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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/j.1460-2075.1985.tb04056.xopenalex-snapshot
Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein.
inferredcites →https://doi.org/10.1002/j.1460-2075.1985.tb04094.xopenalex-snapshot
The 70‐kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles.
inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb03544.xopenalex-snapshot
Initiation of lambda DNA replication with purified host‐ and bacteriophage‐encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins.
inferredcites →https://doi.org/10.1007/bf00446910openalex-snapshot
A new bacterial gene (groPC) which affects λ DNA replication
inferredcites →https://doi.org/10.1016/0022-2836(77)90038-9openalex-snapshot
Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12
inferredcites →https://doi.org/10.1016/0092-8674(86)90532-5openalex-snapshot
Uncoating ATPase is a member of the 70 kilodalton family of stress proteins
inferredcites →https://doi.org/10.1016/0092-8674(86)90693-8openalex-snapshot
Speculations on the functions of the major heat shock and glucose-regulated proteins
inferredcites →https://doi.org/10.1016/0092-8674(86)90746-4openalex-snapshot
An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
inferredcites →https://doi.org/10.1016/0092-8674(90)90268-jopenalex-snapshot
The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
inferredcites →https://doi.org/10.1016/s0021-9258(17)36008-8openalex-snapshot
The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.
inferredcites →https://doi.org/10.1016/s0021-9258(17)39649-7openalex-snapshot
Purification and properties of the dnaJ replication protein of Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(17)47227-9openalex-snapshot
Purification and properties of the Escherichia coli dnaK replication protein.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43642-3openalex-snapshot
A prepriming DNA replication enzyme of Escherichia coli. II. Actions of protein n': a sequence-specific, DNA-dependent ATPase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)45398-7openalex-snapshot
The grpE protein of Escherichia coli. Purification and properties.
inferredcites →https://doi.org/10.1016/s0021-9258(18)81680-5openalex-snapshot
Heat Shock Protein-mediated Disassembly of Nucleoprotein Structures Is Required for the Initiation of Bacteriophage λ DNA Replication
inferredcites →https://doi.org/10.1016/s0021-9258(19)39727-3openalex-snapshot
Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication.
inferredcites →https://doi.org/10.1073/pnas.80.21.6431openalex-snapshot
The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system.
inferredcites →https://doi.org/10.1073/pnas.85.18.6632openalex-snapshot
Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication.
inferredcites →https://doi.org/10.1126/science.2188360openalex-snapshot
Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and Assembly
inferredcites →https://doi.org/10.1126/science.2756425openalex-snapshot
Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly
inferredcites →https://doi.org/10.1128/jb.167.1.25-29.1986openalex-snapshot
Escherichia coli grpE gene codes for heat shock protein B25.3, essential for both lambda DNA replication at all temperatures and host growth at high temperature
inferredcites →https://doi.org/10.1128/jb.168.2.931-935.1986openalex-snapshot
Escherichia coli DnaK protein possesses a 5'-nucleotidase activity that is inhibited by AppppA
inferredcites →https://doi.org/10.1128/jb.171.3.1590-1596.1989openalex-snapshot
Escherichia coli DnaK and GrpE heat shock proteins interact both in vivo and in vitro
inferredcites →https://doi.org/10.1128/jb.171.5.2748-2755.1989openalex-snapshot
The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds
inferredcites →https://doi.org/10.1128/mcb.5.6.1229openalex-snapshot
Rapid Purification of Mammalian 70,000-Dalton Stress Proteins: Affinity of the Proteins for Nucleotides
inferredcites →https://doi.org/10.1128/mcb.7.8.2863openalex-snapshot
Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines.
inferredcites →https://doi.org/10.1128/mcb.7.8.2863-2869.1987openalex-snapshot
Immunological Evidence for the Association of P53 with a Heat Shock Protein, hsc70, in p53-plus-ras-Transformed Cell Lines
inferredcites →https://doi.org/10.1128/mcb.8.3.1206openalex-snapshot
Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and dnaK from murine p53 by ATP.
inferredcites →https://doi.org/10.1128/mcb.8.3.1206-1215.1988openalex-snapshot
Purification of Complexes of Nuclear Oncogene p53 with Rat and Escherichia coli Heat Shock Proteins: In Vitro Dissociation of hsc70 and dnaK from Murine p53 by ATP
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.4788948openalex-extracted
Gmhsp40.1, a Nuclear-Localized Soybean Dnaj Domain-Containing Protein, Participates in Regulation of Flowering Time Through Interacting with Emf1 and Jmj14
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-gopenalex-snapshot
Analysis of a 36·2 kb DNA Sequence Including the Right Telomere of Chromosome VI from Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1002/(sici)1097-0061(19980330)14:5<419::aid-yea238>3.0.co;2-topenalex-snapshot
Heat shock transiently enhances the synthesis rate of Sis1p, a ribosome-associated DnaJ protein in the oleagenous yeastApiotrichum curvatum
inferred← citeshttps://doi.org/10.1002/0471203076.emm1261openalex-snapshot
Heat Shock Response: Cellular and Molecular Responses to Stress, Misfolded Proteins, and Diseases Associated with Protein Aggregation
inferred← citeshttps://doi.org/10.1002/1521-3757(20020402)114:7<1142::aid-ange1142>3.0.co;2-topenalex-snapshot
Molekulare Chaperone: zelluläre Maschinen für die Proteinfaltung
inferred← citeshttps://doi.org/10.1002/1521-3773(20020402)41:7<1098::aid-anie1098>3.0.co;2-9openalex-snapshot
Molecular Chaperones—Cellular Machines for Protein Folding
inferred← citeshttps://doi.org/10.1002/9783527610754.sf15openalex-snapshot
Chaperone Function in Vitro
inferred← citeshttps://doi.org/10.1002/9783527610754.sf19openalex-snapshot
Protein Folding in the Endoplasmic Reticulum
inferred← citeshttps://doi.org/10.1002/9783527619498.ch37openalex-snapshot
Characterization of ATPase Cycles of Molecular Chaperones by Fluorescence and Transient Kinetic Methods
inferred← citeshttps://doi.org/10.1002/9783527619498.ch38openalex-snapshot
Analysis of Chaperone Function in Vitro
inferred← citeshttps://doi.org/10.1002/9783527619498.ch48openalex-snapshot
Regulation of Hsp70 Chaperones by Co‐chaperones
inferred← citeshttps://doi.org/10.1002/9783527619498.ch49openalex-snapshot
Protein Folding in the Endoplasmic Reticulum Via the Hsp70 Family
inferred← citeshttps://doi.org/10.1002/aic.690420525openalex-snapshot
Model for ER chaperone dynamics and secretory protein interactions
inferred← citeshttps://doi.org/10.1002/bip.21302openalex-snapshot
Hsp70 molecular chaperones and Parkinson's disease
inferred← citeshttps://doi.org/10.1002/bip.21304openalex-snapshot
Interplay between protein homeostasis networks in protein aggregation and proteotoxicity
inferred← citeshttps://doi.org/10.1002/bip.22361openalex-snapshot
ATP‐driven molecular chaperone machines
inferred← citeshttps://doi.org/10.1002/bit.23111openalex-snapshot
Localization of BiP to translating ribosomes increases soluble accumulation of secreted eukaryotic proteins in an Escherichia coli cell‐free system
inferred← citeshttps://doi.org/10.1002/cbic.202100459openalex-snapshot
Novel Antibacterial Targets in Protein Biogenesis Pathways
inferred← citeshttps://doi.org/10.1002/dvg.1020160110openalex-snapshot
Tumor suppression in Drosophila is causally related to the function of the lethal(2)tumorous imaginal discs gene, a dnaJ homolog
inferred← citeshttps://doi.org/10.1002/iub.1272openalex-snapshot
The many functions of the endoplasmic reticulum chaperones and folding enzymes
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05029.xopenalex-snapshot
Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05983.xopenalex-snapshot
Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb06097.xopenalex-snapshot
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06433.xopenalex-snapshot
The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06469.xopenalex-snapshot
A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb00190.xopenalex-snapshot
Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07179.xopenalex-snapshot
The ClpX heat‐shock protein of Escherichia coli, the ATP‐dependent substrate specificity component of the ClpP‐ClpX protease, is a novel molecular chaperone.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07222.xopenalex-snapshot
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ‐1.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07351.xopenalex-snapshot
The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb00371.xopenalex-snapshot
A zinc finger‐like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb00393.xopenalex-snapshot
A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb00412.xopenalex-snapshot
Hsp60‐independent protein folding in the matrix of yeast mitochondria.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb00660.xopenalex-snapshot
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb00966.xopenalex-snapshot
The nucleotide exchange factor MGE exerts a key function in the ATP‐dependent cycle of mt‐Hsp70‐Tim44 interaction driving mitochondrial protein import.
inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb01082.xopenalex-snapshot
Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.
inferred← citeshttps://doi.org/10.1002/mco2.161openalex-snapshot
Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities
inferred← citeshttps://doi.org/10.1002/nadc.19970450210openalex-snapshot
Biochemie und Molekulargenetik 1996
inferred← citeshttps://doi.org/10.1002/pro.3223openalex-snapshot
The Hsp40 J‐domain modulates Hsp70 conformation and ATPase activity with a semi‐elliptical spring
inferred← citeshttps://doi.org/10.1002/pro.3725openalex-snapshot
Structural and functional analysis of the Hsp70/Hsp40 chaperone system
inferred← citeshttps://doi.org/10.1002/pro.4267openalex-snapshot
A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP)
inferred← citeshttps://doi.org/10.1002/pro.5190openalex-snapshot
Preferential binding of ADP ‐bound mitochondrial HSP70 to the nucleotide exchange factor GRPEL1 over GRPEL2
inferred← citeshttps://doi.org/10.1002/pro.5560010802openalex-snapshot
83‐Kilodalton heat shock proteins of trypanosomes are potent peptide‐stimulated ATPases
inferred← citeshttps://doi.org/10.1002/pro.5560050421openalex-snapshot
The mitochondrial protein import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
inferred← citeshttps://doi.org/10.1002/pro.5560070513openalex-snapshot
Isolation and characterization of a DnaJ‐like protein in rats: The C‐terminal 10‐kDa domain of hsc70 is not essential for stimulating the ATP‐hydrolytic activity of hsc70 by a DnaJ‐like protein
inferred← citeshttps://doi.org/10.1002/yea.320110109openalex-snapshot
Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX
inferred← citeshttps://doi.org/10.1006/abbi.1999.1354openalex-snapshot
N-Ethylmaleimide-Modified Hsp70 Inhibits Protein Folding
inferred← citeshttps://doi.org/10.1006/jmbi.1996.0762openalex-snapshot
Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1006/jmbi.1997.0947openalex-snapshot
Maturation of mammalian 20 S proteasome: purification and characterization of 13 S and 16 S proteasome precursor complexes
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1072openalex-snapshot
The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.Karn
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1131openalex-snapshot
Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1267openalex-snapshot
Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1815openalex-snapshot
Catapult mechanism renders the chaperone action of hsp70 unidirectional
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1816openalex-snapshot
Functional properties of the molecular chaperone DnaK from Thermus thermophilus
inferred← citeshttps://doi.org/10.1006/jmbi.1998.2465openalex-snapshot
Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system
inferred← citeshttps://doi.org/10.1006/jmbi.1998.2514openalex-snapshot
Mutations in the substrate binding domain of the Escherichia coli 70 kda molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling 1 1Edited by M. Gottesman
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2844openalex-snapshot
Investigation of the Interaction between DnaK and DnaJ by Surface Plasmon Resonance Spectroscopy
inferred← citeshttps://doi.org/10.1006/jmbi.2001.5013openalex-snapshot
The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1 1 1Edited by M. Yaniv
inferred← citeshttps://doi.org/10.1006/jmbi.2001.5116openalex-snapshot
Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response
inferred← citeshttps://doi.org/10.1006/niox.2001.0354openalex-snapshot
Nitric Oxide Inhibits the Cochaperone Activity of the RING Finger-like Protein DnaJ
inferred← citeshttps://doi.org/10.1006/prep.2000.1254openalex-snapshot
Expression of the Arabidopsis thaliana AtJ2 Cochaperone Protein in Pichia pastoris
inferred← citeshttps://doi.org/10.1006/viro.1998.9220openalex-snapshot
A Novel Human DnaJ Protein, hTid-1, a Homolog of the Drosophila Tumor Suppressor Protein Tid56, Can Interact with the Human Papillomavirus Type 16 E7 Oncoprotein
inferred← citeshttps://doi.org/10.1007/3-540-29717-0_1openalex-snapshot
Chaperones in Preventing Protein Denaturation in Living Cells and Protecting Against Cellular Stress
inferred← citeshttps://doi.org/10.1007/978-0-387-39717-7_9openalex-snapshot
Regulation of Hsp70 Function: Hsp40 Co-Chaperones and Nucleotide Exchange Factors
inferred← citeshttps://doi.org/10.1007/978-0-387-49310-7_1openalex-snapshot
Nucleotide Exchange Factors for Hsp70 Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-0-387-49310-7_3openalex-snapshot
Hop: An Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathways
inferred← citeshttps://doi.org/10.1007/978-1-4020-5585-0_17openalex-snapshot
Impact of HSP-Chaperoned Peptides on the MHC Class II-Dependent Presentation and Activation of CD4+ T Cells in Regard of Allo- and Autoantigens
inferred← citeshttps://doi.org/10.1007/978-1-4614-6157-9_11openalex-snapshot
Modeling of Hsp70-Mediated Protein Refolding
inferred← citeshttps://doi.org/10.1007/978-1-4615-0721-5_2openalex-snapshot
Protein Quality Control in Bacterial Cells: Integrated Networks of Chaperones and ATP-Dependent Proteases
inferred← citeshttps://doi.org/10.1007/978-1-4615-2894-4_14openalex-snapshot
Autoregulation of the Heat-Shock Response
inferred← citeshttps://doi.org/10.1007/978-1-4615-4707-5_6openalex-snapshot
Role of Bacterial Chaperones in DNA Replication
inferred← citeshttps://doi.org/10.1007/978-1-4899-1766-9_12openalex-snapshot
Pathways of Protein Remodeling by Escherichia Coli Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-1-4939-1136-3_13openalex-snapshot
Molecular Chaperone Functions in Plastids
inferred← citeshttps://doi.org/10.1007/978-1-4939-7477-1_13openalex-snapshot
Nucleotide Exchange Factors for Hsp70 Chaperones
inferred← citeshttps://doi.org/10.1007/978-1-61779-295-3_7openalex-snapshot
Nucleotide Exchange Factors for Hsp70 Chaperones
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_2openalex-snapshot
General Structural and Functional Features of Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-3-031-14740-1_13openalex-snapshot
HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease
inferred← citeshttps://doi.org/10.1007/978-3-0348-9088-5_2openalex-snapshot
Normal protein folding machinery
inferred← citeshttps://doi.org/10.1007/978-3-0348-9088-5_3openalex-snapshot
Roles for hsp70 in protein translocation across membranes of organelles
inferred← citeshttps://doi.org/10.1007/978-3-319-11731-7_4openalex-snapshot
Specification of Hsp70 Function by Type I and Type II Hsp40
inferred← citeshttps://doi.org/10.1007/978-3-319-23603-2_15openalex-snapshot
Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL
inferred← citeshttps://doi.org/10.1007/978-3-319-27647-2_10openalex-snapshot
The Unfolded Protein Response as a Therapeutic Target for Head and Neck Squamous Cell Carcinoma
inferred← citeshttps://doi.org/10.1007/978-3-319-69042-1_1openalex-snapshot
Hsp70-Substrate Interactions
inferred← citeshttps://doi.org/10.1007/978-3-319-90725-3_3openalex-snapshot
Heat Shock Proteins and Endoplasmic Reticulum Stress
inferred← citeshttps://doi.org/10.1007/978-3-319-91956-0_6openalex-snapshot
Molecular Chaperones: Key Players of Abiotic Stress Response in Plants
inferred← citeshttps://doi.org/10.1007/978-3-642-61126-1_8openalex-snapshot
Protein Folding In The Cell: The Role Of Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-3-642-76988-7_32openalex-snapshot
Bacteriophage λ DNA Replication and the Role of the Universally Conserved dnaK, dnaJ and grpE Heat Shock Proteins
inferred← citeshttps://doi.org/10.1007/978-3-642-78729-4_17openalex-snapshot
Function of Molecular Chaperones in Protein Folding
inferred← citeshttps://doi.org/10.1007/978-3-642-79133-8_1openalex-snapshot
The heat stress response as part of the plant stress network: An overview with six tables
inferred← citeshttps://doi.org/10.1007/978-3-642-79249-6_11openalex-snapshot
Replication: The Role of Escherichia coli Heat Shock Proteins in DNA Replication
inferred← citeshttps://doi.org/10.1007/978-3-642-79502-2_2openalex-snapshot
Heat-shock proteins as molecular chaperones
inferred← citeshttps://doi.org/10.1007/978-3-642-84921-3_18openalex-snapshot
Early Events in Protein Import into Mitochondria
inferred← citeshttps://doi.org/10.1007/978-3-662-02928-2_16openalex-snapshot
Molecular Chaperones HSP70 and HSP60 in Protein Folding and Membrane Translocation
inferred← citeshttps://doi.org/10.1007/978-3-662-02928-2_17openalex-snapshot
Cytosolic Reactions in Mitochondrial Protein Import
inferred← citeshttps://doi.org/10.1007/978-94-007-5943-5_1openalex-snapshot
A General Description of HSPs, The Molecular Structure of HSP70 and The HSP70 Cycle
inferred← citeshttps://doi.org/10.1007/978-94-007-7438-4_2openalex-snapshot
General Structural and Functional Features of Molecular Chaperones
inferred← citeshttps://doi.org/10.1007/978-94-009-0353-1_9openalex-snapshot
Molecular chaperones and protein folding in plants
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The Escherichia coli chaperones involved in DNA replication
inferred← citeshttps://doi.org/10.1007/978-94-011-4802-3_8openalex-snapshot
Transgenic Cereals — Zea mays (maize)
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Molecular Functions of Heat Shock Proteins
inferred← citeshttps://doi.org/10.1007/b136669openalex-snapshot
Chaperone proteins and peroxisomal protein import
inferred← citeshttps://doi.org/10.1007/bf00039383openalex-snapshot
Molecular chaperones and protein folding in plants
inferred← citeshttps://doi.org/10.1007/bf00042234openalex-snapshot
AtJ1, a mitochondrial homologue of theEscherichia coli DnaJ protein
inferred← citeshttps://doi.org/10.1007/bf00201389openalex-snapshot
Spinach leaf 70-kilodalton heat-shock cognate stabilizes bovine adrenal glucose-6-phosphate dehydrogenase in vitro without apparent stable binding
inferred← citeshttps://doi.org/10.1007/bf01923454openalex-snapshot
Hsp70 in mitochondrial biogenesis: From chaperoning nascent polypeptide chains to facilitation of protein degradation
inferred← citeshttps://doi.org/10.1007/bf02703141openalex-snapshot
Regulation of HSP70 in excitatory neurons: Possible implications for neuronal functioning
inferred← citeshttps://doi.org/10.1007/bf02785589openalex-snapshot
Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins fromE. coli
inferred← citeshttps://doi.org/10.1007/bf02935896openalex-snapshot
Isolation of proteins that speifically interact with the ATPase domain of mammalian ER chaperone, BiP
inferred← citeshttps://doi.org/10.1007/bfb0049777openalex-snapshot
Molecular chaperones and intracellular protein translocation
inferred← citeshttps://doi.org/10.1007/pl00012487openalex-snapshot
Protein folding and degradation in bacteria:¶To degrade or not to degrade? That is the question
inferred← citeshttps://doi.org/10.1007/pl00012493openalex-snapshot
A specialized mitochondrial molecular chaperone system:¶A role in formation of Fe/S centers
inferred← citeshttps://doi.org/10.1007/s00018-004-4464-6openalex-snapshot
Hsp70 chaperones: Cellular functions and molecular mechanism
inferred← citeshttps://doi.org/10.1007/s00018-009-8745-yopenalex-snapshot
Functions and pathologies of BiP and its interaction partners
inferred← citeshttps://doi.org/10.1007/s00018-015-1985-0openalex-snapshot
Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes
inferred← citeshttps://doi.org/10.1007/s00203-004-0727-8openalex-snapshot
Complementation studies of the DnaK–DnaJ–GrpE chaperone machineries from Vibrio harveyi and Escherichia coli, both in vivo and in vitro
inferred← citeshttps://doi.org/10.1007/s00203-006-0164-yopenalex-snapshot
Distinct mechanisms regulate expression of the two major groEL homologues in Rhizobium leguminosarum
inferred← citeshttps://doi.org/10.1007/s00425-019-03239-7openalex-snapshot
AtJ3, a specific HSP40 protein, mediates protein farnesylation-dependent response to heat stress in Arabidopsis
inferred← citeshttps://doi.org/10.1007/s00705-003-0196-4openalex-snapshot
Mitochondrial HSP70, HSP40, and HSP60 bind to the 3′ untranslated region of the Murine hepatitis virus genome
inferred← citeshttps://doi.org/10.1007/s007050050452openalex-snapshot
Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo
inferred← citeshttps://doi.org/10.1007/s00709-004-0050-xopenalex-snapshot
Regulation of nucleocytoplasmic localization of the atDjC6 chaperone protein
inferred← citeshttps://doi.org/10.1007/s00709-023-01862-6openalex-snapshot
HSF and Hsp Gene Families in sunflower: a comprehensive genome-wide determination survey and expression patterns under abiotic stress conditions
inferred← citeshttps://doi.org/10.1007/s10126-011-9417-0openalex-snapshot
Heat Shock Protein Gene Family of the Porphyra seriata and Enhancement of Heat Stress Tolerance by PsHSP70 in Chlamydomonas
inferred← citeshttps://doi.org/10.1007/s10254-003-0021-1openalex-snapshot
Hsp70 and Hsp90—a relay team for protein folding
inferred← citeshttps://doi.org/10.1007/s10254-004-0025-5openalex-snapshot
Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies
inferred← citeshttps://doi.org/10.1007/s10265-005-0197-3openalex-snapshot
Interaction between proliferating cell nuclear antigen (PCNA) and a DnaJ induced by DNA damage
inferred← citeshttps://doi.org/10.1007/s10646-020-02185-5openalex-snapshot
Heat-stress induced expression of stress-inducible nucleotide exchange factor Fes1 in seagrass Zostera japonica
inferred← citeshttps://doi.org/10.1007/s10930-010-9261-5openalex-snapshot
Site-Saturation Mutagenesis of Leucine 134 of Bacillus licheniformis Nucleotide Exchange Factor GrpE Reveals the Importance of this Residue to the Co-chaperone Activity
inferred← citeshttps://doi.org/10.1007/s11033-014-3689-1openalex-snapshot
Purification and biochemical characterization of DnaK and its transcriptional activator RpoH from Neisseria gonorrhoeae
inferred← citeshttps://doi.org/10.1007/s11120-004-2216-yopenalex-snapshot
The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast
inferred← citeshttps://doi.org/10.1007/s11295-018-1306-5openalex-snapshot
Genome-wide identification and expression analysis of the molecular chaperone binding protein BiP genes in Citrus
inferred← citeshttps://doi.org/10.1007/s11427-009-0084-6openalex-snapshot
Posttranslational modulation on the biological activities of molecular chaperones
inferred← citeshttps://doi.org/10.1007/s11693-006-9004-2openalex-snapshot
The Hsp70 chaperone system maintains high concentrations of active proteins and suppresses ATP consumption during heat shock
inferred← citeshttps://doi.org/10.1007/s12013-021-00970-5openalex-snapshot
A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins
inferred← citeshttps://doi.org/10.1007/s12088-009-0029-6openalex-snapshot
A 70-kDa molecular chaperone, DnaK, from the industrial bacterium Bacillus licheniformis: gene cloning, purification and molecular characterization of the recombinant protein
inferred← citeshttps://doi.org/10.1007/s12192-010-0173-2openalex-snapshot
The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro
inferred← citeshttps://doi.org/10.1007/s12192-011-0299-xopenalex-snapshot
Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
inferred← citeshttps://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)
inferred← citeshttps://doi.org/10.1007/s12192-012-0395-6openalex-snapshot
Functional analysis of Hsp70 superfamily proteins of rice (Oryza sativa)
inferred← citeshttps://doi.org/10.1007/s12192-016-0697-1openalex-snapshot
J domain independent functions of J proteins
inferred← citeshttps://doi.org/10.1007/s12192-016-0752-yopenalex-snapshot
A disulfide-bonded DnaK dimer is maintained in an ATP-bound state
inferred← citeshttps://doi.org/10.1007/s12192-018-0948-4openalex-snapshot
Function, evolution, and structure of J-domain proteins
inferred← citeshttps://doi.org/10.1007/s12551-019-00563-wopenalex-snapshot
Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins
inferred← citeshttps://doi.org/10.1007/s42485-026-00209-yopenalex-snapshot
Nutrient-driven regulation of the heat shock response: implications for proteostasis and cellular homeostasis
inferred← citeshttps://doi.org/10.1016/0014-5793(93)81446-7openalex-snapshot
Occurrence and sequence of a DnaJ protein in plant (Allium porrum) epidermal cells
inferred← citeshttps://doi.org/10.1016/0014-5793(93)81585-nopenalex-snapshot
Autostimulation of the DnaK (HSP 70) ATPase of Escherichia coli
inferred← citeshttps://doi.org/10.1016/0014-5793(93)81624-9openalex-snapshot
DnaK ATPase activity revisited
inferred← citeshttps://doi.org/10.1016/0014-5793(94)80428-1openalex-snapshot
YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions
inferred← citeshttps://doi.org/10.1016/0014-5793(96)01100-3openalex-snapshot
Isolation and characterisation of a cDNA encoding rat mitochondrial GrpE, a stress‐inducible nucleotide‐exchange factor of ubiquitous appearance in mammalian organs
inferred← citeshttps://doi.org/10.1016/0092-8674(92)90294-mopenalex-snapshot
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor σ32
inferred← citeshttps://doi.org/10.1016/0092-8674(94)90317-4openalex-snapshot
Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
inferred← citeshttps://doi.org/10.1016/0092-8674(95)90099-3openalex-snapshot
Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle
inferred← citeshttps://doi.org/10.1016/0168-6445(95)00077-1openalex-snapshot
Replication of coliphage lambda DNA
inferred← citeshttps://doi.org/10.1016/0378-1097(93)90186-6openalex-snapshot
Nucleotide sequence analysis and heterologous expression of the Erysipelothrix rhusiopathiae dnaJ gene
inferred← citeshttps://doi.org/10.1016/0378-1119(93)90358-aopenalex-snapshot
Cloning and sequencing of the dnaK region of Streptomyces coelicolor A3(2)
inferred← citeshttps://doi.org/10.1016/0378-1119(94)00741-aopenalex-snapshot
Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins
inferred← citeshttps://doi.org/10.1016/0378-1119(94)90333-6openalex-snapshot
XDJ1, a gene encoding a novel non-essential DnaJ homologue from Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/0378-1119(94)90334-4openalex-snapshot
Isolation and characterization of CAJ1, a novel yeast homolog of dnaJ
inferred← citeshttps://doi.org/10.1016/0955-0674(91)90030-3openalex-snapshot
Molecular chaperones: individualists or groupies?
inferred← citeshttps://doi.org/10.1016/0955-0674(92)90130-5openalex-snapshot
Chaperones and protein folding
inferred← citeshttps://doi.org/10.1016/0959-440x(92)90172-4openalex-snapshot
Role of accessory proteins in protein folding
inferred← citeshttps://doi.org/10.1016/0959-440x(95)80014-ropenalex-snapshot
Molecular chaperones in cellular protein folding
inferred← citeshttps://doi.org/10.1016/0960-9822(92)90209-sopenalex-snapshot
Role of accessory proteins in protein folding
inferred← citeshttps://doi.org/10.1016/0960-9822(92)90240-bopenalex-snapshot
Won't you change partners and dance?
inferred← citeshttps://doi.org/10.1016/b978-0-12-168562-1.50169-5openalex-snapshot
FUNCTION AND REGULATION OF THE UNIVERSALLY CONSERVED HEAT-SHOCK RESPONSE
inferred← citeshttps://doi.org/10.1016/b978-0-12-370873-1.00027-7openalex-snapshot
Chaperones and Proteases
inferred← citeshttps://doi.org/10.1016/b978-0-12-381047-2.00002-5openalex-snapshot
New Insights into the Roles of Molecular Chaperones in Chlamydomonas and Volvox
inferred← citeshttps://doi.org/10.1016/b978-0-12-381339-8.00015-9openalex-snapshot
Farnesyl Transferase Inhibitors
inferred← citeshttps://doi.org/10.1016/b978-0-12-385114-7.00014-3openalex-snapshot
The Endoplasmic Reticulum-Associated Degradation and Disulfide Reductase ERdj5
inferred← citeshttps://doi.org/10.1016/b978-0-12-821430-5.00023-7openalex-snapshot
Molecular chaperones, proteases, and unfolded protein responses
inferred← citeshttps://doi.org/10.1016/b978-0-444-82235-2.50023-0openalex-snapshot
The motor of mitochondrial protein import: A mitochondrial analog of the Sec63p-Kar2p system
inferred← citeshttps://doi.org/10.1016/b978-012237455-5/50005-1openalex-snapshot
Chaperonin-Mediated Folding and Assembly of Proteins in Mitochondria
inferred← citeshttps://doi.org/10.1016/b978-012237455-5/50009-9openalex-snapshot
Role of Prokaryotic Chaperonins in Protein Folding
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2025.11.006openalex-snapshot
Molecular chaperone and chaperone-based therapeutic approaches for Alzheimer’s disease
inferred← citeshttps://doi.org/10.1016/bs.enz.2023.07.008openalex-snapshot
The Hsp70 and JDP proteins: Structure-function perspective on molecular chaperone activity
inferred← citeshttps://doi.org/10.1016/j.abb.2006.05.006openalex-snapshot
Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein
inferred← citeshttps://doi.org/10.1016/j.abb.2008.07.023openalex-snapshot
Prion-impairing mutations in Hsp70 chaperone Ssa1: Effects on ATPase and chaperone activities
inferred← citeshttps://doi.org/10.1016/j.arr.2016.09.004openalex-snapshot
Targeting chaperones, heat shock factor-1, and unfolded protein response: Promising therapeutic approaches for neurodegenerative disorders
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.01.002openalex-snapshot
ATP-dependent molecular chaperones in plastids — More complex than expected
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2013.02.010openalex-snapshot
Regulation of molecular chaperones through post-translational modifications: Decrypting the chaperone code
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.11.007openalex-snapshot
Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane
inferred← citeshttps://doi.org/10.1016/j.bbcan.2017.12.004openalex-snapshot
Chaperoning the guardian of the genome. The two-faced role of molecular chaperones in p53 tumor suppressor action
inferred← citeshttps://doi.org/10.1016/j.bbrc.2016.10.061openalex-snapshot
Chromosome mapping, molecular cloning and expression analysis of a novel gene response for leaf width in rice
inferred← citeshttps://doi.org/10.1016/j.biocel.2004.06.009openalex-snapshot
Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium tumefaciens identifies amino acid residues critical to its in vivo function
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1016/j.biocel.2007.02.011openalex-snapshot
The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: Regulating chaperone power in the parasite and the host
inferred← citeshttps://doi.org/10.1016/j.biocel.2007.10.017openalex-snapshot
The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state and chaperone properties
inferred← citeshttps://doi.org/10.1016/j.bpc.2010.04.001openalex-snapshot
Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP
inferred← citeshttps://doi.org/10.1016/j.bpj.2026.06.003openalex-snapshot
ATP-driven membrane binding and polymerization of bacterial actin MreB promotes local membrane fluidization
inferred← citeshttps://doi.org/10.1016/j.cbd.2025.101661openalex-snapshot
Genome-wide characterization of the Hsp40 gene family in Clarias fuscus reveals their roles in thermal stress adaptation and immune modulation
inferred← citeshttps://doi.org/10.1016/j.cbpa.2011.10.019openalex-snapshot
Effect of culture density and antioxidants on naupliar production and gene expression of the cyclopoid copepod, Paracyclopina nana
inferred← citeshttps://doi.org/10.1016/j.cell.2008.05.022openalex-snapshot
Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding
inferred← citeshttps://doi.org/10.1016/j.cell.2009.03.043openalex-snapshot
RhoBTB3: A Rho GTPase-Family ATPase Required for Endosome to Golgi Transport
inferred← citeshttps://doi.org/10.1016/j.cellsig.2020.109880openalex-snapshot
Review: ER stress-induced cell death in osteoarthritic cartilage
inferred← citeshttps://doi.org/10.1016/j.celrep.2020.108161openalex-snapshot
The YdiU Domain Modulates Bacterial Stress Signaling through Mn2+-Dependent UMPylation
inferred← citeshttps://doi.org/10.1016/j.chembiol.2006.07.011openalex-snapshot
Quinocarmycin Analog DX-52-1 Inhibits Cell Migration and Targets Radixin, Disrupting Interactions of Radixin with Actin and CD44
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