On the public citation graph

Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone

0 signed · 90 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.

Claim with ORCID

Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.

See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0282(199905)49:6<451::aid-bip3>3.0.co;2-6openalex-snapshot

1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent

inferredcites →https://doi.org/10.1002/prot.25600openalex-snapshot

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

inferredcites →https://doi.org/10.1006/jmbi.1994.1043openalex-snapshot

Specificity of DnaK-peptide Binding

inferredcites →https://doi.org/10.1007/s00018-004-4464-6openalex-snapshot

Hsp70 chaperones: Cellular functions and molecular mechanism

inferredcites →https://doi.org/10.1007/s00018-006-6192-6openalex-snapshot

The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones

inferredcites →https://doi.org/10.1007/s00438-005-1150-9openalex-snapshot

Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain

inferredcites →https://doi.org/10.1007/s12192-010-0250-6openalex-snapshot

Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock

inferredcites →https://doi.org/10.1007/s12192-011-0307-1openalex-snapshot

Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)

inferredcites →https://doi.org/10.1007/s12192-014-0526-3openalex-snapshot

C-terminal amino acids are essential for human heat shock protein 70 dimerization

inferredcites →https://doi.org/10.1007/s12192-016-0678-4openalex-snapshot

Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion

inferredcites →https://doi.org/10.1007/s12192-017-0797-6openalex-snapshot

Polymyxin B inhibits the chaperone activity of Plasmodium falciparum Hsp70

inferredcites →https://doi.org/10.1007/s12551-019-00563-wopenalex-snapshot

Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins

inferredcites →https://doi.org/10.1016/j.biocel.2006.11.006openalex-snapshot

Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK

inferredcites →https://doi.org/10.1016/j.bmc.2009.01.024openalex-snapshot

Select pyrimidinones inhibit the propagation of the malarial parasite, Plasmodium falciparum

inferredcites →https://doi.org/10.1016/j.bpc.2009.03.006openalex-snapshot

Hsp70-1 from Plasmodium falciparum: Protein stability, domain analysis and chaperone activity

inferredcites →https://doi.org/10.1016/j.febslet.2015.07.040openalex-snapshot

Functionality of Class A and Class B J‐protein co‐chaperones with Hsp70

inferredcites →https://doi.org/10.1016/j.jmb.2012.11.028openalex-snapshot

Structure and Allostery of the Chaperonin GroEL

inferredcites →https://doi.org/10.1016/j.molbiopara.2004.05.016openalex-snapshot

Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum

inferredcites →https://doi.org/10.1016/j.molbiopara.2011.07.004openalex-snapshot

Biochemical characterisation and novel classification of monofunctional S-adenosylmethionine decarboxylase of Plasmodium falciparum

inferredcites →https://doi.org/10.1016/j.molcel.2012.09.023openalex-snapshot

Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones

inferredcites →https://doi.org/10.1016/j.pep.2003.09.010openalex-snapshot

Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70

inferredcites →https://doi.org/10.1016/j.pep.2011.01.005openalex-snapshot

Co-expression of the Plasmodium falciparum molecular chaperone, PfHsp70, improves the heterologous production of the antimalarial drug target GTP cyclohydrolase I, PfGCHI

inferredcites →https://doi.org/10.1016/j.tibs.2013.08.001openalex-snapshot

Hsp70 chaperone dynamics and molecular mechanism

inferredcites →https://doi.org/10.1016/j.tibs.2017.02.007openalex-snapshot

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

inferredcites →https://doi.org/10.1016/s0014-5793(04)00290-xopenalex-snapshot

cis‐Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ‐binding peptides

inferredcites →https://doi.org/10.1016/s0092-8674(01)00517-7openalex-snapshot

Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

inferredcites →https://doi.org/10.1016/s1471-4922(01)01908-0openalex-snapshot

Targeting polyamines of parasitic protozoa in chemotherapy

inferredcites →https://doi.org/10.1021/bi0263208openalex-snapshot

Kinetic Analysis of Interdomain Coupling in a Lidless Variant of the Molecular Chaperone DnaK: DnaK's Lid Inhibits Transition to the Low Affinity State

inferredcites →https://doi.org/10.1021/cr0404390openalex-snapshot

Probing Protein Folding and Conformational Transitions with Fluorescence

inferredcites →https://doi.org/10.1021/ja5055252openalex-snapshot

Nucleotide-Dependent Interactions within a Specialized Hsp70/Hsp40 Complex Involved in Fe–S Cluster Biogenesis

inferredcites →https://doi.org/10.1038/76819openalex-snapshot

Multistep mechanism of substrate binding determines chaperone activity of Hsp70.

inferredcites →https://doi.org/10.1038/ncomms2306openalex-snapshot

Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers

inferredcites →https://doi.org/10.1038/nrm2941openalex-snapshot

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

inferredcites →https://doi.org/10.1073/pnas.0903503106openalex-snapshot

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

inferredcites →https://doi.org/10.1073/pnas.88.7.2874openalex-snapshot

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

inferredcites →https://doi.org/10.1074/jbc.270.5.2183openalex-snapshot

The DnaK Chaperone System of Escherichia coli: Quaternary Structures and Interactions of the DnaK and GrpE Components

inferredcites →https://doi.org/10.1074/jbc.272.13.8744openalex-snapshot

The COOH-terminal Peptide Binding Domain Is Essential for Self-association of the Molecular Chaperone HSC70

inferredcites →https://doi.org/10.1074/jbc.m111.275057openalex-snapshot

Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity

inferredcites →https://doi.org/10.1074/jbc.m111.294728openalex-snapshot

The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation

inferredcites →https://doi.org/10.1074/jbc.m114.596288openalex-snapshot

A Functional DnaK Dimer Is Essential for the Efficient Interaction with Hsp40 Heat Shock Protein

inferredcites →https://doi.org/10.1074/jbc.ra118.002691openalex-snapshot

The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast

inferredcites →https://doi.org/10.1093/emboj/20.5.1042openalex-snapshot

Its substrate specificity characterizes the DnaJ co‐chaperone as a scanning factor for the DnaK chaperone

inferredcites →https://doi.org/10.1093/nar/gkh371openalex-snapshot

DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data

inferredcites →https://doi.org/10.1110/ps.072918107openalex-snapshot

The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum

inferredcites →https://doi.org/10.1111/j.1462-5822.2012.01840.xopenalex-snapshot

Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte

inferredcites →https://doi.org/10.1111/j.1574-695x.2009.00639.xopenalex-snapshot

Plasmodial heat shock proteins: targets for chemotherapy

inferredcites →https://doi.org/10.1126/science.272.5268.1606openalex-snapshot

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

inferredcites →https://doi.org/10.1128/jb.171.5.2337-2346.1989openalex-snapshot

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

inferredcites →https://doi.org/10.1371/journal.pone.0020047openalex-snapshot

Expression of a Malarial Hsp70 Improves Defects in Chaperone-Dependent Activities in ssa1 Mutant Yeast

inferredcites →https://doi.org/10.1371/journal.pone.0065912openalex-snapshot

Characterization of a Novel Putative S-Adenosylmethionine Decarboxylase-Like Protein from Leishmania donovani

inferredcites →https://doi.org/10.1371/journal.pone.0067961openalex-snapshot

Hsp70 Oligomerization Is Mediated by an Interaction between the Interdomain Linker and the Substrate-Binding Domain

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.0152626openalex-snapshot

Use of a Chimeric Hsp70 to Enhance the Quality of Recombinant Plasmodium falciparum S-Adenosylmethionine Decarboxylase Protein Produced in Escherichia coli

inferredcites →https://doi.org/10.1515/bc.2011.040openalex-snapshot

Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1

inferredcites →https://doi.org/10.2174/092986608786071067openalex-snapshot

Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses

inferredcites →https://doi.org/10.2174/092986611794475002openalex-snapshot

Intracellular Protozoan Parasites of Humans: The Role of Molecular Chaperones in Development and Pathogenesis

inferredcites →https://doi.org/10.2174/187152610791163417openalex-snapshot

Malaria Heat Shock Proteins: Drug Targets that Chaperone other Drug Targets

inferredcites →https://doi.org/10.3389/fmicb.2018.01737openalex-snapshot

Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis

inferredcites →https://doi.org/10.3389/fmolb.2015.00034openalex-snapshot

Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle

inferredcites →https://doi.org/10.3390/biom9070295openalex-snapshot

Partners in Mischief: Functional Networks of Heat Shock Proteins of Plasmodium falciparum and Their Influence on Parasite Virulence

inferredcites →https://doi.org/10.3390/biom9100543openalex-snapshot

The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function

inferredcites →https://doi.org/10.3390/ijms20235930openalex-snapshot

Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites

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.

inferred← citeshttps://doi.org/10.2139/ssrn.4670632openalex-extracted

inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_10openalex-snapshot

Heat Shock Proteins of Malaria: Highlights and Future Prospects

inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_3openalex-snapshot

The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum

inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_8openalex-snapshot

Bioprospecting for Novel Heat Shock Protein Modulators: The New Frontier for Antimalarial Drug Discovery?

inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_9openalex-snapshot

Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery

inferred← citeshttps://doi.org/10.1007/978-3-032-24254-9_5openalex-snapshot

Is the Association of Granzyme B and the Exported Parasite Hsp70 a Possible Trojan Horse of Severe Malaria?

inferred← citeshttps://doi.org/10.1007/s12551-021-00794-wopenalex-snapshot

Biophysical Reviews ‘Meet the editor series’—Addmore Shonhai

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2024.119824openalex-snapshot

Proteostasis is a key driver of the pathogenesis in Apicomplexa

inferred← citeshttps://doi.org/10.1016/j.bbapap.2023.140942openalex-snapshot

Distinct dynamical features of plasmodial and human HSP70-HSP110 highlight the divergence in their chaperone-assisted protein folding

inferred← citeshttps://doi.org/10.1016/j.bcab.2020.101833openalex-snapshot

Heterologous expression of heat shock proteins confers stress tolerance in Escherichia coli, an industrial cell factory: A short review

inferred← citeshttps://doi.org/10.1016/j.cstres.2024.03.007openalex-snapshot

Plasmodium falciparum heat shock proteins as antimalarial drug targets: An update

inferred← citeshttps://doi.org/10.1016/j.dib.2021.107177openalex-snapshot

Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70

inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e29690openalex-snapshot

Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.03.056openalex-snapshot

Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.128070openalex-snapshot

Insertion of GGMP repeat residues of Plasmodium falciparum Hsp70-1 in the lid of DnaK adversely impacts client recognition

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.130420openalex-snapshot

Understanding the complex formation of falstatin; an endogenous macromolecular inhibitor of falcipains

inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00120openalex-snapshot

Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers

inferred← citeshttps://doi.org/10.1021/acsomega.3c04494openalex-snapshot

Pharmacophore Model-Based Virtual Screening Workflow for Discovery of Inhibitors Targeting Plasmodium falciparum Hsp90

inferred← citeshttps://doi.org/10.1080/0035919x.2022.2144536openalex-snapshot

Exploring the application of ELISA and slot blot as utility protein–protein interaction analysis tools

inferred← citeshttps://doi.org/10.1515/bmc-2022-0008openalex-snapshot

The capture of host cell’s resources: The role of heat shock proteins and polyamines in SARS-COV-2 (COVID-19) pathway to viral infection

inferred← citeshttps://doi.org/10.3389/fcell.2022.921739openalex-snapshot

Plasmodium falciparum Molecular Chaperones: Guardians of the Malaria Parasite Proteome and Renovators of the Host Proteome

inferred← citeshttps://doi.org/10.3389/fmolb.2022.947203openalex-snapshot

Inhibition of Plasmodium falciparum Hsp70-Hop partnership by 2-phenylthynesulfonamide

inferred← citeshttps://doi.org/10.3389/fsufs.2026.1866725openalex-snapshot

A proteomic analysis of heat shock proteins from pigeonpea (Cajanus cajan) seed

inferred← citeshttps://doi.org/10.3390/ijms22042226openalex-snapshot

Mutation of GGMP Repeat Segments of Plasmodium falciparum Hsp70-1 Compromises Chaperone Function and Hop Co-Chaperone Binding

inferred← citeshttps://doi.org/10.3390/ijms22136776openalex-snapshot

Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue

inferred← citeshttps://doi.org/10.5772/intechopen.98852openalex-snapshot

A Double Line of Defense: Heat Shock Proteins and Polyamines Act as Contributing Factors to Drug Resistance of some Plasmodium Parasites

Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.