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Structural and biochemical characterization of Plasmodium falciparum Hsp70‐x reveals functional versatility of its C‐terminal EEVN motif

https://doi.org/10.1002/prot.25600
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Outgoing claims: the papers this work cites, builds on, or argues with.

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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding.
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Structural and biochemical characterization of Plasmodium falciparum Hsp70‐x reveals functional versatility of its C‐terminal EEVN motif
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The Role of Hsp70s in the Development and Pathogenicity of Plasmodium Species
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Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
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Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion
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Hsp70-1 from Plasmodium falciparum: Protein stability, domain analysis and chaperone activity
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Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum
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Plasmodium Hsp40 and human Hsp70: A potential cochaperone-chaperone complex
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Immunomodulatory activity of zinc peroxide (ZnO2) and titanium dioxide (TiO2) nanoparticles and their effects on DNA and protein integrity
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cis‐Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ‐binding peptides
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Mechanics of Hsp70 chaperones enables differential interaction with client proteins
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Trafficking of the exported P. falciparum chaperone PfHsp70x
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Proteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions
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Identification of an exported heat shock protein 70 inPlasmodium falciparum
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Host Chaperones Are Recruited in Membrane-bound Complexes byPlasmodium falciparum
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Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity
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The Assembly and Intermolecular Properties of the hsp70-Hop-hsp90 Molecular Chaperone Complex
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Not all J domains are created equal: Implications for the specificity of Hsp40–Hsp70 interactions
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The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum
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Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte
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Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte
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Plasmodial heat shock proteins: targets for chemotherapy
inferredcites →https://doi.org/10.1126/science.1102737openalex-snapshot
A Host-Targeting Signal in Virulence Proteins Reveals a Secretome in Malarial Infection
inferredcites →https://doi.org/10.1128/mcb.18.4.2023openalex-snapshot
The Carboxy-Terminal Domain of Hsc70 Provides Binding Sites for a Distinct Set of Chaperone Cofactors
inferredcites →https://doi.org/10.1128/msphere.00363-17openalex-snapshot
The Exported Chaperone PfHsp70x Is Dispensable for the Plasmodium falciparum Intraerythrocytic Life Cycle
inferredcites →https://doi.org/10.1186/1475-2875-9-236openalex-snapshot
Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients
inferredcites →https://doi.org/10.1371/journal.pone.0129445openalex-snapshot
Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein
inferredcites →https://doi.org/10.1371/journal.pone.0135326openalex-snapshot
Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity
inferredcites →https://doi.org/10.1371/journal.pone.0148517openalex-snapshot
The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x
inferredcites →https://doi.org/10.1371/journal.pone.0181656openalex-snapshot
The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites
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Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity
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Immunomodulatory activity of extracellular Hsp70 mediated via paired receptors Siglec‐5 and Siglec‐14
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Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses
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Intracellular Protozoan Parasites of Humans: The Role of Molecular Chaperones in Development and Pathogenesis
inferredcites →https://doi.org/10.3390/molecules22122139openalex-snapshot
(−)-Epigallocatechin-3-Gallate Inhibits the Chaperone Activity of Plasmodium falciparum Hsp70 Chaperones and Abrogates Their Association with Functional Partners

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum
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The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells
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Role of Heat Shock Proteins in Immune Modulation in Malaria
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Bioprospecting for Novel Heat Shock Protein Modulators: The New Frontier for Antimalarial Drug Discovery?
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Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery
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Hsp70/Hsp90 Organising Protein (Hop): Coordinating Much More than Chaperones
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Is the Association of Granzyme B and the Exported Parasite Hsp70 a Possible Trojan Horse of Severe Malaria?
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Plasmodium falciparum: Transporter and Drug Target
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Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1
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Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro
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Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins
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Chaperoning of asparagine repeat-containing proteins in Plasmodium falciparum
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Proteostasis is a key driver of the pathogenesis in Apicomplexa
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Distinct dynamical features of plasmodial and human HSP70-HSP110 highlight the divergence in their chaperone-assisted protein folding
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Plasmodium falciparum heat shock proteins as antimalarial drug targets: An update
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Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection
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Heat shock protein 70 of filarial parasite Setaria equina: Cloning, expression, and analysis of binding with diethylcarbamazine citrate
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Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone
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Insertion of GGMP repeat residues of Plasmodium falciparum Hsp70-1 in the lid of DnaK adversely impacts client recognition
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Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers
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Structural–functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding
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Exploring the application of ELISA and slot blot as utility protein–protein interaction analysis tools
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The Plasmodium falciparum Hsp70‐x chaperone assists the heat stress response of the malaria parasite
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Plasmodium falciparum Molecular Chaperones: Guardians of the Malaria Parasite Proteome and Renovators of the Host Proteome
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Heat shock proteins in osteoarthritis: molecular mechanisms, pathogenic roles, and therapeutic opportunities
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Inhibition of Plasmodium falciparum Hsp70-Hop partnership by 2-phenylthynesulfonamide
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Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone
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Partners in Mischief: Functional Networks of Heat Shock Proteins of Plasmodium falciparum and Their Influence on Parasite Virulence
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The Role of Non-Canonical Hsp70s (Hsp110/Grp170) in Cancer
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Establishing Computational Approaches Towards Identifying Malarial Allosteric Modulators: A Case Study of Plasmodium falciparum Hsp70s
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Trypanosoma brucei J-Protein 2 Functionally Co-Operates with the Cytosolic Hsp70 and Hsp70.4 Proteins
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Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites
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Mutation of GGMP Repeat Segments of Plasmodium falciparum Hsp70-1 Compromises Chaperone Function and Hop Co-Chaperone Binding
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Acanthospermum australe Extract Inhibits the Chaperone Activity of Plasmodium falciparum Heat Shock Protein 70-1
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