| review article | Q7318358 |
| scholarly article | Q13442814 |
| P50 | author | Elke Deuerling | Q61961366 |
| Bernd Bukau | Q20742605 | ||
| P2860 | cites work | GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. | Q52865481 |
| GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. | Q53971914 | ||
| Trigger factor and DnaK cooperate in folding of newly synthesized proteins. | Q54081409 | ||
| Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. | Q54500735 | ||
| The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. | Q54559605 | ||
| Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. | Q54559767 | ||
| In vivo observation of polypeptide flux through the bacterial chaperonin system. | Q54560154 | ||
| Recombination of protein domains facilitated by co-translational folding in eukaryotes. | Q54561866 | ||
| The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. | Q54563745 | ||
| Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. | Q54582676 | ||
| Co-translocational misfolding in the ER of living cells | Q54806598 | ||
| Proteins as molecular chaperones. | Q55060494 | ||
| Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis | Q57073746 | ||
| Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones | Q59060241 | ||
| Identification of in vivo substrates of the chaperonin GroEL | Q59068045 | ||
| A protein complex required for signal-sequence-specific sorting and translocation | Q24315826 | ||
| Effects of macromolecular crowding on protein folding and aggregation | Q24529974 | ||
| Molecular chaperones as HSF1-specific transcriptional repressors | Q24606489 | ||
| Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit | Q27619579 | ||
| The complete atomic structure of the large ribosomal subunit at 2.4 A resolution | Q27626400 | ||
| The structural basis of ribosome activity in peptide bond synthesis | Q27626414 | ||
| Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution | Q27627220 | ||
| Structure of the 30S ribosomal subunit | Q27627261 | ||
| Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein | Q27667092 | ||
| Structural analysis of substrate binding by the molecular chaperone DnaK | Q27732810 | ||
| The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex | Q27742747 | ||
| Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. | Q27863666 | ||
| Initial characterization of the nascent polypeptide-associated complex in yeast | Q27930105 | ||
| A functional chaperone triad on the yeast ribosome | Q27930569 | ||
| The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. | Q27931088 | ||
| Zuotin, a ribosome-associated DnaJ molecular chaperone | Q27933106 | ||
| Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria | Q27933539 | ||
| The nascent polypeptide-associated complex (NAC) of yeast functions in the targeting process of ribosomes to the ER membrane | Q27934800 | ||
| The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex | Q27935359 | ||
| RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. | Q27938678 | ||
| The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions | Q28138434 | ||
| Understanding protein folding via free-energy surfaces from theory and experiment | Q28139374 | ||
| Molecular chaperones in the cytosol: from nascent chain to folded protein | Q28205903 | ||
| Nascent-polypeptide-associated complex | Q28217074 | ||
| Principles that govern the folding of protein chains | Q28236872 | ||
| Kinetics of molecular chaperone action | Q28259596 | ||
| T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol | Q28283227 | ||
| From Levinthal to pathways to funnels | Q28300934 | ||
| The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity | Q28354278 | ||
| An insertional mutation in the BTF3 transcription factor gene leads to an early postimplantation lethality in mice | Q28588824 | ||
| The Hsp70 and Hsp60 chaperone machines | Q29547601 | ||
| Common principles of protein translocation across membranes | Q29616412 | ||
| Folding of newly translated proteins in vivo: the role of molecular chaperones | Q29619368 | ||
| Protein import into mitochondria | Q29620420 | ||
| Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity. | Q30164196 | ||
| Random circular permutation of DsbA reveals segments that are essential for protein folding and stability | Q30648508 | ||
| Trigger Factor and DnaK possess overlapping substrate pools and binding specificities | Q31132930 | ||
| Principles of protein folding in the cellular environment | Q33536619 | ||
| GroEL/GroES: structure and function of a two-stroke folding machine | Q33537194 | ||
| Chaperone rings in protein folding and degradation. | Q33740150 | ||
| Role and regulation of the ER chaperone BiP. | Q33794221 | ||
| Getting newly synthesized proteins into shape. | Q33901641 | ||
| Binding specificity of Escherichia coli trigger factor | Q33951759 | ||
| Conformational changes studied by cryo-electron microscopy | Q34019493 | ||
| The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain | Q34046935 | ||
| Folding of a nascent peptide on the ribosome | Q34070555 | ||
| Molecular basis for interactions of the DnaK chaperone with substrates. | Q34081455 | ||
| The ribosomal exit tunnel functions as a discriminating gate | Q34118341 | ||
| The protein import motor of mitochondria | Q34142481 | ||
| In vivo analysis of the overlapping functions of DnaK and trigger factor | Q34165784 | ||
| Versatility of the mitochondrial protein import machinery | Q34238028 | ||
| The structural basis of protein targeting and translocation in bacteria. | Q34261907 | ||
| SecB is a bona fide generalized chaperone in Escherichia coli | Q34336036 | ||
| Hsp70 chaperone machines. | Q34545594 | ||
| Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding | Q34545652 | ||
| Protein folding and unfolding at atomic resolution | Q34574339 | ||
| Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli | Q34626779 | ||
| The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? | Q34808336 | ||
| Mechanisms of protein folding: molecular chaperones and their application in biotechnology | Q34811977 | ||
| Mitochondrial protein import: two membranes, three translocases | Q34970740 | ||
| Diffusion control in an elementary protein folding reaction | Q36153029 | ||
| The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures | Q36174913 | ||
| Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism | Q36176422 | ||
| NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center | Q36235831 | ||
| Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins | Q36322146 | ||
| Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones | Q36351463 | ||
| Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries | Q36857677 | ||
| Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria | Q36919506 | ||
| Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. | Q37639742 | ||
| Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. | Q38316145 | ||
| Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes | Q39790938 | ||
| Macromolecular crowding: biochemical, biophysical, and physiological consequences | Q40488946 | ||
| Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane | Q40611469 | ||
| Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains | Q40901972 | ||
| GroEL-mediated protein folding | Q41429098 | ||
| The major pathways of protein translocation across membranes | Q41458138 | ||
| Interaction of Hsp70 chaperones with substrates | Q41465900 | ||
| Three-dimensional structures of translating ribosomes by Cryo-EM. | Q41628474 | ||
| The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. | Q41633923 | ||
| Cotranslational protein folding | Q41667140 | ||
| Chaperonin function: folding by forced unfolding | Q42097312 | ||
| Folding of malate dehydrogenase inside the GroEL-GroES cavity | Q43688024 | ||
| Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins | Q43760493 | ||
| GroEL/GroES-mediated folding of a protein too large to be encapsulated | Q43774197 | ||
| L23 protein functions as a chaperone docking site on the ribosome | Q44134061 | ||
| The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane | Q44170438 | ||
| Three-state equilibrium of Escherichia coli trigger factor | Q44229595 | ||
| Interaction of trigger factor with the ribosome | Q44298013 | ||
| Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent | Q44684012 | ||
| A cytoplasmic chaperonin that catalyzes beta-actin folding | Q45345723 | ||
| The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane | Q46059428 | ||
| Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed | Q47765907 | ||
| Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. | Q51040073 | ||
| Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. | Q52531960 | ||
| P433 | issue | 5-6 | |
| P921 | main subject | molecular chaperones | Q422496 |
| protein folding | Q847556 | ||
| P304 | page(s) | 261-277 | |
| P577 | publication date | 2004-09-01 | |
| P1433 | published in | Critical Reviews in Biochemistry and Molecular Biology | Q5186661 |
| P1476 | title | Chaperone-assisted folding of newly synthesized proteins in the cytosol | |
| P478 | volume | 39 |
| Q48359218 | AgHalo: A Facile Fluorogenic Sensor to Detect Drug-Induced Proteome Stress. |
| Q42286931 | Altered expression of HSP70 in oral lichen planus |
| Q28248982 | An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell |
| Q34564806 | Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases |
| Q34628984 | Celastrol, an oral heat shock activator, ameliorates multiple animal disease models of cell death |
| Q33287499 | Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli |
| Q36777158 | Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. |
| Q34822475 | Chemical and biological approaches synergize to ameliorate protein-folding diseases. |
| Q37819121 | Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases |
| Q30156882 | Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy |
| Q40292207 | Depletion of hsp90beta induces multiple defects in B cell receptor signaling. |
| Q35039971 | Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain |
| Q41976836 | Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis. |
| Q39190061 | FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts. |
| Q30512981 | FoldEco: a model for proteostasis in E. coli |
| Q36759904 | Formation of covalently modified folding intermediates of simian virus 40 Vp1 in large T antigen-expressing cells |
| Q36539816 | GroEL-mediated protein folding: making the impossible, possible |
| Q36531705 | Heat shock protein 70 selectively mediates the degradation of cytosolic PrPs and restores the cytosolic PrP-induced cytotoxicity via a molecular interaction |
| Q33285751 | Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor |
| Q35236697 | Improved cell-free RNA and protein synthesis system |
| Q39166316 | Increased expression of the integral membrane proteins EGFR and FGFR3 in anti-apoptotic Chinese hamster ovary cell lines |
| Q42734301 | Increased protein synthesis by cells exposed to a 1,800-MHz radio-frequency mobile phone electromagnetic field, detected by proteome profiling |
| Q26779247 | Insights into the molecular mechanism of allostery in Hsp70s |
| Q88596142 | Intra-molecular pathways of allosteric control in Hsp70s |
| Q33247451 | Molecular simulations of cotranslational protein folding: fragment stabilities, folding cooperativity, and trapping in the ribosome |
| Q33523398 | New structural and functional defects in polyphosphate deficient bacteria: a cellular and proteomic study |
| Q30667048 | Pathways of allosteric regulation in Hsp70 chaperones. |
| Q54439108 | Potential new antibiotic sites in the ribosome revealed by deleterious mutations in RNA of the large ribosomal subunit. |
| Q30484647 | Prefoldin 6 is required for normal microtubule dynamics and organization in Arabidopsis. |
| Q34168308 | Protein folding at the exit tunnel |
| Q35689040 | Proteome and antigen profiling of Coxiella burnetii developmental forms |
| Q29614783 | Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging |
| Q54453420 | Real-time observation of trigger factor function on translating ribosomes. |
| Q33766707 | Redox-regulated chaperones |
| Q54483511 | Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms. |
| Q37412871 | SAHA enhances Proteostasis of epilepsy-associated α1(A322D)β2γ2 GABA(A) receptors. |
| Q51096812 | Strain engineering and process optimization for enhancing the production of a thermostable steryl glucosidase in Escherichia coli. |
| Q37424170 | Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins |
| Q60907513 | The Autoantigenic Proinsulin B-Chain Peptide B11-23 Synergises with the 70 kDa Heat Shock Protein DnaK in Macrophage Stimulation |
| Q38967042 | The Blueprint of a Minimal Cell: MiniBacillus |
| Q42957645 | The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G. |
| Q38942835 | The association of SNPs in Hsp90β gene 5' flanking region with thermo tolerance traits and tissue mRNA expression in two chicken breeds |
| Q24676115 | The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system |
| Q36420053 | The physics of the interactions governing folding and association of proteins |
| Q34181891 | The stress of protein misfolding: from single cells to multicellular organisms |
| Q26775973 | The wonderous chaperones: A highlight on therapeutics of cancer and potentially malignant disorders |
| Q35830231 | Topologies of a substrate protein bound to the chaperonin GroEL |
| Q42957820 | Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli |
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