HSP70x

PF3D7_0831700 · heat shock protein 70

Annotated: 2026-09-08

68 papers in source corpus 17 papers cited in narrative 17 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0831700 (HSP70x) is a Plasmodium falciparum-encoded Hsp70-class molecular chaperone that is exported into the host erythrocyte, where it supports the trafficking and surface display of parasite virulence proteins (PMID:22925632, PMID:28732045). It is expressed maximally at the schizont stage and traffics from the parasite through the parasitophorous vacuole into the host cell, localizing to mobile J-dots and to Maurer's clefts (PMID:22925632, PMID:23340228). Export depends on a short 7-residue targeting motif immediately downstream of an N-terminal hydrophobic secretory signal; this signal is acetylated rather than cleaved (unlike PEXEL proteins), and translocation across the parasitophorous vacuole membrane requires the PTEX translocon (PMID:27824087). Within the host cell HSP70x assembles with the exported Hsp40/J-domain co-chaperones PFA0660w and PFE0055c, which selectively stimulate its ATPase activity relative to human Hsp70, and it directly binds the cytoplasmic tail of PfEMP1, forming a ternary chaperone complex that promotes PfEMP1 export and cytoadherence (PMID:26845441, PMID:30804381, PMID:33236291). Functionally, HSP70x is dispensable for intraerythrocytic growth under standard conditions, but its loss delays PfEMP1 export, reduces adhesion, and increases infected-erythrocyte rigidity, and the chaperone specifically supports parasite growth under febrile-temperature heat stress (PMID:28732045, PMID:28959740, PMID:31690116). Its catalytic (ATPase) and substrate-binding domains have been crystallized and closely resemble human erythrocytic Hsp70, though non-conserved residues near the nucleotide-binding pocket provide handles for selective inhibition (PMID:31690116, PMID:33006578, PMID:34341192). The chaperone is also directly engaged by human granzyme B via its conserved TKD motif, and its C-terminal EEVN motif contributes to ATPase activity, co-chaperone interaction, and binding to human Hop (PMID:30183110, PMID:37074531).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps

2012 High
Established that HSP70x is a parasite chaperone that actually functions inside the host cell rather than the parasite, defining its unusual exported role.

Evidence Co-IP, immunofluorescence, and fractionation localizing it to J-dots with exported Hsp40s and PfEMP1

PMID:22925632
Open questions at the time
- Did not establish the export signal or translocation route
- Association with PfEMP1 not shown to be direct
2013 Medium
Refined the localization by showing stage-specific (schizont) expression with a parasitophorous-vacuole pool and a partial exported pool at Maurer's clefts, and confirmed the gene is functional.

Evidence Dual-detergent fractionation and immunofluorescence with peptide-specific antiserum

PMID:23340228
Open questions at the time
- Mechanism partitioning PV-retained versus exported protein unknown
- Single-lab localization
2014 Medium
Provided the first biochemical demonstration that HSP70x has intrinsic chaperone activity and is Hsp40-stimulated, and that it can be selectively inhibited over human Hsp70.

Evidence In vitro ATPase and aggregation-suppression assays with malonganenone A inhibition

PMID:24854538
Open questions at the time
- In vitro only
- Physiological substrates not identified
2016 High
Defined the export determinant and its unusual processing, and identified PFA0660w as a functionally selective co-chaperone, together explaining how HSP70x reaches and operates in the host cell.

Evidence Mutagenesis/GFP reporters plus acetylation mass spectrometry (export); ATPase and binding assays (co-chaperone selectivity)

PMID:26845441 PMID:27824087
Open questions at the time
- Machinery reading the non-cleaved acetylated motif unknown
- Structural basis of PFA0660w selectivity not resolved
2017 High
Tested essentiality and virulence roles genetically, converging on a model in which HSP70x is dispensable for growth but contributes to PfEMP1 export and cytoadherence.

Evidence Two independent knockout/knockdown studies with cytoadherence, rigidity, and export readouts

PMID:28732045 PMID:28959740
Open questions at the time
- The two studies differ on whether PfEMP1 export is affected
- Molecular step where HSP70x acts on PfEMP1 not pinpointed
2018 Medium
Mapped functional roles to the C-terminal EEVN motif, linking it to ATPase activity, chaperone function, and Hop interaction.

Evidence In vitro ATPase, aggregation-suppression, and pull-down assays with an EEVN-deletion mutant

PMID:30183110
Open questions at the time
- Hop interaction not validated in vivo
- Single-lab in vitro reconstitution
2019 Medium
Provided direct biochemical evidence for the PfEMP1-chaperone ternary complex and, structurally, resolved the ATPase domain while linking HSP70x to survival under febrile heat stress.

Evidence Recombinant ternary-complex binding/ATPase assays; X-ray crystallography plus heat-stress growth assays

PMID:30804381 PMID:31690116
Open questions at the time
- Ternary complex not validated in vivo
- How heat-stress protection relates to PfEMP1 role unclear
2020 Medium
Extended the structural and co-chaperone picture by resolving the substrate-binding domain and showing PFE0055c is a stronger, still parasite-selective ATPase stimulator with defined inhibitor pharmacology.

Evidence X-ray crystallography of SBD-peptide complex; ATPase assays with JDP/Hsp70 inhibitors

PMID:33006578 PMID:33236291
Open questions at the time
- High similarity to human Hsp70 complicates selective targeting
- Relative in vivo roles of PFA0660w vs PFE0055c unknown
2021 High
Identified druggable pockets on the ATPase domain and a distinguishing non-conserved residue, advancing HSP70x as a selective antimalarial target.

Evidence Fragment screening and crystallography of ligand-bound ATPase domain

PMID:34341192
Open questions at the time
- No potent lead compound established
- Cellular efficacy not demonstrated
2023 Medium
Revealed a host-immune interaction, showing human granzyme B binds HSP70x via its TKD motif with antiplasmodial consequences.

Evidence ELISA, slot blot, SPR binding, and growth inhibition assays

PMID:37074531
Open questions at the time
- In vivo relevance of GrB engagement unknown
- Mechanism of antiplasmodial activity unresolved
2024 Medium
Extended the trafficking role to sexual stages by linking HSP70x to SBP1 and Maurer's-cleft-associated structures in gametocyte-infected cells.

Evidence Co-IP/mass spectrometry and immunofluorescence in gametocyte-infected erythrocytes

PMID:38331312
Open questions at the time
- Functional consequence of the SBP1 interaction not tested
- Single Co-IP without reciprocal validation
2026 Low
Two studies further probed co-chaperone promiscuity and the export route, suggesting exported JDPs can also stimulate human Hsp70s and that EV/ESCRT trafficking contributes to HSP70x export during heat stress.

Evidence In vitro ATPase assays with J-domain fragments; PfVps60 knockout with EV proteomics

PMID:41618743 PMID:42253101
Open questions at the time
- EV-export evidence is indirect and secondary to a PfVps60-focused study
- Whether host-Hsp70 hijacking occurs in vivo is untested

Open questions

Synthesis pass · forward-looking unresolved questions

The endogenous substrate repertoire of HSP70x in the host cell and the mechanistic step by which the chaperone complex promotes PfEMP1 surface display remain undefined.
No comprehensive in-cell client identification
Structural basis of PfEMP1 tail recognition unresolved
Discrepant KO phenotypes on PfEMP1 export not reconciled

Mechanism profile

Synthesis pass · controlled-vocabulary classification

Partners

HUMAN GRANZYME B HUMAN HOP (HSP70-HSP90 ORGANIZING PROTEIN)PFA0660W (EXPORTED HSP40/J-DOMAIN PROTEIN)PFE0055C (EXPORTED J-DOMAIN PROTEIN)PFEMP1 (CYTOPLASMIC TAIL)PTEX TRANSLOCON (EXPORT REQUIREMENT)SBP1 (SKELETON BINDING PROTEIN 1)

Complex memberships

PfHsp70-x / PFA0660w / PfEMP1 ternary complexPfHsp70-x / PFA0660w J-dot chaperone complexPfHsp70-x / PFE0055c chaperone-cochaperone pair

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus

Year	Finding	Method	Journal	Conf	PMIDs
2012	HSP70x (PfHsp70-x) is exported to the host erythrocyte where it forms a complex with exported PfHsp40s (PFA0660w and PFE55) in mobile structures termed J-dots, and is closely associated with PfEMP1; the protein was identified as a parasite-encoded chaperone operating within the host cell.	Co-immunoprecipitation, immunofluorescence microscopy, subcellular fractionation, Western blotting	Cellular microbiology	High	22925632
2013	PfHsp70-x is expressed maximally at the schizont stage, localizes primarily to the parasitophorous vacuole, and a portion is exported to the erythrocyte compartment where it associates with Maurer's clefts; it carries an endoplasmic reticulum signal peptide and is encoded by a functional (not pseudo) gene.	Subcellular fractionation (saponin and streptolysin-O), immunofluorescence, immunoblotting with peptide-specific antiserum	Parasite (Paris, France)	Medium	23340228
2016	Trafficking of PfHsp70-x to the host erythrocyte requires a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal; both reversed and scrambled versions of the motif retained export capacity, but site-directed mutagenesis of glutamate residues within this region blocked trafficking within the parasitophorous vacuole lumen. Unlike PEXEL-containing proteins, the targeting signal is not cleaved but is acetylated. Export also requires the vacuolar translocon PTEX.	Site-directed mutagenesis, GFP reporter constructs, immunofluorescence microscopy, mass spectrometry (acetylation detection)	Scientific reports	High	27824087
2017	Knockout of PfHsp70-x (Δhsp70-x) did not affect parasite growth in vitro, but delayed export of PfEMP1 cytoadherence proteins and resulted in reduced adhesion of infected erythrocytes and increased rigidity of infected erythrocytes compared to wild-type controls.	Gene knockout, cytoadherence assays, erythrocyte rigidity measurements, transcriptional and translational profiling	PloS one	High	28732045
2017	Complete CRISPR/Cas9 gene knockout of PfHsp70x, as well as knockdown using DHFR-based destabilization domain and glmS ribozyme, did not affect P. falciparum intraerythrocytic growth or export of PfEMP1 to the host RBC.	CRISPR/Cas9 gene knockout, conditional knockdown (DHFR destabilization domain, glmS ribozyme), immunofluorescence, growth assays	mSphere	High	28959740
2016	PFA0660w (an exported Hsp40/J-domain protein) specifically stimulates the ATPase activity of PfHsp70-x but not that of PfHsp70-1 or human Hsp70, indicating a selective functional co-chaperone/chaperone partnership; protein binding studies confirmed a direct interaction dependent on the J domain.	ATPase activity assay, protein aggregation suppression assay, co-chaperone binding studies (protein binding in presence/absence of ATP)	PloS one	Medium	26845441
2018	The C-terminal EEVN motif of PfHsp70-x is important for its ATPase activity, chaperone function (protein aggregation suppression), and direct interaction with human Hsp70-Hsp90 organizing protein (hHop) in vitro; deletion of the EEVN motif (PfHsp70-xT) reduced these activities.	In vitro ATPase assay, protein aggregation suppression assay, pull-down/binding assay with recombinant proteins	Proteins	Medium	30183110
2014	PfHsp70-x possesses intrinsic chaperone activity (protein aggregation suppression) that is stimulated by Hsp40 co-chaperones; malonganenone A inhibits PfHsp70-x Hsp40-stimulated ATPase activity and its aggregation suppression activity, and disrupts the interaction between PfHsp70-x and Hsp40, selectively over human Hsp70.	ATPase activity assay, protein aggregation suppression assay, small-molecule inhibition studies	Biological chemistry	Medium	24854538
2019	Crystallographic structures of the PfHsp70-x catalytic (ATPase) domain were resolved, revealing high similarity to human Hsp70 chaperones but identifying specific sites that may allow selective inhibition; the J-domain of its stimulatory Hsp40 co-chaperone was also structurally characterized. PfHsp70-x supports parasite growth under elevated temperature conditions simulating febrile episodes, especially early in the intraerythrocytic life cycle.	X-ray crystallography, biochemical/biophysical analyses, parasite growth assays under heat stress	FASEB journal	High	31690116
2020	The crystal structure of the substrate-binding domain (SBD) of PfHsp70-x was resolved in complex with a hydrophobic peptide, showing the SBD is highly similar to the counterpart from human erythrocytic Hsp70, with conserved substrate binding at the interface between the β-sandwich and α-helical subdomains.	X-ray crystallography	Acta crystallographica. Section F, Structural biology communications	High	33006578
2021	Fragment screening against the PfHsp70-x ATPase domain identified two binding sites, with most ligands binding proximal to the nucleotide-binding pocket; crystallographic structures of the ATPase domain in complex with three chemical fragments were determined. One non-conserved residue near the ligand-binding site distinguishes PfHsp70-x from human erythrocytic chaperones.	Fragment screening, X-ray crystallography of ligand-bound ATPase domain	Acta crystallographica. Section F, Structural biology communications	High	34341192
2019	PfHsp70-x directly interacts with the cytoplasmic tail of PfEMP1 in vitro, and simultaneously binds cholesterol-bound PFA0660w to form a ternary complex (PfHsp70-x / PFA0660w / PfEMP1); the N-terminal domain of PFA0660w and C-terminal domain of PfHsp70-x are critical for their interaction.	Recombinant protein biochemical assays, direct binding assays (pull-down/co-incubation), ATPase activity assays	Scientific reports	Medium	30804381
2020	The exported J-domain protein PFE0055c specifically stimulates the basal ATPase activity of PfHsp70-x to a greater extent than PFA0660w, but does not significantly stimulate human Hsp70 ATPase activity, confirming a specific co-chaperone/chaperone partnership. The Hsp70 inhibitors JG231 and JG98 inhibit both basal and PFE0055c-stimulated ATPase activity of PfHsp70-x; C86 (a JDP inhibitor) only inhibits PFE0055c-stimulated activity, consistent with PFE0055c engaging PfHsp70-x via its J domain.	ATPase activity assay, small-molecule inhibition studies with JDP and Hsp70 inhibitors	Cell stress & chaperones	Medium	33236291
2023	Human granzyme B (GrB) directly binds PfHsp70-x in vitro with higher affinity than for human Hsp70; the TKD motif of PfHsp70-x mediates GrB binding, and the C-terminal EEVN motif augments (but is not prerequisite for) this affinity. GrB displays antiplasmodial activity (IC50 ~0.5 µM) in vitro.	ELISA, slot blot assay, surface plasmon resonance (SPR), growth inhibition assay	Cell stress & chaperones	Medium	37074531
2024	Skeleton binding protein 1 (SBP1) co-immunoprecipitates with PfHSP70-x in gametocyte-infected erythrocytes (identified by mass spectrometry), and some PfHSP70-x localizes to dot-like structures in the cytoplasm of immature gametocyte-infected erythrocytes, suggesting PfHSP70-x participates in protein trafficking via Maurer's clefts during gametocyte stages.	Co-immunoprecipitation, mass spectrometry, immunofluorescence microscopy	Parasitology international	Medium	38331312
2026	In vitro ATPase assays demonstrate that isolated J-domains from three exported PfJDPs (PFA0660w, PFE0055c, and a third homolog) all stimulate the ATPase activity of PfHSP70-x (as well as human HsHSP70 and HsHSC70), with differences observed in stimulation magnitude between individual PfJDP-HSP70 pairings, supporting a model where the parasite exports JDPs to exploit host chaperone machinery.	In vitro ATPase activity assay with recombinant J-domain fragments and recombinant HSP70 proteins	FEBS open bio	Medium	41618743
2026	In a PfVps60 knockout line disrupting ESCRT-dependent vesicular trafficking, PfHsp70-x was reduced among EV-associated cargo during thermal stress, and protein aggregates redistributed near the parasitophorous vacuole, indicating that PfHsp70-x is normally exported via EV-mediated trafficking as part of the parasite's proteostasis response to heat shock.	Gene knockout (PfVps60KO), proteomic profiling of extracellular vesicle cargo, fluorescence microscopy of protein aggregates, parasite viability assays	Emerging microbes & infections	Low	42253101

Source papers

Stage 0 corpus · 68 papers · ranked by NIH iCite citations

Year	Title	Journal	Citations	PMID
1994	Demonstration of heat-shock protein 70 in the sporozoite stage of malaria parasites.	Parasitology research	182	8153120
1986	A repetitive antigen of Plasmodium falciparum that is homologous to heat shock protein 70 of Drosophila melanogaster.	Proceedings of the National Academy of Sciences of the United States of America	159	3095842
1991	Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family.	Molecular and biochemical parasitology	144	1779989
2012	Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte.	Cellular microbiology	119	22925632
2007	The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum.	Protein science : a publication of the Protein Society	103	17766381
2011	Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis.	Protein and peptide letters	90	20955165
2004	Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70.	Protein expression and purification	61	14711509
2011	Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop).	Cell stress & chaperones	59	22005844
2019	The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite.	FASEB journal : official publication of the Federation of American Societies for Experimental Biology	52	31690116
2005	Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain.	Molecular genetics and genomics : MGG	51	15973516
2017	The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites.	PloS one	49	28732045
2014	Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity.	Biological chemistry	49	24854538
2010	Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock.	Cell stress & chaperones	49	21191678
2011	Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1.	Biological chemistry	48	21426241
2008	Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses.	Protein and peptide letters	47	19075824
2017	The Exported Chaperone PfHsp70x Is Dispensable for the Plasmodium falciparum Intraerythrocytic Life Cycle.	mSphere	45	28959740
2011	Gold nanoparticle-based fluorescence immunoassay for malaria antigen detection.	Analytical and bioanalytical chemistry	44	22089818
2008	The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns.	The international journal of biochemistry & cell biology	43	18674634
2015	Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity.	PloS one	40	26267894
2017	Polymyxin B inhibits the chaperone activity of Plasmodium falciparum Hsp70.	Cell stress & chaperones	39	28455613
2015	Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein.	PloS one	39	26083397
2018	Structural and biochemical characterization of Plasmodium falciparum Hsp70-x reveals functional versatility of its C-terminal EEVN motif.	Proteins	38	30183110
2019	Cholesterol bound Plasmodium falciparum co-chaperone 'PFA0660w' complexes with major virulence factor 'PfEMP1' via chaperone 'PfHsp70-x'.	Scientific reports	37	30804381
2021	Design and synthesis of quinoline-pyrimidine inspired hybrids as potential plasmodial inhibitors.	European journal of medicinal chemistry	34	33744688
2016	J-dot targeting of an exported HSP40 in Plasmodium falciparum-infected erythrocytes.	International journal for parasitology	33	27063072
1998	Actin-binding proteins of invasive malaria parasites and the regulation of actin polymerization by a complex of 32/34-kDa proteins associated with heat shock protein 70kDa.	Molecular and biochemical parasitology	33	9662713
2016	The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x.	PloS one	31	26845441
2019	Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins.	Biophysical reviews	30	31280465
2013	Identification of an exported heat shock protein 70 in Plasmodium falciparum.	Parasite (Paris, France)	30	23340228
2007	Detection of malaria infection via latex agglutination assay.	Analytical chemistry	30	17511424
2014	Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives.	Parasitology	29	24666996
2013	Malaria proteomics: insights into the parasite-host interactions in the pathogenic space.	Journal of proteomics	27	24140976
2016	Trafficking of the exported P. falciparum chaperone PfHsp70x.	Scientific reports	25	27824087
2013	Plasmodium falciparum Hsp70-x: a heat shock protein at the host-parasite interface.	Journal of biomolecular structure & dynamics	24	24028577
1993	Expression of members of the heat-shock protein 70 family in the exoerythrocytic stages of Plasmodium berghei and Plasmodium falciparum.	Parasitology research	22	8475027
2020	Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership.	Cell stress & chaperones	21	33236291
2021	Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum.	Advances in experimental medicine and biology	16	34569022
2021	The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum.	Advances in experimental medicine and biology	13	34569021
2020	Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x.	Acta crystallographica. Section F, Structural biology communications	12	33006578
2019	Establishing Computational Approaches Towards Identifying Malarial Allosteric Modulators: A Case Study of Plasmodium falciparum Hsp70s.	International journal of molecular sciences	12	31717270
2023	The Plasmodium falciparum exported J domain proteins fine-tune human and malarial Hsp70s: pathological exploitation of proteostasis machinery.	Frontiers in molecular biosciences	11	37457831
2019	Structural insights into the binding mechanism of Plasmodium falciparum exported Hsp40-Hsp70 chaperone pair.	Computational biology and chemistry	11	31430682
1991	Lack of correlation between red cell invasion by merozoites and anti-heat shock protein-70 antibody levels in malaria patients' sera.	International journal for parasitology	11	1869355
2025	Two sides of the same coin: heat shock proteins as biomarkers and therapeutic targets for some complex diseases.	Frontiers in molecular biosciences	10	40051500
2015	Immunophilin-protein interactions in Plasmodium falciparum.	Parasitology	10	26156578
2012	Plasmodium yoelii blood-stage antigens newly identified by immunoaffinity using purified IgG antibodies from malaria-resistant mice.	Immunobiology	10	22658767
2007	Characterization of Plasmodium vivax heat shock protein 70 and evaluation of its value for serodiagnosis of tertian malaria.	Clinical and vaccine immunology : CVI	10	17229883
2016	Plasmodium falciparum Hep1 Is Required to Prevent the Self Aggregation of PfHsp70-3.	PloS one	9	27253881
2020	Chaperoning of asparagine repeat-containing proteins in Plasmodium falciparum.	Journal of parasitic diseases : official organ of the Indian Society for Parasitology	8	33184535
2017	Immunoproteomics of Plasmodium falciparum-infected red blood cell membrane fractions.	Memorias do Instituto Oswaldo Cruz	8	29211247
1991	Human response to a malaria vaccine candidate antigen.	Vaccine	7	1897303
2022	Neurotransmitters and molecular chaperones interactions in cerebral malaria: Is there a missing link?	Frontiers in molecular biosciences	6	36090033
2024	A promising class of antiprotozoal agents, design and synthesis of novel Pyrimidine-Cinnamoyl hybrids.	European journal of medicinal chemistry	5	39549508
1996	Molecular cloning and antigenic mapping of heat-shock protein 70 from the malaria species Plasmodium bergheI.	The American journal of tropical medicine and hygiene	5	8940993
2024	Phytochemical evaluation of Ziziphus mucronata and Xysmalobium undulutum towards the discovery and development of anti-malarial drugs.	Malaria journal	4	38734650
2023	Artemisinin resistance in P. falciparum: probing the interacting partners of Kelch13 protein in parasite.	Journal of global antimicrobial resistance	4	37633420
2023	Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro.	Cell stress & chaperones	3	37074531
2021	Structures of the Plasmodium falciparum heat-shock protein 70-x ATPase domain in complex with chemical fragments identify conserved and unique binding sites.	Acta crystallographica. Section F, Structural biology communications	3	34341192
2009	The effect of mimicking febrile temperature and drug stress on malarial development.	Annals of clinical microbiology and antimicrobials	3	19523215
2024	Understanding the complex formation of falstatin; an endogenous macromolecular inhibitor of falcipains.	International journal of biological macromolecules	2	38460641
2024	Avian malaria in a feral-pet pigeon: a case report.	Malaria journal	2	39358742
2026	Promiscuous stimulation of HSP70 ATPase activity by parasite-derived J-domains.	FEBS open bio	1	41618743
2026	Flow cytometry-based evaluation of hepatic infection by non-fluorescent Plasmodium parasites.	International journal for parasitology	0	41864451
2026	Is the Association of Granzyme B and the Exported Parasite Hsp70 a Possible Trojan Horse of Severe Malaria?	Advances in experimental medicine and biology	0	42213323
2026	Extracellular vesicles participate in proteostasis and heat shock adaptation in Plasmodium falciparum.	Emerging microbes & infections	0	42253101
2026	Plasmodium falciparum leucine-rich repeat 5 disruption alters the transcription progression during asexual and sexual stage development.	mSphere	0	42294623
2024	Skeleton binding protein 1 localizes to the Maurer's cleft and interacts with PfHSP70-1 and PfHSP70-x in Plasmodium falciparum gametocyte-infected erythrocytes.	Parasitology international	0	38331312
2024	Iso-mukaadial acetate and ursolic acid acetate bind to Plasmodium Falciparum heat shock protein 70: towards targeting parasite protein folding pathway.	BMC chemistry	0	38500145