Molecular chaperones in cellular protein folding (Q29547795)

Europe PubMed Central

title

Molecular chaperones in cellular protein folding (English)

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

23 April 2017

0 references

0 references

1

Hartl FU

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

23 April 2017

language of work or name

1 reference

23 April 2017

publication date

13 June 1996

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

23 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

23 April 2017

volume

381

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

23 April 2017

issue

6583

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

23 April 2017

page(s)

571-9

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

Principles that govern the folding of protein chains

23 April 2017

cites work

1 reference

7 January 2021

Proteins as molecular chaperones.

1 reference

7 January 2021

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

1 reference

7 January 2021

Protein folding in the cell

1 reference

7 January 2021

Molecular chaperone functions of heat-shock proteins

1 reference

7 January 2021

Protein disulphide isomerase: building bridges in protein folding

1 reference

7 January 2021

Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions

1 reference

7 January 2021

Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA

1 reference

7 January 2021

Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides

1 reference

7 January 2021

Speculations on the functions of the major heat shock and glucose-regulated proteins

1 reference

7 January 2021

Immunoglobulin heavy chain binding protein

1 reference

7 January 2021

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

1 reference

7 January 2021

70K heat shock related proteins stimulate protein translocation into microsomes.

1 reference

7 January 2021

Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

1 reference

7 January 2021

Peptide-binding specificity of the molecular chaperone BiP

1 reference

7 January 2021

Host participation in bacteriophage lambda head assembly

1 reference

7 January 2021

Abortive bacteriophage T4 head assembly in mutants of Escherichia coli

1 reference

7 January 2021

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

1 reference

7 January 2021

Inhibition of ribulose bisphosphate carboxylase assembly by antibody to a binding protein

1 reference

7 January 2021

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

7 January 2021

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

Understanding how proteins fold: the lysozyme story so far.

1 reference

7 January 2021

Global suppression of protein folding defects and inclusion body formation

1 reference

7 January 2021

Protein folding in the cell: competing models of chaperonin function.

1 reference

7 January 2021

Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

1 reference

7 January 2021

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

1 reference

7 January 2021

The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA.

1 reference

7 January 2021

Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides

1 reference

7 January 2021

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

1 reference

7 January 2021

Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes

1 reference

7 January 2021

Folding of firefly luciferase during translation in a cell-free system.

1 reference

7 January 2021

Contribution of cotranslational folding to the rate of formation of native protein structure

1 reference

7 January 2021

Cotranslational folding and calnexin binding during glycoprotein synthesis

1 reference

7 January 2021

Sec61p and BiP directly facilitate polypeptide translocation into the ER.

1 reference

7 January 2021

Role of auxilin in uncoating clathrin-coated vesicles.

1 reference

7 January 2021

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

1 reference

7 January 2021

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

1 reference

7 January 2021

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.

1 reference

7 January 2021

The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology

1 reference

7 January 2021

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.

1 reference

7 January 2021

1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78)

1 reference

7 January 2021

A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

1 reference

7 January 2021

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

1 reference

7 January 2021

Different peptide binding specificities of hsp70 family members.

1 reference

7 January 2021

Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences

1 reference

7 January 2021

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

1 reference

7 January 2021

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

1 reference

7 January 2021

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

1 reference

7 January 2021

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

1 reference

7 January 2021

Kinetics of molecular chaperone action

1 reference

7 January 2021

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

1 reference

7 January 2021

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

1 reference

7 January 2021

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates

1 reference

7 January 2021

Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

1 reference

7 January 2021

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

1 reference

7 January 2021

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

1 reference

7 January 2021

Protein disaggregation mediated by heat-shock protein Hsp104.

1 reference

7 January 2021

Roles of molecular chaperones in protein degradation

1 reference

7 January 2021

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

1 reference

7 January 2021

The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria

1 reference

7 January 2021

Mitochondrial Hsp70/MIM44 complex facilitates protein import

1 reference

7 January 2021

What drives the translocation of proteins?

1 reference

7 January 2021

Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44

1 reference

7 January 2021

Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane

1 reference

7 January 2021

The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.

1 reference

7 January 2021

Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coli

1 reference

7 January 2021

A polypeptide bound by the chaperonin groEL is localized within a central cavity

1 reference

7 January 2021

ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

1 reference

7 January 2021

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

7 January 2021

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

1 reference

7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

7 January 2021

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

1 reference

7 January 2021

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

1 reference

7 January 2021

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

1 reference

7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

7 January 2021

The hydrophobic nature of GroEL-substrate binding

1 reference

7 January 2021

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

1 reference

7 January 2021

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

1 reference

7 January 2021

Prevention of protein denaturation under heat stress by the chaperonin Hsp60

1 reference

7 January 2021

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

7 January 2021

Protein folding. Secrets of a double-doughnut.

1 reference

7 January 2021

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 reference

7 January 2021

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

7 January 2021

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

7 January 2021

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

1 reference

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

7 January 2021

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

1 reference

7 January 2021

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

1 reference

7 January 2021

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

1 reference

7 January 2021

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

7 January 2021

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

1 reference

7 January 2021

Proper and improper folding of proteins in the cellular environment

1 reference

7 January 2021

Unfolding protein folding

1 reference

7 January 2021

To fold or not to fold....

1 reference

7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

7 January 2021

Revisiting the Anfinsen cage

1 reference

7 January 2021

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

7 January 2021

Refolding of barnase in the presence of GroE

1 reference

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

7 January 2021

Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin

1 reference

7 January 2021

A cytoplasmic chaperonin that catalyzes beta-actin folding

1 reference

7 January 2021

TCP1 complex is a molecular chaperone in tubulin biogenesis

1 reference

7 January 2021

Specificity in chaperonin-mediated protein folding

1 reference

7 January 2021

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

1 reference

7 January 2021

Structure of a molecular chaperone from a thermophilic archaebacterium

1 reference

7 January 2021

Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.

1 reference

7 January 2021

Primary structure of the thermosome from Thermoplasma acidophilum.

1 reference

7 January 2021

Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms

1 reference

7 January 2021

Calnexin: a membrane-bound chaperone of the endoplasmic reticulum

1 reference

7 January 2021

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

1 reference

7 January 2021

Sequencing and analysis of bacterial genomes

1 reference

7 January 2021

Successive action of Escherichia coli chaperones in vivo.

1 reference

7 January 2021

Synthesis of chloramphenicol acetyltransferase in a coupled transcription-translation in vitro system lacking the chaperones DnaK and DnaJ.

1 reference

7 January 2021

Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence.

1 reference

7 January 2021

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

1 reference

7 January 2021

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

1 reference

7 January 2021

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

1 reference

7 January 2021

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.

1 reference

7 January 2021

Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding

1 reference

7 January 2021

Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria

1 reference

7 January 2021

Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60

1 reference

7 January 2021

A protein complex required for signal-sequence-specific sorting and translocation

1 reference

7 January 2021

NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center

1 reference

7 January 2021

Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1.

1 reference

7 January 2021

Intracellular protein trafficking defects in human disease

1 reference

7 January 2021

Resting places on folding pathways

1 reference

7 January 2021

How chaperones tell wrong from right

1 reference

7 January 2021

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

Identifiers

2 references

23 April 2017

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

40127

1029280955

0 references

40127

1 reference

Consolidated OpenCitations Corpus – April 2017

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592

2 references

23 April 2017

Consolidated OpenCitations Corpus – April 2017