Molecular chaperones in cellular protein folding

No abstract is available for this paper.

• Publication year

  1996

• Venue

  Nature

• Publication date

  1996-06-13

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1038/381571A0PMID 8637592
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Revisiting the Anfinsen cage.

  1996cited by this paper
• Roles of molecular chaperones in protein degradation

  1996cited by this paper
• Protein folding in the central cavity of the GroEL–GroES chaperonin complex

  1996cited by this paper
• The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding.

  1996cited by this paper
• Sequencing and analysis of bacterial genomes.

  1996cited by this paper
• Hsp60‐independent protein folding in the matrix of yeast mitochondria.

  1996cited by this paper
• The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

  1996cited by this paper
• A zinc finger‐like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

  1996cited by this paper
• Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.

  1996cited by this paper
• Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae

  1996cited by this paper
• Characterization of the Active Intermediate of a GroEL – GroES-Mediated Protein Folding Reaction

  1996cited by this paper
• The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.

  1996cited by this paper
• The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

  1996cited by this paper
• Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB

  1996cited by this paper
• Protein folding in the cell: competing models of chaperonin function

  1996cited by this paper
• Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein.

  1996cited by this paper
• Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

  1996cited by this paper
• Principles of Chaperone-Assisted Protein Folding: Differences Between in Vitro and in Vivo Mechanisms

  1996cited by this paper
• Primary structure of the thermosome from Thermoplasma acidophilum.

  1995cited by this paper
• A ribosome‐associated peptidyl‐prolyl cis/trans isomerase identified as the trigger factor.

  1995cited by this paper
• The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.

  1995cited by this paper
• Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes

  1995cited by this paper
• The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology.

  1995cited by this paper
• NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center

  1995cited by this paper
• Cotranslational folding and calnexin binding during glycoprotein synthesis.

  1995cited by this paper
• The Dissociation of ATP from hsp70 of Saccharomyces cerevisiae Is Stimulated by Both Ydj1p and Peptide Substrates (*)

  1995cited by this paper
• The origins and consequences of asymmetry in the chaperonin reaction cycle.

  1995cited by this paper
• Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

  1995cited by this paper
• Hsc70-binding Peptides Selected from a Phage Display Peptide Library that Resemble Organellar Targeting Sequences (*)

  1995cited by this paper
• Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

  1995cited by this paper
• Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60

  1995cited by this paper
• Contribution of cotranslational folding to the rate of formation of native protein structure.

  1995cited by this paper
• Revisiting the Anfinsen cage.

  1995cited by this paper
• Identification of GroEL as a constituent of an mRNA‐protection complex in Escherichia coli

  1995cited by this paper
• Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution

  1995cited by this paper
• The Importance of the N-terminal Segment for DnaJ-mediated Folding of Rhodanese While Bound to Ribosomes as Peptidyl-tRNA (*)

  1995cited by this paper
• Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

  1995cited by this paper
• 1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78).

  1995cited by this paper
• Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle.

  1995cited by this paper
• Specificity in chaperonin-mediated protein folding

  1995cited by this paper
• A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s

  1995cited by this paper
• Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

  1995cited by this paper
• Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ‐1.

  1995cited by this paper
• Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding

  1995cited by this paper
• Trigger factor is involved in GroEL‐dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins.

  1995cited by this paper
• Synthesis of chloramphenicol acetyltransferase in a coupled transcription‐translation in vitro system lacking the chaperones DnaK and DnaJ

  1995cited by this paper
• Role of auxilin in uncoating clathrin-coated vesicles

  1995cited by this paper
• Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.

  1995cited by this paper
• The Hydrophobic Nature of GroEL-Substrate Binding (*)

  1995cited by this paper
• Kinetics of molecular chaperone action.

  1994cited by this paper
• How chaperones tell wrong from right

  1994cited by this paper
• Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.

  1994cited by this paper
• NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.

  1994cited by this paper
• Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry

  1994cited by this paper
• Mitochondrial Hsp70/MIM44 complex facilitates protein import

  1994cited by this paper
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

  1994cited by this paper
• Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy

  1994cited by this paper
• Protein disaggregation mediated by heat-shock protein Hspl04

  1994cited by this paper
• A protein complex required for signal-sequence-specific sorting and translocation

  1994cited by this paper
• Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

  1994cited by this paper
• Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence.

  1994cited by this paper
• Calnexin: a membrane-bound chaperone of the endoplasmic reticulum.

  1994cited by this paper
• Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.

  1994cited by this paper
• Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.

  1994cited by this paper
• Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding.

  1994cited by this paper
• Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria

  1994cited by this paper
• Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44

  1994cited by this paper
• A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE

  1994cited by this paper
• The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

  1994cited by this paper
• GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms.

  1994cited by this paper
• Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

  1994cited by this paper
• Residues in chaperonin GroEL required for polypeptide binding and release

  1994cited by this paper
• Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin.

  1994cited by this paper
• The formation of symmetrical GroEL‐GroES complexes in the presence of ATP

  1994cited by this paper
• Successive action of Escherichia coli chaperones in vivo

  1994cited by this paper
• Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

  1994cited by this paper
• Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.

  1994cited by this paper
• Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones.

  1994cited by this paper
• Protein disulphide isomerase: building bridges in protein folding.

  1994cited by this paper
• The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.

  1994cited by this paper
• Folding of firefly luciferase during translation in a cell‐free system.

  1994cited by this paper
• Symmetric complexes of GroE chaperonins as part of the functional cycle.

  1994cited by this paper
• The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria.

  1994cited by this paper
• hsp70-protein complexes. Complex stability and conformation of bound substrate protein.

  1994cited by this paper
• Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes.

  1994cited by this paper
• Protein folding. Secrets of a double-doughnut.

  1994cited by this paper
• Different peptide binding specificities of hsp70 family members.

  1994cited by this paper
• Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane.

  1994cited by this paper
• Understanding how proteins fold: the lysozyme story so far.

  1994cited by this paper
• Molecular Chaperones: Opening and closing the Anfinsen cage

  1994cited by this paper
• Protein folding. Secrets of a double-doughnut.

  1994cited by this paper
• Protein disaggregation mediated by heat-shock protein Hsp104.

  1994cited by this paper
• Molecular chaperone functions of heat-shock proteins.

  1993cited by this paper
• Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.

  1993cited by this paper
• Characterization of a functionally important mobile domain of GroES

  1993cited by this paper
• ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis

  1993cited by this paper
• A polypeptide bound by the chaperonin groEL is localized within a central cavity.

  1993cited by this paper
• To fold or not to fold....

  1993cited by this paper
• Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

  1993cited by this paper
• Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

  1993cited by this paper

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