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https://doi.org/10.2139/ssrn.4670632

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inferredcites →https://doi.org/10.1002/prot.25600openalex-extracted
Structural and biochemical characterization of Plasmodium falciparum Hsp70‐x reveals functional versatility of its C‐terminal EEVN motif
inferredcites →https://doi.org/10.1007/978-3-030-78397-6_3openalex-extracted
The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum
inferredcites →https://doi.org/10.1007/s00018-004-4464-6openalex-extracted
Hsp70 chaperones: Cellular functions and molecular mechanism
inferredcites →https://doi.org/10.1007/s00438-005-1150-9openalex-extracted
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/s12192-011-0299-xopenalex-extracted
Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
inferredcites →https://doi.org/10.1007/s12192-011-0307-1openalex-extracted
Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)
inferredcites →https://doi.org/10.1007/s12192-016-0678-4openalex-extracted
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/s12551-019-00563-wopenalex-extracted
Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins
inferredcites →https://doi.org/10.1016/j.bpj.2013.11.1446openalex-extracted
Allosteric Opening of the Polypeptide-Binding Site When an Hsp70 Binds ATP
inferredcites →https://doi.org/10.1016/j.cell.2008.05.022openalex-extracted
Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding
inferredcites →https://doi.org/10.1016/j.celrep.2015.03.063openalex-extracted
Hsp70 Forms Antiparallel Dimers Stabilized by Post-translational Modifications to Position Clients for Transfer to Hsp90
inferredcites →https://doi.org/10.1016/j.febslet.2015.10.034openalex-extracted
GroEL to DnaK chaperone network behind the stability modulation of σ32 at physiological temperature in Escherichia coli
inferredcites →https://doi.org/10.1016/j.ijbiomac.2021.03.056openalex-extracted
Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone
inferredcites →https://doi.org/10.1016/j.ijbiomac.2023.128070openalex-extracted
Insertion of GGMP repeat residues of Plasmodium falciparum Hsp70-1 in the lid of DnaK adversely impacts client recognition
inferredcites →https://doi.org/10.1016/j.molcel.2007.08.022openalex-extracted
Structural Basis of J Cochaperone Binding and Regulation of Hsp70
inferredcites →https://doi.org/10.1016/j.molcel.2008.05.006openalex-extracted
Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine
inferredcites →https://doi.org/10.1021/pr070540wopenalex-extracted
Improving Sensitivity by Probabilistically Combining Results from Multiple MS/MS Search Methodologies
inferredcites →https://doi.org/10.1038/356683a0openalex-extracted
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
inferredcites →https://doi.org/10.1038/nrm2941openalex-extracted
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
inferredcites →https://doi.org/10.1038/s41594-018-0177-7openalex-extracted
The multiple facets of the Hsp90 machine
inferredcites →https://doi.org/10.1074/jbc.271.31.18471openalex-extracted
Effect of Nucleotides, Peptides, and Unfolded Proteins on the Self-association of the Molecular Chaperone HSC70
inferredcites →https://doi.org/10.1074/jbc.272.13.8744openalex-extracted
The COOH-terminal Peptide Binding Domain Is Essential for Self-association of the Molecular Chaperone HSC70
inferredcites →https://doi.org/10.1074/jbc.273.6.3679openalex-extracted
Hop Modulates hsp70/hsp90 Interactions in Protein Folding
inferredcites →https://doi.org/10.1074/jbc.m114.596288openalex-extracted
A Functional DnaK Dimer Is Essential for the Efficient Interaction with Hsp40 Heat Shock Protein
inferredcites →https://doi.org/10.1074/mcp.ra118.001044openalex-extracted
Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding*
inferredcites →https://doi.org/10.1128/jb.01131-08openalex-extracted
Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies
inferredcites →https://doi.org/10.1128/jb.169.1.283-290.1987openalex-extracted
Escherichia coli dnaK null mutants are inviable at high temperature
inferredcites →https://doi.org/10.1371/journal.pone.0067961openalex-extracted
Hsp70 Oligomerization Is Mediated by an Interaction between the Interdomain Linker and the Substrate-Binding Domain
inferredcites →https://doi.org/10.1371/journal.pone.0135326openalex-extracted
Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity
inferredcites →https://doi.org/10.1379/1466-1268(2000)005<0276:thagsp>2.0.co;2openalex-extracted
The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s
inferredcites →https://doi.org/10.2174/092986608786071067openalex-extracted
Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses
inferredcites →https://doi.org/10.3389/fmicb.2018.01737openalex-extracted
Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis
inferredcites →https://doi.org/10.3389/fmolb.2015.00022openalex-extracted
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation
inferredcites →https://doi.org/10.3389/fmolb.2021.694012openalex-extracted
The Hsp70-Chaperone Machines in Bacteria
inferredcites →https://doi.org/10.3390/biom10060856openalex-extracted
Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone
inferredcites →https://doi.org/10.3390/biom9100543openalex-extracted
The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function
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