect method with no reciprocal or direct interaction validation\", \"DYN1 role in Golgi–microneme trafficking not functionally tested\", \"Proximity does not establish physical or functional partnership\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether DYN1 physically assembles into a defined complex, what membranes it directly remodels, and how its distinct roles (hemoglobin uptake, ER/vesicle association, mitochondrial fission signaling, Golgi–microneme axis) are mechanistically integrated remain open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No validated direct binding partners identified\", \"No structural model of the assembled/oligomeric protein\", \"Direct genetic dissection separating DYN1 from DYN2 functions lacking\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003924\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005525\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0016020\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0031410\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006897\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0016559\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"PfPK7 (transcriptional regulation via melatonin signaling) [#2]\",\n      \"PfPX2 (candidate proximal interactor, unvalidated) [#3]\"\n    ],\n    \"other_free_text\": [\n      \"Contains a tripartite N-terminal GTPase domain, coiled-coil region, and C-terminal domain; recombinant protein is Triton X-100 insoluble and expressed only in the mature asexual sub-stage [#0].\",\n      \"GTPase activity is inhibited in vitro by dynasore; dynasore treatment reduces hemoglobin uptake and hemozoin accumulation, but dynasore is not specific to DYN1 over DYN2 [#1].\",\n      \"dsRNA targeting the C-terminus inhibits erythrocytic growth [#0].\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1145400","name":null,"product":"dynamin-like protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0903600","name":null,"product":"dynamin-like protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0943300","name":null,"product":"dynamin-like protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"DYN1","evaluation":null}