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Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/jmbi.1999.3040openalex-snapshot
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices 1 1Edited by J. Karn
inferredcites →https://doi.org/10.1006/jsbi.2001.4352openalex-snapshot
Review: Mechanisms of Disaggregation and Refolding of Stable Protein Aggregates by Molecular Chaperones
inferredcites →https://doi.org/10.1006/jsbi.2001.4373openalex-snapshot
ATP-Induced Structural Change of the Thermosome Is Temperature-Dependent
inferredcites →https://doi.org/10.1006/prep.2001.1465openalex-snapshot
High-Throughput Proteomics: Protein Expression and Purification in the Postgenomic World
inferredcites →https://doi.org/10.1016/0092-8674(93)90470-bopenalex-snapshot
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
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/s0065-2164(01)50007-6openalex-snapshot
Protein folding and molecular chaperones in Archaea
inferredcites →https://doi.org/10.1016/s0092-8674(00)00165-3openalex-snapshot
Structure of the Molecular Chaperone Prefoldin
inferredcites →https://doi.org/10.1016/s0092-8674(00)80408-0openalex-snapshot
Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin
inferredcites →https://doi.org/10.1016/s0092-8674(00)80509-7openalex-snapshot
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
inferredcites →https://doi.org/10.1016/s0092-8674(00)80692-3openalex-snapshot
Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL
inferredcites →https://doi.org/10.1016/s0092-8674(00)80787-4openalex-snapshot
Polypeptide Flux through Bacterial Hsp70
inferredcites →https://doi.org/10.1016/s0092-8674(00)80806-5openalex-snapshot
Getting Newly Synthesized Proteins into Shape
inferredcites →https://doi.org/10.1016/s0092-8674(00)80830-2openalex-snapshot
Structure of TPR Domain–Peptide Complexes
inferredcites →https://doi.org/10.1016/s0092-8674(00)80928-9openalex-snapshot
The Hsp70 and Hsp60 Chaperone Machines
inferredcites →https://doi.org/10.1016/s0092-8674(00)81152-6openalex-snapshot
Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT
inferredcites →https://doi.org/10.1016/s0092-8674(00)81293-3openalex-snapshot
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
inferredcites →https://doi.org/10.1016/s0092-8674(00)81342-2openalex-snapshot
The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
inferredcites →https://doi.org/10.1016/s0092-8674(00)81446-4openalex-snapshot
Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin
inferredcites →https://doi.org/10.1016/s0092-8674(00)81673-6openalex-snapshot
The Crystal Structure of a GroEL/Peptide Complex
inferredcites →https://doi.org/10.1016/s0092-8674(01)00517-7openalex-snapshot
Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding
inferredcites →https://doi.org/10.1016/s0092-8674(01)00523-2openalex-snapshot
GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated
inferredcites →https://doi.org/10.1016/s0959-440x(00)00172-xopenalex-snapshot
Macromolecular crowding: an important but neglected aspect of the intracellular environment
inferredcites →https://doi.org/10.1016/s0959-440x(99)00045-7openalex-snapshot
Implications of macromolecular crowding for protein assembly
inferredcites →https://doi.org/10.1016/s0959-440x(99)00046-9openalex-snapshot
Enzymes that catalyse the restructuring of proteins
inferredcites →https://doi.org/10.1016/s0959-440x(99)80012-8openalex-snapshot
The fundamentals of protein folding: bringing together theory and experiment
inferredcites →https://doi.org/10.1016/s0960-9822(01)00487-0openalex-snapshot
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
inferredcites →https://doi.org/10.1016/s0960-9822(01)00620-0openalex-snapshot
Molecular chaperones: Inside and outside the Anfinsen cage
inferredcites →https://doi.org/10.1016/s0968-0004(00)01707-2openalex-snapshot
Protein folding: progress made and promises ahead
inferredcites →https://doi.org/10.1016/s0968-0004(98)01193-1openalex-snapshot
The ins and outs of a molecular chaperone machine
inferredcites →https://doi.org/10.1016/s0968-0004(99)01373-0openalex-snapshot
Hsp90 & Co. – a holding for folding
inferredcites →https://doi.org/10.1016/s0968-0004(99)01445-0openalex-snapshot
Protein misfolding, evolution and disease
inferredcites →https://doi.org/10.1016/s0969-2126(00)00170-2openalex-snapshot
The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
inferredcites →https://doi.org/10.1016/s1097-2765(00)80158-6openalex-snapshot
J Proteins Catalytically Activate Hsp70 Molecules to Trap a Wide Range of Peptide Sequences
inferredcites →https://doi.org/10.1021/bi972928iopenalex-snapshot
Folding of Firefly (Photinus pyralis) Luciferase: Aggregation and Reactivation of Unfolding Intermediates
inferredcites →https://doi.org/10.1038/14032openalex-snapshot
Co-translational folding of an alphavirus capsid protein in the cytosol of living cells
inferredcites →https://doi.org/10.1038/23301openalex-snapshot
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
inferredcites →https://doi.org/10.1038/35037619openalex-snapshot
The complete sequence of the mucosal pathogen Ureaplasma urealyticum
inferredcites →https://doi.org/10.1038/35050618openalex-snapshot
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
inferredcites →https://doi.org/10.1038/356683a0openalex-snapshot
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
inferredcites →https://doi.org/10.1038/370111a0openalex-snapshot
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
inferredcites →https://doi.org/10.1038/370434a0openalex-snapshot
A protein complex required for signal-sequence-specific sorting and translocation
inferredcites →https://doi.org/10.1038/379420a0openalex-snapshot
Protein folding in the central cavity of the GroEL–GroES chaperonin complex
inferredcites →https://doi.org/10.1038/381571a0openalex-snapshot
Molecular chaperones in cellular protein folding
inferredcites →https://doi.org/10.1038/41024openalex-snapshot
Recombination of protein domains facilitated by co-translational folding in eukaryotes
inferredcites →https://doi.org/10.1038/41944openalex-snapshot
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
inferredcites →https://doi.org/10.1038/45977openalex-snapshot
Identification of in vivo substrates of the chaperonin GroEL
inferredcites →https://doi.org/10.1038/74062openalex-snapshot
Structural insights into substrate binding by the molecular chaperone DnaK.
inferredcites →https://doi.org/10.1038/76819openalex-snapshot
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
inferredcites →https://doi.org/10.1038/90443openalex-snapshot
Folding of malate dehydrogenase inside the GroEL-GroES cavity.
inferredcites →https://doi.org/10.1073/pnas.071057198openalex-snapshot
RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin
inferredcites →https://doi.org/10.1073/pnas.261432298openalex-snapshot
Binding specificity of Escherichia coli trigger factor
inferredcites →https://doi.org/10.1073/pnas.91.22.10345openalex-snapshot
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.
inferredcites →https://doi.org/10.1073/pnas.93.9.4437openalex-snapshot
Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
inferredcites →https://doi.org/10.1073/pnas.94.4.1107openalex-snapshot
The effect of macromolecular crowding on chaperonin-mediated protein folding
inferredcites →https://doi.org/10.1073/pnas.95.22.12860openalex-snapshot
Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
inferredcites →https://doi.org/10.1074/jbc.275.7.4613openalex-snapshot
The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome
inferredcites →https://doi.org/10.1074/jbc.m006368200openalex-snapshot
The α and β Subunit of the Nascent Polypeptide-associated Complex Have Distinct Functions
inferredcites →https://doi.org/10.1083/jcb.145.2.265openalex-snapshot
Prefoldin–Nascent Chain Complexes in the Folding of Cytoskeletal Proteins
inferredcites →https://doi.org/10.1083/jcb.149.3.591openalex-snapshot
The Interaction of the Chaperonin Tailless Complex Polypeptide 1 (Tcp1) Ring Complex (Tric) with Ribosome-Bound Nascent Chains Examined Using Photo-Cross-Linking
inferredcites →https://doi.org/10.1093/emboj/16.20.6209openalex-snapshot
GrpE‐like regulation of the Hsc70 chaperone by the anti‐apoptotic protein BAG‐1
inferredcites →https://doi.org/10.1093/emboj/16.7.1501openalex-snapshot
Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries
inferredcites →https://doi.org/10.1093/emboj/17.14.3981openalex-snapshot
The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome–nascent chain complex
inferredcites →https://doi.org/10.1093/emboj/17.4.952openalex-snapshot
A novel protein complex promoting formation of functional α‐ and γ‐tubulin
inferredcites →https://doi.org/10.1093/emboj/18.1.75openalex-snapshot
Compartmentation of protein folding in vivo: sequestration of non‐native polypeptide by the chaperonin–GimC system
inferredcites →https://doi.org/10.1093/emboj/18.1.85openalex-snapshot
In vivo newly translated polypeptides are sequestered in a protected folding environment
inferredcites →https://doi.org/10.1093/emboj/18.23.6730openalex-snapshot
MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
inferredcites →https://doi.org/10.1093/emboj/18.24.6927openalex-snapshot
Effects of macromolecular crowding on protein folding and aggregation
inferredcites →https://doi.org/10.1093/emboj/19.22.5971openalex-snapshot
Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi‐native conformations
inferredcites →https://doi.org/10.1093/emboj/20.15.4065openalex-snapshot
The ‘sequential allosteric ring’ mechanism in the eukaryotic chaperonin‐assisted folding of actin and tubulin
inferredcites →https://doi.org/10.1093/emboj/20.5.1042openalex-snapshot
Its substrate specificity characterizes the DnaJ co‐chaperone as a scanning factor for the DnaK chaperone
inferredcites →https://doi.org/10.1093/hmg/10.14.1511openalex-snapshot
Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
inferredcites →https://doi.org/10.1107/s0021889891004399openalex-snapshot
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
inferredcites →https://doi.org/10.1126/science.1057268openalex-snapshot
Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors
inferredcites →https://doi.org/10.1126/science.272.5268.1606openalex-snapshot
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
inferredcites →https://doi.org/10.1126/science.276.5311.431openalex-snapshot
Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK
inferredcites →https://doi.org/10.1126/science.284.5415.822openalex-snapshot
Chaperonin Function: Folding by Forced Unfolding
inferredcites →https://doi.org/10.1126/science.287.5459.1837openalex-snapshot
Genetic Suppression of Polyglutamine Toxicity in Drosophila
inferredcites →https://doi.org/10.1126/science.289.5481.920openalex-snapshot
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
inferredcites →https://doi.org/10.1128/jb.171.3.1379-1385.1989openalex-snapshot
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
inferredcites →https://doi.org/10.1146/annurev.biochem.67.1.581openalex-snapshot
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
inferredcites →https://doi.org/10.1146/annurev.biochem.70.1.603openalex-snapshot
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Direct Observation of the Mechanical Role of Bacterial Chaperones in Protein Folding
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Chaperones, Molecular
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Stress-Induced Expression of Heat Shock Proteins and Action of the Heat Shock Protein Effectors
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Protein Folding in Vivo
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Chaperones, Chaperonins and Heat‐Shock Proteins
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Mechanism and Function of the Eukaryotic Chaperonin CCT
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A Hitchhiker's Guide to Evolving Networks
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Cataract as a Protein‐Aggregation Disease
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Role of Molecular Chaperones in Protein Folding
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Caenorhabditis Elegansas a Model System to Study the Biology of Protein Aggregation and Toxicity
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HSP60 Speaks to the Immune System in Many Voices
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Fundamental Structures and Behaviors of Proteins
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Potential of Heat Shock Protein Targeting for Human Therapy
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Intrinsically Disordered Chaperones and Neurodegeneration
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Therapeutics: Harnessing the Power of Molecular and Pharmacological Chaperones
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Regulation of the Polyglutamine Androgen Receptor by the Hsp90/Hsp70‐Based Chaperone Machinery
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Chaperone‐Dependent Amyloid Assembly and Prion Toxicity
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General Overview of Basic Concepts in Molecular Biophysics
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GroEL/ES Chaperonin: Unfolding and Refolding Reactions
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Plasmodesmata: Protein Transport Signals and Receptors
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Metallocenter Biosynthesis & Assembly
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Metallocenter Biosynthesis & AssemblyUpdate based on the original article by Scott B. Mulrooney and Robert P. Hausinger,Encyclopedia of Inorganic Chemistry© 2005, John Wiley & Sons, Ltd
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An Overview of Protein Misfolding Diseases
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Studying Protein Folding in Vivo
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Analysis of Chaperone Function in Vitro
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Ribosome‐associated Proteins Acting on Newly Synthesized Polypeptide Chains
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The Role of Trigger Factor in Folding of Newly Synthesized Proteins
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Cellular Functions of Hsp70 Chaperones
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Unfolding of Proteins During Import into Mitochondria
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The Chaperone System of Mitochondria
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An Overview of Protein Misfolding Diseases
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Insights into the Nature of Yeast Prions
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Polyglutamine Aggregates as a Model for Protein‐misfolding Diseases
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Biomimetic Design of a Robustly Stabilized Folded State Enabling Seed‐Initiated Supramolecular Polymerization under Microfluidic Mixing**
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Mechanical Nanosensor Based on FRET within a Thermosome: Damage‐Reporting Polymeric Materials
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Programmed Morphological Transitions of Multisegment Assemblies by Molecular Chaperone Analogues
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Maintenance of Amyloid β Peptide Homeostasis by Artificial Chaperones Based on Mixed‐Shell Polymeric Micelles
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AgHalo: A Facile Fluorogenic Sensor to Detect Drug‐Induced Proteome Stress
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Seeded Polymerization through the Interplay of Folding and Aggregation of an Amino‐Acid‐based Diamide
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Biomimetic Design of a Robustly Stabilized Folded State Enabling Seed‐Initiated Supramolecular Polymerization under Microfluidic Mixing**
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Sudden origins: A general mechanism of evolution based on stress protein concentration and rapid environmental change
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Effects of heat shock on ovary development and hsp83 expression in Tribolium castaneum (Coleoptera: Tenebrionidae)
inferred← citeshttps://doi.org/10.1002/arch.21536openalex-snapshot
Molecular characterization and expression patterns of Phenacoccus solenopsis (Hemiptera: Pseudococcidae) heat shock protein genes and their response to host stress
inferred← citeshttps://doi.org/10.1002/bies.20020openalex-snapshot
Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance
inferred← citeshttps://doi.org/10.1002/bies.201000081openalex-snapshot
The polypeptide tunnel exit of the mitochondrial ribosome is tailored to meet the specific requirements of the organelle
inferred← citeshttps://doi.org/10.1002/bies.201900250openalex-snapshot
Peptidylprolylisomerases, Protein Folders, or Scaffolders? The Example of FKBP51 and FKBP52
inferred← citeshttps://doi.org/10.1002/bies.20852openalex-snapshot
Dysfunction of the ubiquitin–proteasome system in multiple disease conditions: therapeutic approaches
inferred← citeshttps://doi.org/10.1002/biot.200900106openalex-snapshot
An antibody‐based affinity chromatography tool to assess Cu, Zn superoxide dismutase (SOD) G93A structural complexity in vivo
inferred← citeshttps://doi.org/10.1002/biot.201800039openalex-snapshot
Heat Shock Protein Reports on Proteome Stress
inferred← citeshttps://doi.org/10.1002/bip.20106openalex-snapshot
The Mycobacterium tuberculosis chaperonin 10 monomer exhibits structural plasticity
inferred← citeshttps://doi.org/10.1002/bip.20665openalex-snapshot
From the test tube to the cell: Exploring the folding and aggregation of a β‐clam protein
inferred← citeshttps://doi.org/10.1002/bip.21302openalex-snapshot
Hsp70 molecular chaperones and Parkinson's disease
inferred← citeshttps://doi.org/10.1002/bip.21426openalex-snapshot
Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation
inferred← citeshttps://doi.org/10.1002/bip.22361openalex-snapshot
ATP‐driven molecular chaperone machines
inferred← citeshttps://doi.org/10.1002/bip.22760openalex-snapshot
Molecular basis of the structural stability of hemochromatosis factor E : A combined molecular dynamic simulation and GdmCl‐induced denaturation study
inferred← citeshttps://doi.org/10.1002/bit.20733openalex-snapshot
Prevention of thermal induced aggregation of cytochrome c at isoelectric pH values by polyanions
inferred← citeshttps://doi.org/10.1002/bit.20781openalex-snapshot
Stabilization of Taq DNA Polymerase at High Temperature by Protein Folding Pathways From a Hyperthermophilic Archaeon, Pyrococcus furiosus
inferred← citeshttps://doi.org/10.1002/bit.20832openalex-snapshot
Protein translocation through a tunnel induces changes in folding kinetics: A lattice model study
inferred← citeshttps://doi.org/10.1002/bit.21234openalex-snapshot
Molecular portrait of high productivity in recombinant NS0 cells
inferred← citeshttps://doi.org/10.1002/bit.21253openalex-snapshot
Proteome analysis of heat shock protein expression in Pseudomonas alcaligenes NCIMB 9867 in response to gentisate exposure and elevated growth temperature
inferred← citeshttps://doi.org/10.1002/bit.23111openalex-snapshot
Localization of BiP to translating ribosomes increases soluble accumulation of secreted eukaryotic proteins in an Escherichia coli cell‐free system
inferred← citeshttps://doi.org/10.1002/bit.26879openalex-snapshot
RNA‐dependent chaperone (chaperna) as an engineered pro‐region for the folding of recombinant microbial transglutaminase
inferred← citeshttps://doi.org/10.1002/cbic.201000166openalex-snapshot
Rational Design of Novel Peptidic DnaK Ligands
inferred← citeshttps://doi.org/10.1002/cbic.201000602openalex-snapshot
Bacterial Inclusion Bodies of Alzheimer's Disease β‐Amyloid Peptides Can Be Employed To Study Native‐Like Aggregation Intermediate States
inferred← citeshttps://doi.org/10.1002/cbic.202100459openalex-snapshot
Novel Antibacterial Targets in Protein Biogenesis Pathways
inferred← citeshttps://doi.org/10.1002/cbin.10321openalex-snapshot
Maternal caffeine exposure impairs insulin secretion by pancreatic β‐cells and increases the risk of type II diabetes mellitus in offspring
inferred← citeshttps://doi.org/10.1002/cfg.405openalex-snapshot
Investigation into the use of C‐ and N‐terminal GFP fusion proteins for subcellular localization studies using reverse transfection microarrays
inferred← citeshttps://doi.org/10.1002/cm.20480openalex-snapshot
Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity
inferred← citeshttps://doi.org/10.1002/cmdc.200900256openalex-snapshot
Structure‐Based and in silico Design of Hsp90 Inhibitors
inferred← citeshttps://doi.org/10.1002/cphc.200400609openalex-snapshot
Single‐Molecule Fluorescence Spectroscopy of Protein Folding
inferred← citeshttps://doi.org/10.1002/cphc.200700662openalex-snapshot
From Valleys to Ridges: Exploring the Dynamic Energy Landscape of Single Membrane Proteins
inferred← citeshttps://doi.org/10.1002/dvdy.21524openalex-snapshot
Hsp60C is required in follicle as well as germline cells during oogenesis in Drosophila melanogaster
inferred← citeshttps://doi.org/10.1002/eji.200425603openalex-snapshot
Scant activation of CD8 T cells by antigen loaded on heat shock protein
inferred← citeshttps://doi.org/10.1002/eji.200737661openalex-snapshot
A heat shock protein gene (Hsp70.1) is critically involved in the generation of the immune response to myelin antigen
inferred← citeshttps://doi.org/10.1002/emmm.200900002openalex-snapshot
The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease
inferred← citeshttps://doi.org/10.1002/hep.20108openalex-snapshot
Immunohistochemical analysis of Mallory bodies in Wilsonian and non-Wilsonian hepatic copper toxicosis
inferred← citeshttps://doi.org/10.1002/hep.29732openalex-snapshot
Extracellular vesicles from mice with alcoholic liver disease carry a distinct protein cargo and induce macrophage activation through heat shock protein 90
inferred← citeshttps://doi.org/10.1002/humu.22335openalex-snapshot
Correction of Cystathionine β-Synthase Deficiency in Mice by Treatment with Proteasome Inhibitors
inferred← citeshttps://doi.org/10.1002/ibd.21944openalex-snapshot
Mitochondria at the Interface Between Danger Signaling and Metabolism: Role of Unfolded Protein Responses in Chronic Inflammation
inferred← citeshttps://doi.org/10.1002/ijc.24520openalex-snapshot
Regulation of HSP70 on activating macrophages using PDT‐induced apoptotic cells
inferred← citeshttps://doi.org/10.1002/iub.1656openalex-snapshot
Substrate specificity in the context of molecular chaperones
inferred← citeshttps://doi.org/10.1002/iub.526openalex-snapshot
Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine
inferred← citeshttps://doi.org/10.1002/jat.1352openalex-snapshot
Lack of cross‐tolerance following heat and cadmium exposure in functional MDCK monolayers
inferred← citeshttps://doi.org/10.1002/jcb.21362openalex-snapshot
HSPA1A is an important regulator of the stability and function of ZNF198 and its oncogenic derivative, ZNF198–FGFR1
inferred← citeshttps://doi.org/10.1002/jcb.24550openalex-snapshot
Protective induction of Hsp70 in heat‐stressed primary myoblasts: Involvement of MAPKs
inferred← citeshttps://doi.org/10.1002/jccs.200400169openalex-snapshot
Mutational Analysis of the Yeast Nucleotide Exchange Factor Mge1p
inferred← citeshttps://doi.org/10.1002/jcp.10268openalex-snapshot
Heat shock proteins and the pancreas
inferred← citeshttps://doi.org/10.1002/jcp.20327openalex-snapshot
Electromagnetic fields at mobile phone frequency induce apoptosis and inactivation of the multi‐chaperone complex in human epidermoid cancer cells
inferred← citeshttps://doi.org/10.1002/jcp.20386openalex-snapshot
Thermotolerance induced at a mild temperature of 40°C protects cells against heat shock‐induced apoptosis
inferred← citeshttps://doi.org/10.1002/jemt.10341openalex-snapshot
Immunohistochemical study of heat shock proteins 27, 60 and 70 in the normal human adrenal and in adrenal tumors with suppressed ACTH production
inferred← citeshttps://doi.org/10.1002/jmr.707openalex-snapshot
Chaperonin function—effects of crowding and confinement
inferred← citeshttps://doi.org/10.1002/jnr.21417openalex-snapshot
Molecular chaperone‐mediated tau protein metabolism counteracts the formation of granular tau oligomers in human brain
inferred← citeshttps://doi.org/10.1002/jnr.23755openalex-snapshot
Chaperones as potential therapeutics for Krabbe disease
inferred← citeshttps://doi.org/10.1002/lsm.22268openalex-snapshot
Effects of laser treatment on the expression of cytosolic proteins in the synovium of patients with osteoarthritis
inferred← citeshttps://doi.org/10.1002/mabi.200900396openalex-snapshot
Effect of GroEL on Thermal Aggregation of Glycogen Phosphorylase b from Rabbit Skeletal Muscle
inferred← citeshttps://doi.org/10.1002/macp.202400531openalex-snapshot
Fight Aβ Aggregation with Molecular Aggregates
inferred← citeshttps://doi.org/10.1002/mc.20009openalex-snapshot
Intronic polymorphism (1541‐1542delGT) of the constitutive heat shock protein 70 gene has functional significance and shows evidence of association with lung cancer risk
inferred← citeshttps://doi.org/10.1002/mds.21013openalex-snapshot
Ubiquitin–proteasome system and Parkinson's disease
inferred← citeshttps://doi.org/10.1002/med.21807openalex-snapshot
Targeting the HSP90–CDC37–kinase chaperone cycle: A promising therapeutic strategy for cancer
inferred← citeshttps://doi.org/10.1002/micr.20115openalex-snapshot
Protein abnormality in denervated skeletal muscles from patients with brachial injury
inferred← citeshttps://doi.org/10.1002/mus.20373openalex-snapshot
Heat shock proteins and neuromuscular disease
inferred← citeshttps://doi.org/10.1002/neu.10247openalex-snapshot
Role for calcium in heat shock‐mediated synaptic thermoprotection in Drosophila larvae
inferred← citeshttps://doi.org/10.1002/neu.20105openalex-snapshot
Systematic screening and identification of antigens recognized by monoclonal antibodies raised against the developing lateral olfactory tract
inferred← citeshttps://doi.org/10.1002/pi.4671openalex-snapshot
Bioinspired single‐chain polymer nanoparticles
inferred← citeshttps://doi.org/10.1002/pmic.200300735openalex-snapshot
Effect of high concentration of Co (II) on Enterobacter liquefaciens strain C‐1: A bacterium highly resistant to heavy metals with an unknown genome.
inferred← citeshttps://doi.org/10.1002/pmic.200400818openalex-snapshot
Activation and expression of proteins during synchronous germination of aerial spores of Streptomyces granaticolor
inferred← citeshttps://doi.org/10.1002/pmic.200400951openalex-snapshot
Restoration of heat shock protein70 suppresses gastric mucosal inducible nitric oxide synthase expression induced by Helicobacter pylori
inferred← citeshttps://doi.org/10.1002/pmic.200401091openalex-snapshot
Comparative analysis of protein aggregates by blue native electrophoresis and subsequent sodium dodecyl sulfate‐polyacrylamide gel electrophoresis in a three‐dimensional geometry gel
inferred← citeshttps://doi.org/10.1002/pmic.200401215openalex-snapshot
Subproteomic analysis of metal‐interacting proteins in human B cells
inferred← citeshttps://doi.org/10.1002/pmic.200500680openalex-snapshot
Quantitative analysis of 2,3,7,8‐tetrachlorodibenzo‐ p ‐dioxin‐induced proteome alterations in 5L rat hepatoma cells using isotope‐coded protein labels
inferred← citeshttps://doi.org/10.1002/pmic.200600783openalex-snapshot
Proteome analysis of whole saliva: A new tool for rheumatic diseases – the example of Sjögren's syndrome
inferred← citeshttps://doi.org/10.1002/pmic.200700053openalex-snapshot
Denaturing and refolding of protein molecules on surfaces
inferred← citeshttps://doi.org/10.1002/pmic.200700377openalex-snapshot
Pro‐oxidative DEP chemicals induce heat shock proteins and an unfolding protein response in a bronchial epithelial cell line as determined by DIGE analysis
inferred← citeshttps://doi.org/10.1002/pmic.200800113openalex-snapshot
Intracellular signaling pathways regulating radioresistance of human prostate carcinoma cells
inferred← citeshttps://doi.org/10.1002/pmic.201100479openalex-snapshot
Proteome dynamics in primary target organ of infectious bursal disease virus
inferred← citeshttps://doi.org/10.1002/pmic.201400527openalex-snapshot
Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1002/pmic.201500503openalex-snapshot
Absolute protein quantification of the yeast chaperome under conditions of heat shock
inferred← citeshttps://doi.org/10.1002/pmic.202100196openalex-snapshot
Proteomic profiling of metformin effects in 3T3‐L1 adipocytes by SILAC‐based quantification
inferred← citeshttps://doi.org/10.1002/pro.158openalex-snapshot
Integrity of N‐ and C‐termini is important for E. coli Hsp31 chaperone activity
inferred← citeshttps://doi.org/10.1002/pro.196openalex-snapshot
Confined dynamics of a ribosome‐bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions
inferred← citeshttps://doi.org/10.1002/pro.2087openalex-snapshot
Transient interactions of a slow‐folding protein with the Hsp70 chaperone machinery
inferred← citeshttps://doi.org/10.1002/pro.2139openalex-snapshot
Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system
inferred← citeshttps://doi.org/10.1002/pro.2454openalex-snapshot
Opening and closing of a toroidal group II chaperonin revealed by a symmetry constrained elastic network model
inferred← citeshttps://doi.org/10.1002/pro.665openalex-snapshot
Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single‐ring variant SR1 of the E. coli chaperonin GroEL
inferred← citeshttps://doi.org/10.1002/prot.20689openalex-snapshot
Folding behavior of chaperonin‐mediated substrate protein
inferred← citeshttps://doi.org/10.1002/prot.21008openalex-snapshot
Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system
inferred← citeshttps://doi.org/10.1002/prot.21547openalex-snapshot
Lattice simulations of cotranslational folding of single domain proteins
inferred← citeshttps://doi.org/10.1002/prot.21575openalex-snapshot
A model study of protein nascent chain and cotranslational folding using hydrophobic‐polar residues
inferred← citeshttps://doi.org/10.1002/prot.21606openalex-snapshot
Dynamics of group II chaperonin and prefoldin probed by 13C NMR spectroscopy
inferred← citeshttps://doi.org/10.1002/prot.22122openalex-snapshot
Early stages of β2‐microglobulin aggregation and the inhibiting action of αB‐crystallin
inferred← citeshttps://doi.org/10.1002/prot.23224openalex-snapshot
Temperature‐dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9–Tim10 complex
inferred← citeshttps://doi.org/10.1002/prot.24096openalex-snapshot
Choice of synonymous codons associated with protein folding
inferred← citeshttps://doi.org/10.1002/prot.24710openalex-snapshot
Examination of polypeptide substrate specificity for E scherichia coli C lp B
inferred← citeshttps://doi.org/10.1002/prot.25051openalex-snapshot
Folding superfunnel to describe cooperative folding of interacting proteins
inferred← citeshttps://doi.org/10.1002/ps.70790openalex-snapshot
A scalable RNAi nanoparticle approach for lethal gene targeting in the German cockroach
inferred← citeshttps://doi.org/10.1002/psc.1288openalex-snapshot
Analysis of peptides and proteins in their binding to GroEL
inferred← citeshttps://doi.org/10.1002/psc.976openalex-snapshot
Functional and structural characterization of apidaecin and its N‐terminal and C‐terminal fragments
inferred← citeshttps://doi.org/10.1002/rmv.467openalex-snapshot
Current developments in viral DNA vaccines: shall they solve the unsolved?
inferred← citeshttps://doi.org/10.1002/smll.202306746openalex-snapshot
Chaperone Mimetic Strategy for Achieving Organic Room‐Temperature Phosphorescence based on Confined Supramolecular Assembly
inferred← citeshttps://doi.org/10.1002/stem.447openalex-snapshot
Decoded Calreticulin-Deficient Embryonic Stem Cell Transcriptome Resolves Latent Cardiophenotype
inferred← citeshttps://doi.org/10.1002/wnan.70059openalex-snapshot
Advances in Self‐Assembly Artificial Chaperone for Protein Folding Regulation
inferred← citeshttps://doi.org/10.1002/yea.1210openalex-snapshot
Physiological effects of unassembled chaperonin Cct subunits in the yeastSaccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1002/yea.1742openalex-snapshot
Hsp70/Hsp90 co‐chaperones are required for efficient Hsp104‐mediated elimination of the yeast [PSI+] prion but not for prion propagation
inferred← citeshttps://doi.org/10.1002/yea.3155openalex-snapshot
Luciferase NanoLuc as a reporter for gene expression and protein levels in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1006/tpbi.2002.1606openalex-snapshot
Heterogeneity of Genome and Proteome Content in Bacteria, Archaea, and Eukaryotes
inferred← citeshttps://doi.org/10.1007/0-306-48579-6_7openalex-snapshot
FtsZ folding, self-association, activation and assembly
inferred← citeshttps://doi.org/10.1007/0-387-23695-3_7openalex-snapshot
The Life Cycle of P53: A Key Target in Drug Development
inferred← citeshttps://doi.org/10.1007/0-387-25919-8_2openalex-snapshot
The Generic Nature of Protein Folding and Misfolding
inferred← citeshttps://doi.org/10.1007/0-387-25919-8_8openalex-snapshot
Chaperone Suppression of Aggregated Protein Toxicity
inferred← citeshttps://doi.org/10.1007/0-387-25919-8_9openalex-snapshot
Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones
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