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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

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1 of the 67 references listed on this page is in the Retraction Watch database as retracted (export 2026-10-21): 10.1016/0092-8674(90)90066-n (notice 1992-09-04).

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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.1460-2075.1988.tb03144.xopenalex-snapshot

Seventy‐kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes.

inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07403.xopenalex-snapshot

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta‐lactamase precursor.

inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07624.xopenalex-snapshot

Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.

inferredcites →https://doi.org/10.1002/j.1460-2075.1990.tb07880.xopenalex-snapshot

A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb04891.xopenalex-snapshot

Sequential action of mitochondrial chaperones in protein import into the matrix.

inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot

A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding

inferredcites →https://doi.org/10.1007/bf00183530openalex-snapshot

Molten globule intermediates and protein folding

inferredcites →https://doi.org/10.1016/0005-2787(80)90129-xopenalex-snapshot

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

inferredcites →https://doi.org/10.1016/0014-5793(90)80143-7openalex-snapshot

Evidence for a molten globule state as a general intermediate in protein folding

inferredcites →https://doi.org/10.1016/0014-5793(90)81469-5openalex-snapshot

Polypeptides traverse the mitochondrial envelope in an extended state

inferredcites →https://doi.org/10.1016/0092-8674(89)90005-6openalex-snapshot

Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells

inferredcites →https://doi.org/10.1016/0092-8674(90)90066-nopenalex-snapshot

Renaturation of denatured λ repressor requires heat shock proteins

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/10.1016/0092-8674(90)90488-zopenalex-snapshot

Stress proteins in biology and medicine

inferredcites →https://doi.org/10.1016/0968-0004(90)90136-yopenalex-snapshot

Protein structure: A practical approach

inferredcites →https://doi.org/10.1016/0968-0004(91)90055-zopenalex-snapshot

Is hsp70 the cellular thermometer?

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(18)66759-6openalex-snapshot

Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.

inferredcites →https://doi.org/10.1016/s0021-9258(18)77163-9openalex-snapshot

Nucleoprotein structures initiating DNA replication, transcription, and site-specific recombination.

inferredcites →https://doi.org/10.1016/s0021-9258(18)81737-9openalex-snapshot

Reversible folding of rhodanese

inferredcites →https://doi.org/10.1016/s0021-9258(18)98800-9openalex-snapshot

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

inferredcites →https://doi.org/10.1016/s0021-9258(19)38558-8openalex-snapshot

Mitochondrial precursor protein. Effects of 70-kilodalton heat shock protein on polypeptide folding, aggregation, and import competence.

inferredcites →https://doi.org/10.1016/s0021-9258(19)39277-4openalex-snapshot

The detection of kinetic intermediate(s) during refolding of rhodanese.

inferredcites →https://doi.org/10.1021/bi00102a010openalex-snapshot

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

inferredcites →https://doi.org/10.1021/bi00220a020openalex-snapshot

GroE facilitates refolding of citrate synthase by suppressing aggregation

inferredcites →https://doi.org/10.1021/bi00227a001openalex-snapshot

Protein folding: local structures, domains, subunits, and assemblies

inferredcites →https://doi.org/10.1021/bi00244a001openalex-snapshot

The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

inferredcites →https://doi.org/10.1021/bi00461a001openalex-snapshot

The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell

inferredcites →https://doi.org/10.1038/273124a0openalex-snapshot

The covalent and tertiary structure of bovine liver rhodanese

inferredcites →https://doi.org/10.1038/328378a0openalex-snapshot

Proteins as molecular chaperones

inferredcites →https://doi.org/10.1038/332776a0openalex-snapshot

Coming in from the cold

inferredcites →https://doi.org/10.1038/332800a0openalex-snapshot

A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

inferredcites →https://doi.org/10.1038/332805a0openalex-snapshot

70K heat shock related proteins stimulate protein translocation into microsomes

inferredcites →https://doi.org/10.1038/333330a0openalex-snapshot

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

inferredcites →https://doi.org/10.1038/336254a0openalex-snapshot

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein

inferredcites →https://doi.org/10.1038/337044a0openalex-snapshot

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

inferredcites →https://doi.org/10.1038/337620a0openalex-snapshot

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

inferredcites →https://doi.org/10.1038/337655a0openalex-snapshot

Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

inferredcites →https://doi.org/10.1038/341125a0openalex-snapshot

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

inferredcites →https://doi.org/10.1038/342884a0openalex-snapshot

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

inferredcites →https://doi.org/10.1038/344882a0openalex-snapshot

Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli

inferredcites →https://doi.org/10.1038/348137a0openalex-snapshot

Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

inferredcites →https://doi.org/10.1038/349627a0openalex-snapshot

A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast

inferredcites →https://doi.org/10.1038/350165a0openalex-snapshot

Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

inferredcites →https://doi.org/10.1038/350518a0openalex-snapshot

The molten globule protein conformation probed by disulphide bonds

inferredcites →https://doi.org/10.1038/352017a0openalex-snapshot

Unfolding protein folding

inferredcites →https://doi.org/10.1038/352036a0openalex-snapshot

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

inferredcites →https://doi.org/10.1038/353726a0openalex-snapshot

Peptide-binding specificity of the molecular chaperone BiP

inferredcites →https://doi.org/10.1038/354434a0openalex-snapshot

A cytoplasmic chaperonin?

inferredcites →https://doi.org/10.1038/354490a0openalex-snapshot

A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1

inferredcites →https://doi.org/10.1038/355033a0openalex-snapshot

Protein folding in the cell

inferredcites →https://doi.org/10.1073/pnas.84.12.4156openalex-snapshot

SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth.

inferredcites →https://doi.org/10.1073/pnas.88.13.5719openalex-snapshot

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.

inferredcites →https://doi.org/10.1073/pnas.88.18.7903openalex-snapshot

Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin.

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/10.1083/jcb.109.6.2665openalex-snapshot

A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.

inferredcites →https://doi.org/10.1083/jcb.114.4.609openalex-snapshot

Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein.

inferredcites →https://doi.org/10.1083/jcb.114.4.623openalex-snapshot

Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins.

inferredcites →https://doi.org/10.1111/j.1432-1033.1987.tb10900.xopenalex-snapshot

Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits

inferredcites →https://doi.org/10.1126/science.181.4096.223openalex-snapshot

Principles that Govern the Folding of Protein Chains

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.250.4983.954openalex-snapshot

Molecular Chaperones: The Plant Connection

inferredcites →https://doi.org/10.1126/science.2938257openalex-snapshot

Selectivity of Intracellular Proteolysis: Protein Substrates Activate the ATP-Dependent Protease (La)

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/jb.172.9.4827-4835.1990openalex-snapshot

Isolation and characterization of dnaJ null mutants of Escherichia coli

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/10.1146/annurev.cb.05.110189.001425openalex-snapshot

Protein Oligomerization in the Endoplasmic Reticulum

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/10.1002/(sici)1097-4652(199702)170:2<115::aid-jcp3>3.0.co;2-ropenalex-snapshot

Endoplasmic reticulum stress-inducible protein GRP94 is associated with an Mg2+-dependent serine kinase activity modulated by Ca2+ and GRP78/BiP

inferred← citeshttps://doi.org/10.1002/(sici)1098-2787(1997)16:4<165::aid-mas1>3.0.co;2-fopenalex-snapshot

Mass spectrometry as a readout of protein structure and function

inferred← citeshttps://doi.org/10.1002/(sici)1098-2795(199907)53:3<336::aid-mrd9>3.0.co;2-mopenalex-snapshot

Thermotolerance of IVM-derived bovine oocytes and embryos after short-term heat shock

inferred← citeshttps://doi.org/10.1002/047120918x.emb1228openalex-snapshot

Protein FoldingIn Vivo

inferred← citeshttps://doi.org/10.1002/1097-0290(20010205)72:3<255::aid-bit1>3.0.co;2-#openalex-snapshot

Variable specific activity of Escherichia coli β‐galactosidase in bacterial cells

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/10.1002/1873-3468.13844openalex-snapshot

Recent advances in understanding catalysis of protein folding by molecular chaperones

inferred← citeshttps://doi.org/10.1002/2211-5463.13550openalex-snapshot

A curcumin analogue GO‐Y030 depletes cancer stem cells by inhibiting the interaction between the HSP70 / HSP40 complex and its substrates

inferred← citeshttps://doi.org/10.1002/3527600906.mcb.200300085openalex-snapshot

Aggregation, Protein

inferred← citeshttps://doi.org/10.1002/3527600906.mcb.200300182openalex-snapshot

Chaperones, Molecular

inferred← citeshttps://doi.org/10.1002/9780470015902.a0000552.pub3openalex-snapshot

Protein Folding in Vivo

inferred← citeshttps://doi.org/10.1002/9780470514771.ch10openalex-snapshot

The 67 kDa Spliced Variant of β‐Galactosidase Serves as a Reusable Protective Chaperone for Tropoelastin

inferred← citeshttps://doi.org/10.1002/9780470572702openalex-snapshot

Protein Misfolding Diseases

inferred← citeshttps://doi.org/10.1002/9780470572702.ch3openalex-snapshot

Role of Molecular Chaperones in Protein Folding

inferred← citeshttps://doi.org/10.1002/9780470769829.ch1openalex-snapshot

Fundamental Structures and Behaviors of Proteins

inferred← citeshttps://doi.org/10.1002/9781118063903.ch8openalex-snapshot

Chaperone‐Dependent Amyloid Assembly and Prion Toxicity

inferred← citeshttps://doi.org/10.1002/9781118845363.ch2openalex-snapshot

Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins

inferred← citeshttps://doi.org/10.1002/9781119075691.ch60openalex-snapshot

Biophysical Studies of a Micellar Protein α‐Crystallin by Fluorescence METHODS

inferred← citeshttps://doi.org/10.1002/9783527610754.sf18openalex-snapshot

Hsp 70 Chaperones

inferred← citeshttps://doi.org/10.1002/9783527619498.ch47openalex-snapshot

Cellular Functions of Hsp70 Chaperones

inferred← citeshttps://doi.org/10.1002/9783527619498.ch64openalex-snapshot

The Chaperone System of Mitochondria

inferred← citeshttps://doi.org/10.1002/bies.950160916openalex-snapshot

Molecular chaperones in cellular protein folding

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/bit.21797openalex-snapshot

In situ protein folding and activation in bacterial inclusion bodies

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/ijch.201000015openalex-snapshot

Early Nascent Chain Folding Events on the Ribosome

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05581.xopenalex-snapshot

Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05582.xopenalex-snapshot

Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1993.tb05855.xopenalex-snapshot

Stepwise assembly of hyperaggregated forms of Drosophila zeste mutant protein suppresses white gene expression in vivo.

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.tb06054.xopenalex-snapshot

The heat shock cognate protein from Dictyostelium affects actin polymerization through interaction with the actin‐binding protein cap32/34.

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.tb06306.xopenalex-snapshot

A role for calnexin (IP90) in the assembly of class II MHC molecules.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06618.xopenalex-snapshot

Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06843.xopenalex-snapshot

Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1994.tb06844.xopenalex-snapshot

MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria.

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.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.tb00409.xopenalex-snapshot

The delta psi‐ and Hsp70/MIM44‐dependent reaction cycle driving early steps of protein import into 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.

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Association of Hsp47, Grp78, and Grp94 with procollagen supports the successive or coupled action of molecular chaperones

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Members of the 70 kDa heat shock protein family specifically recognize sulfoglycolipids: Role in gamete recognition and mycoplasma‐related infertility

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Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

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Activation and expression of proteins during synchronous germination of aerial spores of Streptomyces granaticolor

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Significant hydrogen exchange protection in GroEL‐bound DHFR is maintained during iterative rounds of substrate cycling

inferred← citeshttps://doi.org/10.1002/pro.5560070510openalex-snapshot

Reactivation of thermally inactivated pre‐β‐lactamase by DnaK, DnaJ, and GrpE

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.745openalex-snapshot

Cloning and characterization of a LON gene homologue from the human pathogen Paracoccidioides brasiliensis

inferred← citeshttps://doi.org/10.1006/abbi.1999.1354openalex-snapshot

N-Ethylmaleimide-Modified Hsp70 Inhibits Protein Folding

inferred← citeshttps://doi.org/10.1006/abbi.2000.2166openalex-snapshot

An Additional Serine Residue at the C Terminus of Rhodanese Destabilizes the Enzyme

inferred← citeshttps://doi.org/10.1006/abbi.2001.2472openalex-snapshot

Complex Effects of Molecular Chaperones on the Aggregation and Refolding of Fibroblast Growth Factor-1

inferred← citeshttps://doi.org/10.1006/bbrc.1997.6454openalex-snapshot

DnaJ Potentiates the Interaction between DnaK and α-Helical Peptides

inferred← citeshttps://doi.org/10.1006/bbrc.1997.6992openalex-snapshot

Sequence and Analysis of adnaJHomologue Gene in CyanobacteriumSynechococcussp. PCC7942

inferred← citeshttps://doi.org/10.1006/bbrc.1999.0931openalex-snapshot

Association of Prokaryotic and Eukaryotic Chaperone Proteins with the Human 1α,25-Dihydroxyvitamin D3 Receptor

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Transcription of the ibpB Heat-Shock Gene Is under Control of ς32- and ς54-Promoters, a Third Regulon of Heat-Shock Response

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JDD1, a Novel Member of the DnaJ Family, Is Expressed in the Germinal Zone of the Rat Brain

inferred← citeshttps://doi.org/10.1006/cbir.1999.0344openalex-snapshot

In situ localization of heat‐shock and histone proteins in honey‐bee (apis mellifera l.) larvae infected with paenibacillus larvae

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Stage-Specific Expression of Heat Shock Protein 90 in Murine Malaria Parasite Plasmodium yoelii

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

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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.1999.3320openalex-snapshot

Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli

inferred← citeshttps://doi.org/10.1006/jsbi.2001.4352openalex-snapshot

Review: Mechanisms of Disaggregation and Refolding of Stable Protein Aggregates by Molecular Chaperones

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Review: Nucleotide Binding to the Thermoplasma Thermosome: Implications for the Functional Cycle of Group II Chaperonins

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/prep.2000.1359openalex-snapshot

Expression of Recombinant ζ-Crystallin in Escherichia coli with the Help of GroEL/ES and Its Purification

inferred← citeshttps://doi.org/10.1006/prep.2001.1424openalex-snapshot

Isolation, Expression, and Characterization of Fully Functional Nontoxic BiP/GRP78 Mutants

inferred← citeshttps://doi.org/10.1006/prep.2001.1520openalex-snapshot

Production of Correctly Folded Fab Antibody Fragment in the Cytoplasm of Escherichia coli trxB gor Mutants via the Coexpression of Molecular Chaperones

inferred← citeshttps://doi.org/10.1006/scdb.1999.0347openalex-snapshot

Roles of molecular chaperones in cytoplasmic protein folding

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Cotranslational Folding and Transmembrane Transport of Proteins

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Rubisco: Assembly and Mechanism

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The Cyanobacterial Heat-Shock Response and the Molecular Chaperones

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Molecular Roles of Chaperones in Assisted Folding and Assembly of Proteins

inferred← citeshttps://doi.org/10.1007/3-540-29717-0_5openalex-snapshot

Chaperoning of Glucocorticoid Receptors

inferred← citeshttps://doi.org/10.1007/7355_2015_92openalex-snapshot

Hsp40 Co-chaperones as Drug Targets: Towards the Development of Specific Inhibitors

inferred← citeshttps://doi.org/10.1007/978-0-387-49310-7_4openalex-snapshot

Do Hsp40s Act as Chaperones or Co-Chaperones?

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/10.1007/978-1-4615-2407-6_17openalex-snapshot

Extrinsic Factors in Ribosome Assembly

inferred← citeshttps://doi.org/10.1007/978-1-4615-6177-4_1openalex-snapshot

An Overview of the Heat Shock Proteins, Their Regulation, and Function

inferred← citeshttps://doi.org/10.1007/978-1-4615-7817-8_18openalex-snapshot

Cotranslational Folding and Transmembrane Transport of Proteins

inferred← citeshttps://doi.org/10.1007/978-1-4684-8601-8_23openalex-snapshot

Heat Shock Regulation

inferred← citeshttps://doi.org/10.1007/978-1-4899-1349-4_12openalex-snapshot

Theoretical Perspectives on In Vitro and In Vivo Protein Folding

inferred← citeshttps://doi.org/10.1007/978-1-4899-1727-0_2openalex-snapshot

Compact Intermediates States in Protein Folding

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/10.1007/978-1-4939-1130-1_15openalex-snapshot

The Interaction Networks of E. coli Chaperones

inferred← citeshttps://doi.org/10.1007/978-1-4939-1136-3_13openalex-snapshot

Molecular Chaperone Functions in Plastids

inferred← citeshttps://doi.org/10.1007/978-1-60327-412-8_3openalex-snapshot

Membrane Insertion of Small Proteins

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_4openalex-snapshot

Specification of Hsp70 Function by Hsp40 Co-chaperones

inferred← citeshttps://doi.org/10.1007/978-3-0348-5703-1_5openalex-snapshot

Vom Gen zum Protein

inferred← citeshttps://doi.org/10.1007/978-3-0348-9088-5_2openalex-snapshot

Normal protein folding machinery

inferred← citeshttps://doi.org/10.1007/978-3-319-11731-7_4openalex-snapshot

Specification of Hsp70 Function by Type I and Type II Hsp40

inferred← citeshttps://doi.org/10.1007/978-3-319-74715-6_8openalex-snapshot

Molecular Chaperones: Structure-Function Relationship and their Role in Protein Folding

inferred← citeshttps://doi.org/10.1007/978-3-642-51463-0_4openalex-snapshot

Chaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes

inferred← citeshttps://doi.org/10.1007/978-3-642-60929-9_17openalex-snapshot

The Role of Molecular Chaperones Hsp70 And Hsp60 in Protein Folding

inferred← citeshttps://doi.org/10.1007/978-3-642-61126-1_12openalex-snapshot

Protein Import Across the Inner Mitochondrial Membrane

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/10.1007/978-3-642-78729-4_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/10.1007/978-3-642-79133-8_29openalex-snapshot

Caps, Cors, Dehydrins, and Molecular Chaperones: Their Relationship with Low Temperature Responses in Spinach

inferred← citeshttps://doi.org/10.1007/978-3-642-79502-2_2openalex-snapshot

Heat-shock proteins as molecular chaperones

inferred← citeshttps://doi.org/10.1007/978-3-662-02928-2_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/10.1007/978-94-007-7438-4_2openalex-snapshot

General Structural and Functional Features of Molecular Chaperones

inferred← citeshttps://doi.org/10.1007/978-94-011-0227-8_26openalex-snapshot

The Cyanobacterial Heat-Shock Response and the Molecular Chaperones

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_1openalex-snapshot

The general concept of molecular chaperones

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_12openalex-snapshot

Roles of molecular chaperones in protein targeting to mitochondria

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_3openalex-snapshot

The Escherichia coli chaperones involved in DNA replication

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_5openalex-snapshot

What does protein refolding in vitro tell us about protein folding in the cell?

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_6openalex-snapshot

Chaperonins and protein folding: unity and disunity of mechanisms

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_8openalex-snapshot

Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

inferred← citeshttps://doi.org/10.1007/978-94-011-2108-8_9openalex-snapshot

Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells

inferred← citeshttps://doi.org/10.1007/978-94-011-4802-3_8openalex-snapshot

Transgenic Cereals — Zea mays (maize)

inferred← citeshttps://doi.org/10.1007/978-94-017-2087-8_16openalex-snapshot

Multi-level Regulation of Purple Bacterial Light-harvesting Complexes

inferred← citeshttps://doi.org/10.1007/978-981-10-3707-8_3openalex-snapshot

Crosstalk Between Osmolytes and Cellular Chaperones: Examples in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1007/978-981-92-0056-6_2openalex-snapshot

Beginning of Silkworm Biotechnology

inferred← citeshttps://doi.org/10.1007/bf00017750openalex-snapshot

Import and assembly of the ? and ?-polypeptides of the light-harvesting complex I (B870) in the membrane system of Rhodobacter capsulatus investigated in an in vitro translation system

inferred← citeshttps://doi.org/10.1007/bf00042234openalex-snapshot

AtJ1, a mitochondrial homologue of theEscherichia coli DnaJ protein

inferred← citeshttps://doi.org/10.1007/bf00180036openalex-snapshot

Transport of proteins across mitochondrial membranes

inferred← citeshttps://doi.org/10.1007/bf00211091openalex-snapshot

Mitochondrial protein import: Specific recognition and membrane translocation of preproteins

inferred← citeshttps://doi.org/10.1007/bf00280382openalex-snapshot

MSl3, a multicopy suppressor of mutants hyperactivated in the RAS-CAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1007/bf00339139openalex-snapshot

Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms

inferred← citeshttps://doi.org/10.1007/bf00571378openalex-snapshot

Interspecific variation in thermal denaturation of proteins in the congeneric musselsMytilus trossulus andM. galloprovincialis: evidence from the heat-shock response and protein ubiquitination

inferred← citeshttps://doi.org/10.1007/bf00902735openalex-snapshot

Overproduction and purification of Lon protease fromEscherichia coli using a maltose-binding protein fusion system

inferred← citeshttps://doi.org/10.1007/bf00986963openalex-snapshot

Translational regulation of the heat shock response

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/bf01952100openalex-snapshot

Polypeptide translocation machinery of the yeast endoplasmic reticulum

inferred← citeshttps://doi.org/10.1007/bf02118307openalex-snapshot

Mammalian heat shock protein families. Expression and functions

inferred← citeshttps://doi.org/10.1007/bf02527705openalex-snapshot

Antisense oligonucleotide to the 70-kDa heat shock cognate protein inhibits synthesis of myelin basic protein

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/bf02843633openalex-snapshot

Heat-shock protein 70 expression in shrimpFenneropenaeus chinensis during thermal and immune-challenged stress

inferred← citeshttps://doi.org/10.1007/bf02936124openalex-snapshot

Heat stress response and heat stress transcription factors

inferred← citeshttps://doi.org/10.1007/bf03041347openalex-snapshot

Rheumatoid arthritis and enteric bacteria

inferred← citeshttps://doi.org/10.1007/bfb0049777openalex-snapshot

Molecular chaperones and intracellular protein translocation

inferred← citeshttps://doi.org/10.1007/pl00000583openalex-snapshot

Heat stress proteins and transcription factors

inferred← citeshttps://doi.org/10.1007/pl00006219openalex-snapshot

The sequences of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus- Thermus group and cyanobacteria

inferred← citeshttps://doi.org/10.1007/s00018-006-6192-6openalex-snapshot

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

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/s002030050370openalex-snapshot

Formation of the light-harvesting complex I (B870) of anoxygenic phototrophic purple bacteria

inferred← citeshttps://doi.org/10.1007/s00253-009-2305-0openalex-snapshot

DnaK/DnaJ-assisted recombinant protein production in Trichoplusia ni larvae

inferred← citeshttps://doi.org/10.1007/s00300-023-03213-wopenalex-snapshot

Cold adaptation and response genes of Antarctic Cryobacterium sp. SO2 from the Fildes Peninsula, King George Island

inferred← citeshttps://doi.org/10.1007/s00343-015-4321-5openalex-snapshot

Identification and characterization of a DnaJ gene from red alga Pyropia yezoensis (Bangiales, Rhodophyta)

inferred← citeshttps://doi.org/10.1007/s00406-024-01905-wopenalex-snapshot

DNAJC13 influences responses of the extended reward system to conditioned stimuli: a genome-wide association study

inferred← citeshttps://doi.org/10.1007/s004380051198openalex-snapshot

Functional specificity of the mitochondrial DnaJ protein, Mdj1p, in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1007/s004410050759openalex-snapshot

Differential distribution of the mitochondrial heat-shock protein 60 in rat gastrointestinal tract

inferred← citeshttps://doi.org/10.1007/s004410050839openalex-snapshot

Distribution of heat-shock protein 60 immunoreactivity in testes of infertile men

inferred← citeshttps://doi.org/10.1007/s10254-003-0011-3openalex-snapshot

Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes

inferred← citeshttps://doi.org/10.1007/s10254-005-0001-0openalex-snapshot

The diverse roles of J-proteins, the obligate Hsp70 co-chaperone

inferred← citeshttps://doi.org/10.1007/s10539-012-9332-4openalex-snapshot

Proteins, the chaperone function and heredity

inferred← citeshttps://doi.org/10.1007/s10555-005-6193-1openalex-snapshot

Prokaryotic expression of antibodies

inferred← citeshttps://doi.org/10.1007/s11229-004-4421-9openalex-snapshot

Emergence and Its Place in Nature: A Case Study of Biochemical Networks

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/s12035-023-03846-2openalex-snapshot

Molecular Chaperones as Therapeutic Target: Hallmark of Neurodegenerative Disorders

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/s12104-018-9823-6openalex-snapshot

1H, 15N and 13C resonance assignments of the J-domain of co-chaperone Sis1 from Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1007/s12275-022-2425-0openalex-snapshot

Cytoplasmic molecular chaperones in Pseudomonas species

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(92)80894-mopenalex-snapshot

Amino acid substitutions influencing intracellular protein folding pathways

inferred← citeshttps://doi.org/10.1016/0014-5793(93)80290-bopenalex-snapshot

ATP‐dependent protein refolding activity in reticulocyte lysate

inferred← citeshttps://doi.org/10.1016/0014-5793(93)80585-iopenalex-snapshot

Interaction of homologues of Hsp70 and Cpn60 with ferredoxin‐NADP+ reductase upon its import into chloroplasts

inferred← citeshttps://doi.org/10.1016/0014-5793(93)80615-2openalex-snapshot

Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase

inferred← citeshttps://doi.org/10.1016/0014-5793(93)80649-fopenalex-snapshot

A constitutive form of heat‐shock protein 70 is located in the outer membranes of mitochondria from rat liver

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(94)80381-1openalex-snapshot

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES

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(94)80567-9openalex-snapshot

Tumour necrosis factor is in equilibrium with a trimeric molten globule at low pH

inferred← citeshttps://doi.org/10.1016/0014-5793(94)80620-9openalex-snapshot

Protein uptake into E. coll during Bdellovibrio infection

inferred← citeshttps://doi.org/10.1016/0014-5793(95)00024-4openalex-snapshot

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation

inferred← citeshttps://doi.org/10.1016/0014-5793(95)00704-dopenalex-snapshot

Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators

inferred← citeshttps://doi.org/10.1016/0014-5793(96)00049-xopenalex-snapshot

Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat‐induced protein aggregation

inferred← citeshttps://doi.org/10.1016/0092-8674(93)90287-zopenalex-snapshot

Eukaryotic DnaJ homologs and the specificity of Hsp70 activity

inferred← citeshttps://doi.org/10.1016/0092-8674(93)90470-bopenalex-snapshot

Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL

inferred← citeshttps://doi.org/10.1016/0092-8674(93)90492-9openalex-snapshot

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP

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/10.1016/0141-0229(93)90002-jopenalex-snapshot

Stable expression plasmid for high-level production of GroE molecular chaperones in large-scale cultures

inferred← citeshttps://doi.org/10.1016/0166-6851(94)90036-1openalex-snapshot

The Plasmodium falciparum protein RESA interacts with the erythrocyte cytoskeleton and modifies erythrocyte thermal stability

inferred← citeshttps://doi.org/10.1016/0167-4781(93)90104-lopenalex-snapshot

Human cDNA encoding DnaJ protein homologue

inferred← citeshttps://doi.org/10.1016/0167-4781(94)00011-qopenalex-snapshot

Protein translocation in Escherichia coli

inferred← citeshttps://doi.org/10.1016/0167-4781(94)90025-6openalex-snapshot

The initiator protein DnaA: evolution, properties and function

inferred← citeshttps://doi.org/10.1016/0167-4781(95)00063-mopenalex-snapshot

A cDNA of Schizosaccharomyces pombe encoding a homologue of DnaJ-like protein

inferred← citeshttps://doi.org/10.1016/0167-4838(95)00007-hopenalex-snapshot

Affinity-purification and identification of GrpE homologues from mammalian mitochondria

inferred← citeshttps://doi.org/10.1016/0167-4838(95)00146-lopenalex-snapshot

On the interaction of α-crystallin with unfolded proteins

inferred← citeshttps://doi.org/10.1016/0169-4758(95)80032-8openalex-snapshot

Home improvements: Malaria and the red blood cell

inferred← citeshttps://doi.org/10.1016/0304-4157(94)90012-4openalex-snapshot

Protein translocation in Escherichia coli

inferred← citeshttps://doi.org/10.1016/0305-0491(93)90043-5openalex-snapshot

Heat-shock response in camel (Camelus dromedarius) blood cells and adaptation to hyperthermia

inferred← citeshttps://doi.org/10.1016/0378-1097(93)90105-bopenalex-snapshot

Impairment of nucleoid segregation and cell division at high osmolarity in a strain of Escherichia coli overproducing the chaperone DnaK

inferred← citeshttps://doi.org/10.1016/0378-1097(95)00235-wopenalex-snapshot

Expression of DnaK and GroEL homologs in Leuconostoc esenteroides in response to heat shock, cold shock or chemical stress

inferred← citeshttps://doi.org/10.1016/0378-1119(93)90593-ropenalex-snapshot

Overproduction of Anabaena 7120 ribulose-bisphosphate carboxylase/oxygenase in Escherichia coli

inferred← citeshttps://doi.org/10.1016/0378-1119(93)90626-eopenalex-snapshot

Cloning and sequencing of the Lactococcus lactis subsp. lactis groESL operon

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

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