{"gene":"PF3D7_0708800","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2012,"finding":"HSP110c (PfHsp110c) prevents aggregation of asparagine repeat-containing proteins (including P. falciparum PFI1155w and yeast Sup35) at febrile temperatures; human and yeast orthologs were far less effective. Gene-knockout of HSP110c was lethal, and conditional knockdown parasites died rapidly upon heat shock and were unable to prevent aggregation of asparagine-repeat proteins, establishing HSP110c as essential for proteostasis during febrile episodes.","method":"Co-expression aggregation assay in mammalian cells, conditional knockdown (protein-stabilizing ligand system) in P. falciparum, gene-knockout viability assay, immunofluorescence-based aggregation detection","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (co-expression aggregation assay, conditional knockdown, gene-knockout lethality) in a single rigorous study with clear functional readouts","pmids":["23250440"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"finding":"HSP110c (PfHsp70-z) possesses independent chaperone (holdase) activity, suppressing protein aggregation in vitro, and associates with the canonical cytosolic PfHsp70-1 in a nucleotide-dependent manner, consistent with a nucleotide exchange factor (NEF) role for PfHsp70-1.","method":"In vitro aggregation suppression assay (chaperone activity), co-immunoaffinity chromatography, surface plasmon resonance (SPR)","journal":"Cell stress & chaperones","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — in vitro biochemical assay plus two orthogonal interaction methods (co-immunoaffinity and SPR), single lab","pmids":["26894764"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"HSP110c (PfHsp70-z) is heat-stable, possesses ATPase activity, and is capable of self-association; its expression is upregulated in P. falciparum cells subjected to heat stress in vitro.","method":"Recombinant protein biochemical assays (ATPase activity assay, thermal stability assay, self-association assay), in vitro culture heat stress and protein expression analysis","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple in vitro biochemical assays on recombinant protein, single lab","pmids":["26083397"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"The unique linker segment of HSP110c (PfHsp70-z) modulates its global conformation and regulates client protein binding, holdase chaperone activity, and ATPase activity; the rigid linker (as opposed to the flexible linker of canonical PfHsp70-1) confers notable thermal stability. Linker switch mutants (replacing HSP110c linker with that of PfHsp70-1 or DnaK) disrupted these properties, demonstrating that the linker restricts HSP110c to holdase function and prevents refoldase activity.","method":"Site-directed mutagenesis (linker switch mutants), circular dichroism, intrinsic and extrinsic fluorescence spectroscopy, ATPase activity assay, client protein binding assay, cellular analyses","journal":"International journal of biological macromolecules","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — mutagenesis combined with multiple orthogonal biophysical and biochemical assays, single lab","pmids":["33741370"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"Surface plasmon resonance analysis of linker switch mutants confirmed that the HSP110c (PfHsp70-z) linker influences ATP-binding affinity and the interaction with cytosolic co-chaperone PfHsp40; swapping the linker with that of canonical Hsp70s altered these interactions.","method":"Surface plasmon resonance (SPR), intrinsic and extrinsic fluorescence spectroscopy, stability assays (pH and urea)","journal":"Data in brief","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — SPR-based direct binding measurements on mutant proteins, corroborating data from companion paper, single lab","pmids":["34141839"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"HSP110c (PfHsp70-z, PF3D7_0708800) is an essential cytosolic Hsp110-family chaperone in P. falciparum that acts as a holdase to prevent aggregation of the parasite's asparagine repeat-rich proteome during febrile temperatures, possesses intrinsic ATPase activity and self-association capacity, and interacts with the canonical cytosolic chaperone PfHsp70-1 in a nucleotide-dependent manner consistent with a nucleotide exchange factor role; its unique rigid linker segment is the structural determinant that restricts it to holdase (rather than refoldase) function, confers exceptional thermal stability, and modulates client binding, ATPase activity, and co-chaperone interactions."},"narrative":{"mechanistic_narrative":"HSP110c (PF3D7_0708800) is an essential cytosolic Hsp110-family chaperone that maintains proteostasis in P. falciparum during the febrile episodes of malaria infection, functioning as a holdase that prevents aggregation of the parasite's asparagine repeat-rich proteome at elevated temperatures [PMID:23250440]. Gene knockout is lethal and conditional knockdown parasites die rapidly upon heat shock, unable to suppress aggregation of asparagine-repeat clients such as PFI1155w, while human and yeast orthologs are far less effective at this task—establishing HSP110c as specifically adapted to the parasite's repeat-rich proteome [PMID:23250440]. Biochemically, recombinant HSP110c is heat-stable, possesses intrinsic ATPase activity, self-associates, and is upregulated under heat stress [PMID:26083397]; it suppresses protein aggregation in vitro and binds the canonical cytosolic chaperone PfHsp70-1 in a nucleotide-dependent manner consistent with a nucleotide exchange factor role [PMID:26894764]. Its unique rigid linker segment is the structural determinant that restricts HSP110c to holdase (rather than refoldase) function, confers thermal stability, and tunes client binding, ATPase activity, ATP-binding affinity, and co-chaperone (PfHsp40) interactions, as shown by linker-switch mutants that swap in the flexible linkers of PfHsp70-1 or DnaK [PMID:33741370, PMID:34141839]. Beyond these findings, no further mechanistic detail has been characterized in the available corpus.","teleology":[{"year":2012,"claim":"Whether P. falciparum requires a dedicated chaperone to survive febrile temperatures was unresolved; this work established HSP110c as essential for proteostasis by protecting the parasite's asparagine repeat-rich proteome from heat-induced aggregation.","evidence":"co-expression aggregation assay in mammalian cells, conditional knockdown and gene knockout in P. falciparum with immunofluorescence aggregation readout","pmids":["23250440"],"confidence":"High","gaps":["the full repertoire of endogenous asparagine-repeat clients was not defined","structural basis for the parasite ortholog's superior anti-aggregation activity not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"To determine the intrinsic biochemical properties underlying its chaperone role, recombinant HSP110c was shown to be heat-stable, to have ATPase activity, to self-associate, and to be heat-inducible in culture.","evidence":"recombinant protein ATPase, thermal stability and self-association assays plus heat-stress expression analysis","pmids":["26083397"],"confidence":"Medium","gaps":["functional consequence of self-association in vivo not established","ATPase cycle not linked to a defined client-binding mechanism"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"claim":"Whether HSP110c acts autonomously or cooperatively was addressed by showing it has independent holdase activity and binds PfHsp70-1 nucleotide-dependently, positioning it as a candidate nucleotide exchange factor for the canonical Hsp70.","evidence":"in vitro aggregation suppression assay, co-immunoaffinity chromatography, and surface plasmon resonance","pmids":["26894764"],"confidence":"High","gaps":["NEF activity inferred from nucleotide-dependent binding but not directly measured as nucleotide exchange kinetics","cellular role of the PfHsp70-1 interaction not tested by perturbation"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"The structural determinant restricting HSP110c to holdase function was identified: linker-switch mutants demonstrated that its rigid linker (versus the flexible linker of canonical Hsp70s) governs conformation, client binding, holdase activity, ATPase activity, ATP-binding affinity, and PfHsp40 interaction, and prevents refoldase activity.","evidence":"linker-switch site-directed mutagenesis with circular dichroism, fluorescence spectroscopy, ATPase and client-binding assays, and SPR","pmids":["33741370","34141839"],"confidence":"High","gaps":["the linker's role in intact parasites not tested by allelic replacement","high-resolution structure of the full-length protein not determined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"It remains unknown how HSP110c's holdase and putative nucleotide-exchange functions are integrated within the parasite cytosolic chaperone network in vivo and which endogenous clients it engages during a febrile cycle.","evidence":"no direct experimental evidence in the available corpus","pmids":[],"confidence":"Low","gaps":["in vivo client interactome undefined","no structural model of client or co-chaperone complexes","NEF activity not demonstrated by functional exchange assay"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["PFHSP70-1","PFHSP40"],"other_free_text":["Essential in P. falciparum: gene knockout lethal, conditional knockdown lethal upon heat shock [#0]","Holdase-only chaperone; rigid linker prevents refoldase activity [#3]","Prevents aggregation of asparagine repeat-containing clients including PFI1155w; more effective than human and yeast orthologs [#0]","Rigid linker segment confers thermal stability and tunes client binding, ATPase and ATP-binding affinity, and co-chaperone interactions [#3, #4]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"23250440","id":"PMC_23250440","title":"Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers.","date":"2012","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/23250440","citation_count":116,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["heat shock protein 110","PfHSP110c"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26894764","id":"PMC_26894764","title":"Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion.","date":"2016","source":"Cell stress & chaperones","url":"https://pubmed.ncbi.nlm.nih.gov/26894764","citation_count":46,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26083397","id":"PMC_26083397","title":"Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein.","date":"2015","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26083397","citation_count":39,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33741370","id":"PMC_33741370","title":"Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone.","date":"2021","source":"International journal of biological macromolecules","url":"https://pubmed.ncbi.nlm.nih.gov/33741370","citation_count":13,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26052682","id":"PMC_26052682","title":"Co-evolutionary analysis implies auxiliary functions of HSP110 in Plasmodium falciparum.","date":"2015","source":"Proteins","url":"https://pubmed.ncbi.nlm.nih.gov/26052682","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34141839","id":"PMC_34141839","title":"Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70.","date":"2021","source":"Data in brief","url":"https://pubmed.ncbi.nlm.nih.gov/34141839","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["heat shock protein 110"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5861,"output_tokens":1556,"usd":0.020462,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6585,"output_tokens":2580,"usd":0.048712,"stage2_stop_reason":"end_turn"},"total_usd":0.069174,"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\": 2012,\n      \"finding\": \"HSP110c (PfHsp110c) prevents aggregation of asparagine repeat-containing proteins (including P. falciparum PFI1155w and yeast Sup35) at febrile temperatures; human and yeast orthologs were far less effective. Gene-knockout of HSP110c was lethal, and conditional knockdown parasites died rapidly upon heat shock and were unable to prevent aggregation of asparagine-repeat proteins, establishing HSP110c as essential for proteostasis during febrile episodes.\",\n      \"method\": \"Co-expression aggregation assay in mammalian cells, conditional knockdown (protein-stabilizing ligand system) in P. falciparum, gene-knockout viability assay, immunofluorescence-based aggregation detection\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (co-expression aggregation assay, conditional knockdown, gene-knockout lethality) in a single rigorous study with clear functional readouts\",\n      \"pmids\": [\"23250440\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"HSP110c (PfHsp70-z) possesses independent chaperone (holdase) activity, suppressing protein aggregation in vitro, and associates with the canonical cytosolic PfHsp70-1 in a nucleotide-dependent manner, consistent with a nucleotide exchange factor (NEF) role for PfHsp70-1.\",\n      \"method\": \"In vitro aggregation suppression assay (chaperone activity), co-immunoaffinity chromatography, surface plasmon resonance (SPR)\",\n      \"journal\": \"Cell stress & chaperones\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — in vitro biochemical assay plus two orthogonal interaction methods (co-immunoaffinity and SPR), single lab\",\n      \"pmids\": [\"26894764\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"HSP110c (PfHsp70-z) is heat-stable, possesses ATPase activity, and is capable of self-association; its expression is upregulated in P. falciparum cells subjected to heat stress in vitro.\",\n      \"method\": \"Recombinant protein biochemical assays (ATPase activity assay, thermal stability assay, self-association assay), in vitro culture heat stress and protein expression analysis\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple in vitro biochemical assays on recombinant protein, single lab\",\n      \"pmids\": [\"26083397\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"The unique linker segment of HSP110c (PfHsp70-z) modulates its global conformation and regulates client protein binding, holdase chaperone activity, and ATPase activity; the rigid linker (as opposed to the flexible linker of canonical PfHsp70-1) confers notable thermal stability. Linker switch mutants (replacing HSP110c linker with that of PfHsp70-1 or DnaK) disrupted these properties, demonstrating that the linker restricts HSP110c to holdase function and prevents refoldase activity.\",\n      \"method\": \"Site-directed mutagenesis (linker switch mutants), circular dichroism, intrinsic and extrinsic fluorescence spectroscopy, ATPase activity assay, client protein binding assay, cellular analyses\",\n      \"journal\": \"International journal of biological macromolecules\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — mutagenesis combined with multiple orthogonal biophysical and biochemical assays, single lab\",\n      \"pmids\": [\"33741370\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Surface plasmon resonance analysis of linker switch mutants confirmed that the HSP110c (PfHsp70-z) linker influences ATP-binding affinity and the interaction with cytosolic co-chaperone PfHsp40; swapping the linker with that of canonical Hsp70s altered these interactions.\",\n      \"method\": \"Surface plasmon resonance (SPR), intrinsic and extrinsic fluorescence spectroscopy, stability assays (pH and urea)\",\n      \"journal\": \"Data in brief\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — SPR-based direct binding measurements on mutant proteins, corroborating data from companion paper, single lab\",\n      \"pmids\": [\"34141839\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"HSP110c (PfHsp70-z, PF3D7_0708800) is an essential cytosolic Hsp110-family chaperone in P. falciparum that acts as a holdase to prevent aggregation of the parasite's asparagine repeat-rich proteome during febrile temperatures, possesses intrinsic ATPase activity and self-association capacity, and interacts with the canonical cytosolic chaperone PfHsp70-1 in a nucleotide-dependent manner consistent with a nucleotide exchange factor role; its unique rigid linker segment is the structural determinant that restricts it to holdase (rather than refoldase) function, confers exceptional thermal stability, and modulates client binding, ATPase activity, and co-chaperone interactions.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"HSP110c (PF3D7_0708800) is an essential cytosolic Hsp110-family chaperone that maintains proteostasis in P. falciparum during the febrile episodes of malaria infection, functioning as a holdase that prevents aggregation of the parasite's asparagine repeat-rich proteome at elevated temperatures [#0]. Gene knockout is lethal and conditional knockdown parasites die rapidly upon heat shock, unable to suppress aggregation of asparagine-repeat clients such as PFI1155w, while human and yeast orthologs are far less effective at this task—establishing HSP110c as specifically adapted to the parasite's repeat-rich proteome [#0]. Biochemically, recombinant HSP110c is heat-stable, possesses intrinsic ATPase activity, self-associates, and is upregulated under heat stress [#2]; it suppresses protein aggregation in vitro and binds the canonical cytosolic chaperone PfHsp70-1 in a nucleotide-dependent manner consistent with a nucleotide exchange factor role [#1]. Its unique rigid linker segment is the structural determinant that restricts HSP110c to holdase (rather than refoldase) function, confers thermal stability, and tunes client binding, ATPase activity, ATP-binding affinity, and co-chaperone (PfHsp40) interactions, as shown by linker-switch mutants that swap in the flexible linkers of PfHsp70-1 or DnaK [#3, #4]. Beyond these findings, no further mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2012,\n      \"claim\": \"Whether P. falciparum requires a dedicated chaperone to survive febrile temperatures was unresolved; this work established HSP110c as essential for proteostasis by protecting the parasite's asparagine repeat-rich proteome from heat-induced aggregation.\",\n      \"evidence\": \"co-expression aggregation assay in mammalian cells, conditional knockdown and gene knockout in P. falciparum with immunofluorescence aggregation readout\",\n      \"pmids\": [\"23250440\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"the full repertoire of endogenous asparagine-repeat clients was not defined\",\n        \"structural basis for the parasite ortholog's superior anti-aggregation activity not resolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"To determine the intrinsic biochemical properties underlying its chaperone role, recombinant HSP110c was shown to be heat-stable, to have ATPase activity, to self-associate, and to be heat-inducible in culture.\",\n      \"evidence\": \"recombinant protein ATPase, thermal stability and self-association assays plus heat-stress expression analysis\",\n      \"pmids\": [\"26083397\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"functional consequence of self-association in vivo not established\",\n        \"ATPase cycle not linked to a defined client-binding mechanism\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Whether HSP110c acts autonomously or cooperatively was addressed by showing it has independent holdase activity and binds PfHsp70-1 nucleotide-dependently, positioning it as a candidate nucleotide exchange factor for the canonical Hsp70.\",\n      \"evidence\": \"in vitro aggregation suppression assay, co-immunoaffinity chromatography, and surface plasmon resonance\",\n      \"pmids\": [\"26894764\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"NEF activity inferred from nucleotide-dependent binding but not directly measured as nucleotide exchange kinetics\",\n        \"cellular role of the PfHsp70-1 interaction not tested by perturbation\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The structural determinant restricting HSP110c to holdase function was identified: linker-switch mutants demonstrated that its rigid linker (versus the flexible linker of canonical Hsp70s) governs conformation, client binding, holdase activity, ATPase activity, ATP-binding affinity, and PfHsp40 interaction, and prevents refoldase activity.\",\n      \"evidence\": \"linker-switch site-directed mutagenesis with circular dichroism, fluorescence spectroscopy, ATPase and client-binding assays, and SPR\",\n      \"pmids\": [\"33741370\", \"34141839\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"the linker's role in intact parasites not tested by allelic replacement\",\n        \"high-resolution structure of the full-length protein not determined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown how HSP110c's holdase and putative nucleotide-exchange functions are integrated within the parasite cytosolic chaperone network in vivo and which endogenous clients it engages during a febrile cycle.\",\n      \"evidence\": \"no direct experimental evidence in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"in vivo client interactome undefined\",\n        \"no structural model of client or co-chaperone complexes\",\n        \"NEF activity not demonstrated by functional exchange assay\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051082\", \"supporting_discovery_ids\": [0, 1, 3]},\n      {\"term_id\": \"GO:0016887\", \"supporting_discovery_ids\": [2, 3]},\n      {\"term_id\": \"GO:0000774\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0051087\", \"supporting_discovery_ids\": [1, 4]},\n      {\"term_id\": \"GO:0042803\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0009408\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0042026\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"PfHsp70-1\",\n      \"PfHsp40\"\n    ],\n    \"other_free_text\": [\n      \"Essential in P. falciparum: gene knockout lethal, conditional knockdown lethal upon heat shock [#0]\",\n      \"Holdase-only chaperone; rigid linker prevents refoldase activity [#3]\",\n      \"Prevents aggregation of asparagine repeat-containing clients including PFI1155w; more effective than human and yeast orthologs [#0]\",\n      \"Rigid linker segment confers thermal stability and tunes client binding, ATPase and ATP-binding affinity, and co-chaperone interactions [#3, #4]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0708800","name":null,"product":"heat shock protein 110","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1219300","name":null,"product":"heat shock protein 110, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0107400","name":null,"product":"heat shock protein 110, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"HSP110c","evaluation":null}