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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
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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/prot.340060202openalex-snapshot
The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure
inferredcites →https://doi.org/10.1007/bf00248050openalex-snapshot
Protein folding: Hypotheses and experiments
inferredcites →https://doi.org/10.1007/bf00333274openalex-snapshot
Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes
inferredcites →https://doi.org/10.1007/bf00333275openalex-snapshot
A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene
inferredcites →https://doi.org/10.1016/0014-5793(81)80367-5openalex-snapshot
Protein folding: general physical model
inferredcites →https://doi.org/10.1016/0014-5793(88)80485-xopenalex-snapshot
The ‘molten globule’ state is involved in the translocation of proteins across membranes?
inferredcites →https://doi.org/10.1016/0022-2836(79)90501-1openalex-snapshot
Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly
inferredcites →https://doi.org/10.1016/0022-2836(79)90502-3openalex-snapshot
Purification and properties of groE, a host protein involved in bacteriophage assembly
inferredcites →https://doi.org/10.1016/0167-4838(85)90249-3openalex-snapshot
The assembly mechanism of the lactate dehydrogenase tetramer from Bacillus stearothermophilus; the equilibrium relationships between quaternary structure and the binding of fructose 1,6-biphosphate, NADH and oxamate
inferredcites →https://doi.org/10.1016/0167-4838(85)90319-xopenalex-snapshot
Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus
inferredcites →https://doi.org/10.1016/0378-1119(86)90165-4openalex-snapshot
Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilusl-lactate dehydrogenase gene
inferredcites →https://doi.org/10.1016/0968-0004(89)90064-9openalex-snapshot
Secretion and membrane assembly
inferredcites →https://doi.org/10.1016/0968-0004(89)90168-0openalex-snapshot
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures
inferredcites →https://doi.org/10.1016/s0021-9258(18)67256-4openalex-snapshot
Purification and properties of the groES morphogenetic protein of Escherichia coli.
inferredcites →https://doi.org/10.1021/bi00218a021openalex-snapshot
Detection and characterization of intermediates in the folding of large proteins by the use of genetically inserted tryptophan probes
inferredcites →https://doi.org/10.1021/bi00220a020openalex-snapshot
GroE facilitates refolding of citrate synthase by suppressing aggregation
inferredcites →https://doi.org/10.1021/bi00427a002openalex-snapshot
Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin
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/10.1038/342884a0openalex-snapshot
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
inferredcites →https://doi.org/10.1073/pnas.75.1.131openalex-snapshot
Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product).
inferredcites →https://doi.org/10.1073/pnas.78.3.1629openalex-snapshot
Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis.
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.4772706openalex-extracted
Unraveling the Existence of Different Oligomeric Forms of E. Coli Small Heat-Shock Protein Ibpb Under Heat Stress and the Most Functional Oligomers with Respect to Holding Chaperone Activity
inferred← citeshttps://doi.org/10.1002/1873-3468.15019openalex-snapshot
Two new oligomers of E. coli small heat‐shock protein IbpB identified under heat stress exhibit maximum holding chaperone activity
inferred← citeshttps://doi.org/10.1002/9783527610754.sf21openalex-snapshot
The E . coli Gro E Chaperone
inferred← citeshttps://doi.org/10.1002/9783527615971.ch3openalex-snapshot
Subunit Assembly of Oligomeric Enzymes
inferred← citeshttps://doi.org/10.1002/9783527619498.ch53openalex-snapshot
The E. coli GroE Chaperone
inferred← citeshttps://doi.org/10.1002/bies.950160404openalex-snapshot
The chaperonin cycle and protein folding
inferred← citeshttps://doi.org/10.1002/biot.200800098openalex-snapshot
Role of the ribosome in protein folding
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.1460-2075.1993.tb06098.xopenalex-snapshot
Refolding of barnase mutants and pro‐barnase in the presence and absence of GroEL.
inferred← citeshttps://doi.org/10.1002/jmr.654openalex-snapshot
The substrate recognition mechanisms in chaperonins
inferred← citeshttps://doi.org/10.1002/pro.5560030910openalex-snapshot
The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro
inferred← citeshttps://doi.org/10.1002/pro.5560050309openalex-snapshot
Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli β‐galactosidase
inferred← citeshttps://doi.org/10.1002/pro.5560060401openalex-snapshot
GroEL‐Mediated protein folding
inferred← citeshttps://doi.org/10.1006/abbi.1999.1223openalex-snapshot
GroEL-Assisted and -Unassisted Refolding of Mature and Precursor Adrenodoxin: The Role of the Precursor Sequence
inferred← citeshttps://doi.org/10.1006/bbrc.2001.4715openalex-snapshot
Binding of a Denatured Heme Protein and ATP to Erythroid Spectrin
inferred← citeshttps://doi.org/10.1006/jmbi.1995.0285openalex-snapshot
The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
inferred← citeshttps://doi.org/10.1006/jmbi.1996.0815openalex-snapshot
Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction
inferred← citeshttps://doi.org/10.1006/jmbi.1997.0969openalex-snapshot
GroEL-mediated folding of structurally homologous dihydrofolate reductases 1 1Edited by P. E. Wright
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1481openalex-snapshot
Two conformational states of β-lactamase bound to GroEL: a biophysical characterization 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1630openalex-snapshot
Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1704openalex-snapshot
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3138openalex-snapshot
A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.2000.3648openalex-snapshot
A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar11Edited by C. R. Matthews
inferred← citeshttps://doi.org/10.1006/jmbi.2000.4277openalex-snapshot
From Minichaperone to GroEL 2: Importance of Avidity of the Multisite Ring Structure
inferred← citeshttps://doi.org/10.1007/4735_116openalex-snapshot
The Hsp60 chaperonins from prokaryotes and eukaryotes
inferred← citeshttps://doi.org/10.1007/978-90-481-3034-4_13openalex-snapshot
Computational Modeling of Biological Systems: The LDH Story
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/bf00159520openalex-snapshot
Thermostabilization of enzymes by the chaperonin GroEL
inferred← citeshttps://doi.org/10.1007/bf00279532openalex-snapshot
GroE-mediated folding of bacterial luciferases in vivo
inferred← citeshttps://doi.org/10.1007/bf01024958openalex-snapshot
Sulfhydryl modification ofE. coli cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex
inferred← citeshttps://doi.org/10.1007/bf01891988openalex-snapshot
The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide
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/s00018-009-0164-6openalex-snapshot
Reconciling theories of chaperonin accelerated folding with experimental evidence
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/s10534-006-9078-zopenalex-snapshot
Effects of divalent cations on encapsulation and release in the GroEL-assisted folding
inferred← citeshttps://doi.org/10.1007/s10540-006-9024-xopenalex-snapshot
Spectrin Organization and Dynamics: New Insights
inferred← citeshttps://doi.org/10.1007/s12010-013-0422-9openalex-snapshot
Refolding of Laccase in Dilution Additive Mode with Copper-Based Ionic Liquid
inferred← citeshttps://doi.org/10.1007/s12154-013-0106-5openalex-snapshot
Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL
inferred← citeshttps://doi.org/10.1007/s12192-009-0104-2openalex-snapshot
Differential effects of co-chaperonin homologs on cpn60 oligomers
inferred← citeshttps://doi.org/10.1016/0014-5793(93)80083-7openalex-snapshot
Crystallization and preliminary X‐ray investigation of the Escherichia coli molecular chaperone cpn60 (GroEL)
inferred← citeshttps://doi.org/10.1016/0014-5793(94)00348-3openalex-snapshot
The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted folding
inferred← citeshttps://doi.org/10.1016/0014-5793(95)00768-5openalex-snapshot
The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES
inferred← citeshttps://doi.org/10.1016/0167-4838(94)00227-8openalex-snapshot
GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL
inferred← citeshttps://doi.org/10.1016/0167-4838(94)00231-5openalex-snapshot
Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent
inferred← citeshttps://doi.org/10.1016/0959-440x(92)90168-7openalex-snapshot
Folding and binding editorial overview
inferred← citeshttps://doi.org/10.1016/0959-440x(92)90172-4openalex-snapshot
Role of accessory proteins in protein folding
inferred← citeshttps://doi.org/10.1016/0960-9822(92)90209-sopenalex-snapshot
Role of accessory proteins in protein folding
inferred← citeshttps://doi.org/10.1016/b978-012237455-5/50004-xopenalex-snapshot
Chaperonins of Photosynthetic Organisms
inferred← citeshttps://doi.org/10.1016/b978-012237455-5/50008-7openalex-snapshot
Kinetic and Energetic Aspects of Chaperonin Function
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/j.bbapap.2006.02.002openalex-snapshot
Unfolded, oxidized, and thermoinactivated forms of glyceraldehyde-3-phosphate dehydrogenase interact with the chaperonin GroEL in different ways
inferred← citeshttps://doi.org/10.1016/j.bbrc.2004.09.140openalex-snapshot
Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties
inferred← citeshttps://doi.org/10.1016/j.biocel.2010.01.002openalex-snapshot
Reduced stability and enhanced surface hydrophobicity drive the binding of apo-aconitase with GroEL during chaperone assisted refolding
inferred← citeshttps://doi.org/10.1016/j.biochi.2026.05.011openalex-snapshot
Globular oligomers as the building block units of the filamentous structure of E. coli small heat shock protein IbpA and their holding chaperone activity
inferred← citeshttps://doi.org/10.1016/j.bpj.2014.11.002openalex-snapshot
Role of Denatured-State Properties in Chaperonin Action Probed by Single-Molecule Spectroscopy
inferred← citeshttps://doi.org/10.1016/j.cell.2013.04.052openalex-snapshot
Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein
inferred← citeshttps://doi.org/10.1016/j.pbiomolbio.2008.10.007openalex-snapshot
GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future
inferred← citeshttps://doi.org/10.1016/s0014-5793(97)00348-7openalex-snapshot
GroES binding regulates GroEL chaperonin activity under heat shock
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)34061-9openalex-snapshot
On the role of groES in the chaperonin-assisted folding reaction. Three case studies.
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)36828-xopenalex-snapshot
Chaperone-like activity of alpha-crystallin. The effect of NADPH on its interaction with zeta-crystallin.
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)36876-xopenalex-snapshot
The effect of groES on the groEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP.
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)37369-6openalex-snapshot
Fluorescence detection of conformational changes in GroEL induced by thermal switching and nucleotide binding.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)35813-7openalex-snapshot
Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)41858-3openalex-snapshot
Interaction of GroE with an all-beta-protein.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)43922-1openalex-snapshot
The rates of commitment to renaturation of rhodanese and glutamine synthetase in the presence of the groE chaperonins.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)46878-0openalex-snapshot
Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)46881-0openalex-snapshot
Correlation between the stability of the GroEL-protein ligand complex and the release mechanism.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)47143-8openalex-snapshot
Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)53201-4openalex-snapshot
GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)53331-7openalex-snapshot
Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)53522-5openalex-snapshot
Chaperonin-mediated reconstitution of the phytochrome photoreceptor.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)53561-4openalex-snapshot
Protein folding in a cell-free translation system. The fate of the precursor to mitochondrial aspartate aminotransferase.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)36520-2openalex-snapshot
Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)37111-xopenalex-snapshot
Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)49959-6openalex-snapshot
A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)74317-8openalex-snapshot
Structural features which control folding of homologous proteins in cell-free translation systems. The effect of a mitochondrial-targeting presequence on aspartate aminotransferase.
inferred← citeshttps://doi.org/10.1016/s0021-9258(20)80588-2openalex-snapshot
Thermal switching between enhanced and arrested reactivation of bacterial glucose-6-phosphate dehydrogenase assisted by GroEL in the absence of ATP.
inferred← citeshttps://doi.org/10.1016/s0022-2836(03)00830-1openalex-snapshot
Isolation and Characterisation of Mutants of GroEL that are Fully Functional as Single Rings
inferred← citeshttps://doi.org/10.1016/s0070-2137(96)80008-2openalex-snapshot
Protein folding and association: In vitro studies for self-organization and targeting in the cell
inferred← citeshttps://doi.org/10.1016/s0076-6879(06)08022-0openalex-snapshot
DNA Polymerases for Translesion DNA Synthesis: Enzyme Purification and Mouse Models for Studying Their Function
inferred← citeshttps://doi.org/10.1016/s0167-4838(96)00125-2openalex-snapshot
GroEL reversibly binds to, and causes rapid inactivation of, human carbonic anhydrase II at high temperatures
inferred← citeshttps://doi.org/10.1016/s0167-4838(99)00049-7openalex-snapshot
Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding
inferred← citeshttps://doi.org/10.1016/s0168-9525(96)90022-0openalex-snapshot
A method for the separation of GST fusion proteins from co-purifying GroEL
inferred← citeshttps://doi.org/10.1016/s0304-4165(98)00143-3openalex-snapshot
The production and characterisation of an immobilised chaperonin system
inferred← citeshttps://doi.org/10.1016/s0959-440x(96)80093-5openalex-snapshot
Molecular chaperones in protein folding and translocation
inferred← citeshttps://doi.org/10.1016/s0969-2126(96)00028-7openalex-snapshot
Chaperone-assisted protein expression
inferred← citeshttps://doi.org/10.1016/s1359-0278(97)00046-1openalex-snapshot
Structural and mechanistic consequences of polypeptide binding by GroEL
inferred← citeshttps://doi.org/10.1016/s1389-1723(02)80072-xopenalex-snapshot
Molecular Characterization and Regulatory Analysis of dnaK Operon of Halophilic Lactic Acid Bacterium Tetragenococcus halophila.
inferred← citeshttps://doi.org/10.1016/s1569-2558(08)60402-6openalex-snapshot
Identification, Cellular Localization, and Participation of Chaperonins in Protein Folding
inferred← citeshttps://doi.org/10.1016/s1874-6047(04)80010-6openalex-snapshot
The Role of ATP in directing chaperonin-mediated polypeptide folding
inferred← citeshttps://doi.org/10.1017/s0033583503003883openalex-snapshot
Chaperonin-mediated protein folding: fate of substrate polypeptide
inferred← citeshttps://doi.org/10.1017/s0033583519000143openalex-snapshot
Chaperonin-assisted protein folding: a chronologue
inferred← citeshttps://doi.org/10.1021/bi00061a013openalex-snapshot
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
inferred← citeshttps://doi.org/10.1021/bi00084a024openalex-snapshot
Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
inferred← citeshttps://doi.org/10.1021/bi00129a012openalex-snapshot
Conformational states of ribulose bisphosphate carboxylase and their interaction with chaperonin 60
inferred← citeshttps://doi.org/10.1021/bi00131a010openalex-snapshot
Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP
inferred← citeshttps://doi.org/10.1021/bi00254a004openalex-snapshot
Residue Lysine-34 in GroES Modulates Allosteric Transitions in GroEL
inferred← citeshttps://doi.org/10.1021/bi201237aopenalex-snapshot
Toward a Detailed Description of the Pathways of Allosteric Communication in the GroEL Chaperonin through Atomistic Simulation
inferred← citeshttps://doi.org/10.1021/bp960068bopenalex-snapshot
Molten Globule Intermediate of Recombinant Human Growth Hormone: Stabilization with Surfactants
inferred← citeshttps://doi.org/10.1021/bp970125gopenalex-snapshot
Recovery and Reuse of the Molecular Chaperone GroEL for in Vitro Protein Refolding
inferred← citeshttps://doi.org/10.1021/ja0653977openalex-snapshot
A Theoretical Analysis of Rate Constants and Kinetic Isotope Effects Corresponding to Different Reactant Valleys in Lactate Dehydrogenase
inferred← citeshttps://doi.org/10.1023/a:1006273124726openalex-snapshot
Molecular characterization of DnaK from the halotolerant cyanobacterium Aphanothece halophytica for ATPase, protein folding, and copper binding under various salinity conditions
inferred← citeshttps://doi.org/10.1023/a:1007102402925openalex-snapshot
Stability and Release Requirements of the Complexes of GroEL with Two Homologous Mammalian Aminotransferases
inferred← citeshttps://doi.org/10.1023/a:1007146217946openalex-snapshot
GroEL and Protein Disulfide Isomerase Each Binds with Folding Intermediates of D-Glyceraldehyde-3-Phosphate Dehydrogenase Released from Complexes Formed with the Other
inferred← citeshttps://doi.org/10.1023/a:1020603717781openalex-snapshot
Participation of Chaperonin GroEL in the Folding of D-Glyceraldehyde-3-Phosphate Dehydrogenase. An Approach Based on the Use of Different Oligomeric Forms of the Enzyme Immobilized on Sepharose
inferred← citeshttps://doi.org/10.1038/10735openalex-snapshot
GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.
inferred← citeshttps://doi.org/10.1038/356683a0openalex-snapshot
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
inferred← citeshttps://doi.org/10.1038/368261a0openalex-snapshot
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
inferred← citeshttps://doi.org/10.1038/371261a0openalex-snapshot
Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
inferred← citeshttps://doi.org/10.1038/nsb0794-439openalex-snapshot
The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
inferred← citeshttps://doi.org/10.1042/bj2910139openalex-snapshot
Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase
inferred← citeshttps://doi.org/10.1042/bj3000651openalex-snapshot
Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
inferred← citeshttps://doi.org/10.1042/bj3000717openalex-snapshot
Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes
inferred← citeshttps://doi.org/10.1042/bj3310505openalex-snapshot
Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03024.xopenalex-snapshot
Amyloid‐fibril formation
inferred← citeshttps://doi.org/10.1073/pnas.90.9.3978openalex-snapshot
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
inferred← citeshttps://doi.org/10.1073/pnas.92.18.8100openalex-snapshot
Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.
inferred← citeshttps://doi.org/10.1073/pnas.93.22.12189openalex-snapshot
beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.
inferred← citeshttps://doi.org/10.1073/pnas.94.11.5535openalex-snapshot
Protein folding: How the mechanism of GroEL action is defined by kinetics
inferred← citeshttps://doi.org/10.1073/pnas.95.26.15275openalex-snapshot
Minimal and optimal mechanisms for GroE-mediated protein folding
inferred← citeshttps://doi.org/10.1074/jbc.270.3.1138openalex-snapshot
Homologous Proteins with Different Affinities for groEL
inferred← citeshttps://doi.org/10.1074/jbc.270.48.28551openalex-snapshot
The Chaperonin GroEL Is Destabilized by Binding of ADP
inferred← citeshttps://doi.org/10.1074/jbc.272.13.8236openalex-snapshot
DNA Binding and Bending by the Human Papillomavirus Type 16 E2 Protein
inferred← citeshttps://doi.org/10.1074/jbc.272.8.5105openalex-snapshot
Model Peptide Studies Demonstrate That Amphipathic Secondary Structures Can Be Recognized by the Chaperonin GroEL (cpn60)
inferred← citeshttps://doi.org/10.1074/jbc.273.18.11032openalex-snapshot
The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network
inferred← citeshttps://doi.org/10.1074/jbc.273.39.25073openalex-snapshot
Changing the Nature of the Initial Chaperonin Capture Complex Influences the Substrate Folding Efficiency
inferred← citeshttps://doi.org/10.1074/jbc.273.44.28677openalex-snapshot
Partitioning of Rhodanese onto GroEL
inferred← citeshttps://doi.org/10.1074/jbc.273.7.3915openalex-snapshot
Insight into the Conformation of Protein Folding Intermediate(s) Trapped by GroEL
inferred← citeshttps://doi.org/10.1074/jbc.274.29.20351openalex-snapshot
Chaperone Activity of a Chimeric GroEL Protein That Can Exist in a Single or Double Ring Form
inferred← citeshttps://doi.org/10.1074/jbc.m000795200openalex-snapshot
Refolding of Target Proteins from a “Rigid” Mutant Chaperonin Demonstrates a Minimal Mechanism of Chaperonin Binding and Release
inferred← citeshttps://doi.org/10.1074/jbc.m102098200openalex-snapshot
Characterization of a Novel Complex from Halophilic Archaebacteria, Which Displays Chaperone-like Activities in Vitro
inferred← citeshttps://doi.org/10.1074/jbc.m113.480178openalex-snapshot
Repetitive Protein Unfolding by the trans Ring of the GroEL-GroES Chaperonin Complex Stimulates Folding
inferred← citeshttps://doi.org/10.1074/jbc.m601605200openalex-snapshot
Elucidation of Steps in the Capture of a Protein Substrate for Efficient Encapsulation by GroE
inferred← citeshttps://doi.org/10.1074/jbc.m606433200openalex-snapshot
Significance of the N-terminal Domain for the Function of Chloroplast cpn20 Chaperonin
inferred← citeshttps://doi.org/10.1074/jbc.m710057200openalex-snapshot
The Intermediate Domain Defines Broad Nucleotide Selectivity for Protein Folding in Chlamydophila GroEL1
inferred← citeshttps://doi.org/10.1074/jbc.m802898200openalex-snapshot
Triggering Protein Folding within the GroEL-GroES Complex
inferred← citeshttps://doi.org/10.1080/10409230600760382openalex-snapshot
GroEL-Mediated Protein Folding: Making the Impossible, Possible
inferred← citeshttps://doi.org/10.1083/jcb.125.5.989openalex-snapshot
A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin.
inferred← citeshttps://doi.org/10.1098/rstb.1993.0028openalex-snapshot
Chaperonins and protein folding: unity and disunity of mechanisms
inferred← citeshttps://doi.org/10.1098/rstb.1993.0030openalex-snapshot
Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
inferred← citeshttps://doi.org/10.1110/ps.0213802openalex-snapshot
α‐Crystallin and ATP facilitate the in vitro renaturation of xylanase: enhancement of refolding by metal ions
inferred← citeshttps://doi.org/10.1110/ps.041211205openalex-snapshot
Misfolded forms of glyceraldehyde‐3‐phosphate dehydrogenase interact with GroEL and inhibit chaperonin‐assisted folding of the wild‐type enzyme
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1993.tb18028.xopenalex-snapshot
Lipase from Pseudomonas aeruginosa
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1996.00538.xopenalex-snapshot
Refolding and Reassociation of Glycerol Dehydrogenase from Bacillus Stearothermophilus in the Absence and Presence of Groel
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1996.00613.xopenalex-snapshot
In vitro Protein Folding by Ribosomes from Escherichia coli, Wheat Germ and Rat Liver
inferred← citeshttps://doi.org/10.1111/j.1432-1033.1997.00627.xopenalex-snapshot
Identification of Amino Acid Residues at Nucleotide‐Binding Sites of Chaperonin GroEL/GroES and cpn10 by Photoaffinity Labeling with 2‐azido‐adenosine 5′‐triphosphate
inferred← citeshttps://doi.org/10.1111/j.1749-6632.1992.tb32651.xopenalex-snapshot
The Influence of Chaperonins on Protein Folding
inferred← citeshttps://doi.org/10.1111/j.1749-6632.1994.tb44390.xopenalex-snapshot
Chaperonins and Protein Folding
inferred← citeshttps://doi.org/10.1111/mmi.15109openalex-snapshot
Mycobacterial chaperonins in cellular proteostasis: Evidence for chaperone function of Cpn60.1 and Cpn60.2‐mediated protein folding
inferred← citeshttps://doi.org/10.1126/science.7913555openalex-snapshot
Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding
inferred← citeshttps://doi.org/10.1128/mcb.14.5.2895openalex-snapshot
Facilitated Folding of Actins and Tubulins Occurs via a Nucleotide-Dependent Interaction between Cytoplasmic Chaperonin and Distinctive Folding Intermediates
inferred← citeshttps://doi.org/10.1146/annurev.biochem.67.1.581openalex-snapshot
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
inferred← citeshttps://doi.org/10.1146/annurev.pp.45.060194.002345openalex-snapshot
Structural and Functional Aspects of Chaperonin-Mediated Protein Folding
inferred← citeshttps://doi.org/10.1155/2002/601719openalex-snapshot
Characterization of the proteasome from the extremely halophilic archaeon Haloarcula marismortui
inferred← citeshttps://doi.org/10.1271/bbb.64.2668openalex-snapshot
A Cold Acclimation Protein with Refolding Activity on Frozen Denatured Enzymes
inferred← citeshttps://doi.org/10.1371/journal.pone.0170333openalex-snapshot
A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling
inferred← citeshttps://doi.org/10.1379/csc-219r.1openalex-snapshot
GroEL/S substrate specificity based on substrate unfolding propensity
inferred← citeshttps://doi.org/10.2174/0929866521666131224094408openalex-snapshot
In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques
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