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Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles
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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.2001.5245openalex-snapshot
Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne
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SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields
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EMAN: Semiautomated Software for High-Resolution Single-Particle Reconstructions
inferredcites →https://doi.org/10.1007/3-540-29717-0_5openalex-snapshot
Chaperoning of Glucocorticoid Receptors
inferredcites →https://doi.org/10.1007/s00018-004-4464-6openalex-snapshot
Hsp70 chaperones: Cellular functions and molecular mechanism
inferredcites →https://doi.org/10.1007/s13361-012-0419-6openalex-snapshot
HDX Workbench: Software for the Analysis of H/D Exchange MS Data
inferredcites →https://doi.org/10.1007/s13361-013-0669-yopenalex-snapshot
Time Window Expansion for HDX Analysis of an Intrinsically Disordered Protein
inferredcites →https://doi.org/10.1016/j.jmb.2007.02.057openalex-snapshot
A Conformational Switch in the Ligand-binding Domain Regulates the Dependence of the Glucocorticoid Receptor on Hsp90
inferredcites →https://doi.org/10.1016/j.molcel.2008.09.016openalex-snapshot
Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones
inferredcites →https://doi.org/10.1016/j.molcel.2011.04.023openalex-snapshot
Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex
inferredcites →https://doi.org/10.1016/j.molcel.2012.11.017openalex-snapshot
Uncovering a Region of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast
inferredcites →https://doi.org/10.1016/j.molcel.2014.02.003openalex-snapshot
Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
inferredcites →https://doi.org/10.1016/j.str.2008.01.021openalex-snapshot
Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90
inferredcites →https://doi.org/10.1016/s0021-9258(18)48438-4openalex-snapshot
Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events.
inferredcites →https://doi.org/10.1016/s0021-9258(19)38489-3openalex-snapshot
Mapping the HSP90 binding region of the glucocorticoid receptor.
inferredcites →https://doi.org/10.1016/s0092-8674(02)00817-6openalex-snapshot
Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition
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/s0968-0004(01)01834-5openalex-snapshot
Continuous recycling: a mechanism for modulatory signal transduction
inferredcites →https://doi.org/10.1016/s1047-8477(03)00069-8openalex-snapshot
Accurate determination of local defocus and specimen tilt in electron microscopy
inferredcites →https://doi.org/10.1017/s0033583510000314openalex-snapshot
Conformational dynamics of the molecular chaperone Hsp90
inferredcites →https://doi.org/10.1021/bi002399+openalex-snapshot
Evidence for Iterative Ratcheting of Receptor-Bound hsp70 between Its ATP and ADP Conformations during Assembly of Glucocorticoid Receptor·hsp90 Heterocomplexes
inferredcites →https://doi.org/10.1038/348166a0openalex-snapshot
Reduced levels of hsp90 compromise steroid receptor action in vivo
inferredcites →https://doi.org/10.1038/76819openalex-snapshot
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
inferredcites →https://doi.org/10.1038/emboj.2011.472openalex-snapshot
The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop
inferredcites →https://doi.org/10.1038/nature04716openalex-snapshot
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
inferredcites →https://doi.org/10.1038/nrm2918openalex-snapshot
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
inferredcites →https://doi.org/10.1038/nsmb.2006openalex-snapshot
Mechanics of Hsp70 chaperones enables differential interaction with client proteins
inferredcites →https://doi.org/10.1073/pnas.0609163103openalex-snapshot
Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain
inferredcites →https://doi.org/10.1073/pnas.1104703108openalex-snapshot
Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
inferredcites →https://doi.org/10.1074/jbc.270.13.7288openalex-snapshot
Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase
inferredcites →https://doi.org/10.1074/jbc.270.33.19307openalex-snapshot
ATP Hydrolysis Is Required for the DnaJ-dependent Activation of DnaK Chaperone for Binding to Both Native and Denatured Protein Substrates
inferredcites →https://doi.org/10.1074/jbc.271.22.12833openalex-snapshot
Reconstitution of the Steroid Receptor·hsp90 Heterocomplex Assembly System of Rabbit Reticulocyte Lysate
inferredcites →https://doi.org/10.1074/jbc.272.34.21213openalex-snapshot
Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery
inferredcites →https://doi.org/10.1074/jbc.273.13.7358openalex-snapshot
The Role of DnaJ-like Proteins in Glucocorticoid Receptor·hsp90 Heterocomplex Assembly by the Reconstituted hsp90·p60·hsp70 Foldosome Complex
inferredcites →https://doi.org/10.1074/jbc.273.49.32973openalex-snapshot
The Assembly of Progesterone Receptor-hsp90 Complexes Using Purified Proteins
inferredcites →https://doi.org/10.1074/jbc.273.52.35194openalex-snapshot
Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery
inferredcites →https://doi.org/10.1074/jbc.275.10.6894openalex-snapshot
The Hsp Organizer Protein Hop Enhances the Rate of but Is Not Essential for Glucocorticoid Receptor Folding by the Multiprotein Hsp90-based Chaperone System
inferredcites →https://doi.org/10.1074/jbc.m000434200openalex-snapshot
Stepwise Assembly of a Glucocorticoid Receptor·hsp90 Heterocomplex Resolves Two Sequential ATP-dependent Events Involving First hsp70 and Then hsp90 in Opening of the Steroid Binding Pocket
inferredcites →https://doi.org/10.1074/jbc.m110.108118openalex-snapshot
Hormone Binding and Co-regulator Binding to the Glucocorticoid Receptor are Allosterically Coupled
inferredcites →https://doi.org/10.1074/jbc.m111445200openalex-snapshot
HSP40 Binding Is the First Step in the HSP90 Chaperoning Pathway for the Progesterone Receptor
inferredcites →https://doi.org/10.1074/jbc.m305751200openalex-snapshot
Dissection of the Contribution of Individual Domains to the ATPase Mechanism of Hsp90
inferredcites →https://doi.org/10.1074/jbc.r800023200openalex-snapshot
The Hsp90 Chaperone Machinery Regulates Signaling by Modulating Ligand Binding Clefts
inferredcites →https://doi.org/10.1083/jcb.143.4.901openalex-snapshot
In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis
inferredcites →https://doi.org/10.1093/nar/gkp999openalex-snapshot
Protein Structure Initiative Material Repository: an open shared public resource of structural genomics plasmids for the biological community
inferredcites →https://doi.org/10.1110/ps.5000102openalex-snapshot
Folding and stability of the ligand‐binding domain of the glucocorticoid receptor
inferredcites →https://doi.org/10.1111/j.1742-4658.2010.07737.xopenalex-snapshot
CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70‐bound substrates
inferredcites →https://doi.org/10.1111/j.1749-6632.2009.04988.xopenalex-snapshot
Glucocorticoid Signaling in the Cell
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.1073051openalex-snapshot
Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones
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.7761857openalex-snapshot
Role of the Protein Chaperone YDJ1 in Establishing Hsp90-Mediated Signal Transduction Pathways
inferredcites →https://doi.org/10.1128/mcb.01034-06openalex-snapshot
Nucleotide-Dependent Interaction of Saccharomyces cerevisiae Hsp90 with the Cochaperone Proteins Sti1, Cpr6, and Sba1
inferredcites →https://doi.org/10.1146/annurev.physiol.69.031905.160308openalex-snapshot
Nuclear Receptor Structure: Implications for Function
inferredcites →https://doi.org/10.1210/me.10.6.705openalex-snapshot
Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
inferredcites →https://doi.org/10.1210/me.7.11.1418openalex-snapshot
Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1002/pro.4049openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/pro.4880openalex-snapshot
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Allosteric Inhibitors of Hsp70: Drugging the Second Chaperone of Tumorigenesis
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Modulation of Molecular Chaperones in Huntington’s Disease and Other Polyglutamine Disorders
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Heat Shock Proteins Accelerate the Maturation of Brain Endothelial Cell Glucocorticoid Receptor in Focal Human Drug-Resistant Epilepsy
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Exosomal Protein Biomarkers for Predicting Early Neurological Deterioration Following Intravenous Thrombolysis in Acute Ischemic Stroke
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Associations of HSP90AA2 gene polymorphisms with disease susceptibility, glucocorticoids efficacy and health-related quality of life in Chinese systemic lupus erythematosus patients
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A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand
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Direct observation of Hsp90-induced compaction in a protein chain
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CGG repeats in the human FMR1 gene regulate mRNA localization and cellular stress in developing neurons
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Mechanistic Asymmetry in Hsp90 Dimers
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Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling
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Progesterone Receptor Signaling Mechanisms
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Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90
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BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins
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Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK
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Isoform-Specific Phosphorylation in Human Hsp90β Affects Interaction with Clients and the Cochaperone Cdc37
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Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins
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Dancing with the Diva: Hsp90–Client Interactions
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Intermolecular Interactions between Hsp90 and Hsp70
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The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers
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The Proteome Folding Problem and Cellular Proteostasis
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Grp94 Works Upstream of BiP in Protein Remodeling Under Heat Stress
inferred← citeshttps://doi.org/10.1016/j.jmb.2023.168184openalex-snapshot
J-domain Proteins form Binary Complexes with Hsp90 and Ternary Complexes with Hsp90 and Hsp70
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Modification of Regulatory Tyrosine Residues Biases Human Hsp90α in its Interactions with Cochaperones and Clients
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Effects of heat stress on ovarian development and the expression of HSP genes in mice
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Effects of heat environments on depressive disorders: Neurogenesis-mediated mechanisms
inferred← citeshttps://doi.org/10.1016/j.lfs.2015.01.027openalex-snapshot
EMF radiation at 2450MHz triggers changes in the morphology and expression of heat shock proteins and glucocorticoid receptors in rat thymus
inferred← citeshttps://doi.org/10.1016/j.lfs.2022.121304openalex-snapshot
CTNNAL1 enhances glucocorticoid sensitivity in HDM-induced asthma mouse model through deactivating hsp90 signaling pathway
inferred← citeshttps://doi.org/10.1016/j.mce.2021.111277openalex-snapshot
Generalized and tissue specific glucocorticoid resistance
inferred← citeshttps://doi.org/10.1016/j.mce.2023.112047openalex-snapshot
The transportosome system as a model for the retrotransport of soluble proteins
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.02.022openalex-snapshot
Hsp90: Breaking the Symmetry
inferred← citeshttps://doi.org/10.1016/j.molcel.2016.04.005openalex-snapshot
Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37
inferred← citeshttps://doi.org/10.1016/j.molcel.2017.08.004openalex-snapshot
The Plasticity of the Hsp90 Co-chaperone System
inferred← citeshttps://doi.org/10.1016/j.molcel.2017.09.013openalex-snapshot
Picky Hsp90—Every Game with Another Mate
inferred← citeshttps://doi.org/10.1016/j.molcel.2018.03.028openalex-snapshot
Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System
inferred← citeshttps://doi.org/10.1016/j.molcel.2018.04.010openalex-snapshot
Conformational Activation of Argonaute by Distinct yet Coordinated Actions of the Hsp70 and Hsp90 Chaperone Systems
inferred← citeshttps://doi.org/10.1016/j.molcel.2019.03.026openalex-snapshot
Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.09.027openalex-snapshot
Control of Glucocorticoid Receptor Levels by PTEN Establishes a Failsafe Mechanism for Tumor Suppression
inferred← citeshttps://doi.org/10.1016/j.molcel.2021.12.031openalex-snapshot
NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems
inferred← citeshttps://doi.org/10.1016/j.molcel.2022.01.016openalex-snapshot
The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones
inferred← citeshttps://doi.org/10.1016/j.molcel.2022.03.040openalex-snapshot
There are more Hsp90 chaperone mechanisms in heaven and earth, dear reader, than are dreamt of in your philosophy
inferred← citeshttps://doi.org/10.1016/j.molcel.2025.12.002openalex-snapshot
The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle
inferred← citeshttps://doi.org/10.1016/j.pbb.2024.173916openalex-snapshot
Fluoxetine treatment reverses chronic stress-induced promotion on Fk506-binding protein 5 expression and multiple effects on glucocorticoid receptor phosphorylation in the paraventricular nucleus of mice
inferred← citeshttps://doi.org/10.1016/j.phrs.2016.07.023openalex-snapshot
Novel targets for paclitaxel nano formulations: Hopes and hypes in triple negative breast cancer
inferred← citeshttps://doi.org/10.1016/j.psj.2020.04.009openalex-snapshot
Increased serum levels of advanced glycation end products due to induced molting in hen layers trigger a proinflammatory response by peripheral blood leukocytes
inferred← citeshttps://doi.org/10.1016/j.psyneuen.2014.11.005openalex-snapshot
A role for synapsin in FKBP51 modulation of stress responsiveness: Convergent evidence from animal and human studies
inferred← citeshttps://doi.org/10.1016/j.sbi.2014.08.007openalex-snapshot
HDX-MS guided drug discovery: small molecules and biopharmaceuticals
inferred← citeshttps://doi.org/10.1016/j.sbi.2015.02.008openalex-snapshot
Non-equilibrium conformational dynamics in the function of molecular chaperones
inferred← citeshttps://doi.org/10.1016/j.steroids.2022.109094openalex-snapshot
Progestogens exhibit progestogen-, promoter- and isoform-specific effects via the progesterone receptor
inferred← citeshttps://doi.org/10.1016/j.str.2016.05.011openalex-snapshot
Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes
inferred← citeshttps://doi.org/10.1016/j.str.2018.01.016openalex-snapshot
Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System
inferred← citeshttps://doi.org/10.1016/j.supmat.2025.100116openalex-snapshot
Recent advances of supramolecular systems in precise cancer theranostics
inferred← citeshttps://doi.org/10.1016/j.tcb.2018.10.004openalex-snapshot
The Hsp70–Hsp90 Chaperone Cascade in Protein Folding
inferred← citeshttps://doi.org/10.1016/j.tcb.2022.11.002openalex-snapshot
Glucocorticoid receptor and RAS: an unexpected couple in cancer
inferred← citeshttps://doi.org/10.1016/j.theriogenology.2023.08.023openalex-snapshot
Association of glucocorticoid receptor expression with key members of the insulin signaling pathway and heat shock proteins in the bovine ovary
inferred← citeshttps://doi.org/10.1016/j.tibs.2014.12.002openalex-snapshot
Hsp90 interaction with clients
inferred← citeshttps://doi.org/10.1016/j.tibs.2016.01.003openalex-snapshot
Heat Shock Proteins Promote Cancer: It's a Protection Racket
inferred← citeshttps://doi.org/10.1016/j.tibs.2017.07.002openalex-snapshot
How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches
inferred← citeshttps://doi.org/10.1016/j.tibs.2018.12.005openalex-snapshot
Chaperone-Bound Clients: The Importance of Being Dynamic
inferred← citeshttps://doi.org/10.1016/j.toxlet.2019.11.022openalex-snapshot
Acetylation of Hsp90 reverses dexamethasone-mediated inhibition of insulin secretion
inferred← citeshttps://doi.org/10.1016/j.ttbdis.2023.102178openalex-snapshot
The diurnal salivary glands transcriptome of Dermacentor nuttalli from the first four days of blood feeding
inferred← citeshttps://doi.org/10.1016/j.virol.2020.10.013openalex-snapshot
Hsp90 is involved in pseudorabies virus virion assembly via stabilizing major capsid protein VP5
inferred← citeshttps://doi.org/10.1016/j.ygcen.2019.113355openalex-snapshot
Stress hypothesis overload: 131 hypotheses exploring the role of stress in tradeoffs, transitions, and health
inferred← citeshttps://doi.org/10.1016/j.ynstr.2021.100401openalex-snapshot
Analysis of the cerebellar molecular stress response led to first evidence of a role for FKBP51 in brain FKBP52 expression in mice and humans
inferred← citeshttps://doi.org/10.1016/s1872-2040(17)61071-5openalex-snapshot
Progress in Molecular Chaperone Regulation of Heat Shock Protein 90 and Cancer
inferred← citeshttps://doi.org/10.1021/ac5040242openalex-snapshot
Applications of Hydrogen/Deuterium Exchange MS from 2012 to 2014
inferred← citeshttps://doi.org/10.1021/acs.biochem.5b00801openalex-snapshot
Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c01342openalex-snapshot
Inhibitor Combinations Reveal Wiring of the Proteostasis Network in Prostate Cancer Cells
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.8b00825openalex-snapshot
Allosteric Modulators of HSP90 and HSP70: Dynamics Meets Function through Structure-Based Drug Design
inferred← citeshttps://doi.org/10.1021/acs.jpcb.1c00972openalex-snapshot
Diverse Native Ensembles Dictate the Differential Functional Responses of Nuclear Receptor Ligand-Binding Domains
inferred← citeshttps://doi.org/10.1021/acs.jpcb.2c03464openalex-snapshot
Conformational Dynamics and Mechanisms of Client Protein Integration into the Hsp90 Chaperone Controlled by Allosteric Interactions of Regulatory Switches: Perturbation-Based Network Approach for Mutational Profiling of the Hsp90 Binding and Allostery
inferred← citeshttps://doi.org/10.1021/acschembio.8b00454openalex-snapshot
Targeting the FKBP51/GR/Hsp90 Complex to Identify Functionally Relevant Treatments for Depression and PTSD
inferred← citeshttps://doi.org/10.1021/acsomega.2c02331openalex-snapshot
Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta
inferred← citeshttps://doi.org/10.1021/acsomega.4c08802openalex-snapshot
Chaihu Shugan San Exerts Antidepressant Effects by Regulating Glucocorticoid Metabolism in CUMS Rats and Network Pharmacology Provides Complementary Mechanistic Insights
inferred← citeshttps://doi.org/10.1038/nature20137openalex-snapshot
Alternative modes of client binding enable functional plasticity of Hsp70
inferred← citeshttps://doi.org/10.1038/nm.3776openalex-snapshot
A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease
inferred← citeshttps://doi.org/10.1038/npp.2016.87openalex-snapshot
Potential of Environmental Enrichment to Prevent Transgenerational Effects of Paternal Trauma
inferred← citeshttps://doi.org/10.1038/nsmb.2927openalex-snapshot
The Hsp90 ensemble: coordinated Hsp90–cochaperone complexes regulate diverse cellular processes
inferred← citeshttps://doi.org/10.1038/pr.2017.66openalex-snapshot
Glucocorticoid receptor expression on circulating leukocytes in healthy and asthmatic adolescents in response to exercise
inferred← citeshttps://doi.org/10.1038/s41398-020-00979-zopenalex-snapshot
Childhood trauma, suicide risk and inflammatory phenotypes of depression: insights from monocyte gene expression
inferred← citeshttps://doi.org/10.1038/s41419-018-0779-3openalex-snapshot
The Hsp70 inhibitor 2-phenylethynesulfonamide inhibits replication and carcinogenicity of Epstein–Barr virus by inhibiting the molecular chaperone function of Hsp70
inferred← citeshttps://doi.org/10.1038/s41419-023-05676-5openalex-snapshot
Melatonin-mediated FKBP4 downregulation protects against stress-induced neuronal mitochondria dysfunctions by blocking nuclear translocation of GR
inferred← citeshttps://doi.org/10.1038/s41419-026-08543-1openalex-snapshot
APOE4 exacerbates glucocorticoid stress hormone-induced tau pathology via mitochondrial dysfunction
inferred← citeshttps://doi.org/10.1038/s41467-017-00444-4openalex-snapshot
Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell
inferred← citeshttps://doi.org/10.1038/s41467-017-02711-wopenalex-snapshot
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
inferred← citeshttps://doi.org/10.1038/s41467-018-03946-xopenalex-snapshot
A switch point in the molecular chaperone Hsp90 responding to client interaction
inferred← citeshttps://doi.org/10.1038/s41467-018-07829-zopenalex-snapshot
Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
inferred← citeshttps://doi.org/10.1038/s41467-019-11594-yopenalex-snapshot
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor
inferred← citeshttps://doi.org/10.1038/s41467-020-19783-wopenalex-snapshot
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
inferred← citeshttps://doi.org/10.1038/s41467-021-24845-8openalex-snapshot
Cisplatin-mediated activation of glucocorticoid receptor induces platinum resistance via MAST1
inferred← citeshttps://doi.org/10.1038/s41467-022-31396-zopenalex-snapshot
Hsp multichaperone complex buffers pathologically modified Tau
inferred← citeshttps://doi.org/10.1038/s41467-022-32318-9openalex-snapshot
Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors
inferred← citeshttps://doi.org/10.1038/s41467-023-36598-7openalex-snapshot
Identification of global inhibitors of cellular glycosylation
inferred← citeshttps://doi.org/10.1038/s41467-024-53178-5openalex-snapshot
Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation
inferred← citeshttps://doi.org/10.1038/s41467-024-55026-yopenalex-snapshot
The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding
inferred← citeshttps://doi.org/10.1038/s41467-025-58658-wopenalex-snapshot
Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors
inferred← citeshttps://doi.org/10.1038/s41580-019-0133-3openalex-snapshot
The Hsp70 chaperone network
inferred← citeshttps://doi.org/10.1038/s41586-021-04236-1openalex-snapshot
Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism
inferred← citeshttps://doi.org/10.1038/s41586-021-04252-1openalex-snapshot
Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
inferred← citeshttps://doi.org/10.1038/s41586-026-10640-2openalex-snapshot
Structural basis for chaperone-guided assembly of RNA-induced silencing complex
inferred← citeshttps://doi.org/10.1038/s41594-018-0057-1openalex-snapshot
Mapping interactions with the chaperone network reveals factors that protect against tau aggregation
inferred← citeshttps://doi.org/10.1038/s41594-023-01098-1openalex-snapshot
Large-scale, in-cell photocrosslinking at single-residue resolution reveals the molecular basis for glucocorticoid receptor regulation by immunophilins
inferred← citeshttps://doi.org/10.1038/s41594-023-01128-yopenalex-snapshot
Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor
inferred← citeshttps://doi.org/10.1038/s41594-024-01337-zopenalex-snapshot
Structural basis for the dynamic chaperoning of disordered clients by Hsp90
inferred← citeshttps://doi.org/10.1038/s41594-025-01619-0openalex-snapshot
Conformational plasticity of a BiP–GRP94 chaperone complex
inferred← citeshttps://doi.org/10.1038/s41598-017-01666-8openalex-snapshot
Placental O-GlcNAc-transferase expression and interactions with the glucocorticoid receptor are sex specific and regulated by maternal corticosterone exposure in mice
inferred← citeshttps://doi.org/10.1038/s41598-017-07565-2openalex-snapshot
A high-throughput chemical screen identifies novel inhibitors and enhancers of anti-inflammatory functions of the glucocorticoid receptor
inferred← citeshttps://doi.org/10.1038/s41598-017-18650-xopenalex-snapshot
Determining direct binders of the Androgen Receptor using a high-throughput Cellular Thermal Shift Assay
inferred← citeshttps://doi.org/10.1038/s41598-018-21210-6openalex-snapshot
Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes
inferred← citeshttps://doi.org/10.1038/s41598-018-25393-wopenalex-snapshot
Relationship Between Homodimeric Glucocorticoid Receptor and Transcriptional Regulation Assessed via an In Vitro Fluorescence Correlation Spectroscopy-Microwell System
inferred← citeshttps://doi.org/10.1038/s41598-019-48109-0openalex-snapshot
head-bent resistant Hsc70 variants show reduced Hsp40 affinity and altered protein folding activity
inferred← citeshttps://doi.org/10.1038/s41598-020-67645-8openalex-snapshot
Glucocorticoid receptor complexes form cooperatively with the Hsp90 co-chaperones Pp5 and FKBPs
inferred← citeshttps://doi.org/10.1038/s41598-021-00885-4openalex-snapshot
Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90
inferred← citeshttps://doi.org/10.1038/s41598-021-91107-4openalex-snapshot
Ipomoeassin-F disrupts multiple aspects of secretory protein biogenesis
inferred← citeshttps://doi.org/10.1038/s41598-021-92039-9openalex-snapshot
Glucocorticoid resistance conferring mutation in the C-terminus of GR alters the receptor conformational dynamics
inferred← citeshttps://doi.org/10.1038/s41598-023-43368-4openalex-snapshot
Single-cell transcriptomics delineates the immune cell landscape in equine lower airways and reveals upregulation of FKBP5 in horses with asthma
inferred← citeshttps://doi.org/10.1038/s41598-025-88780-0openalex-snapshot
Early-life environmental enrichment promotes positive animal welfare for juvenile Atlantic salmon (Salmo salar) in aquaculture research
inferred← citeshttps://doi.org/10.1038/s44321-026-00423-7openalex-snapshot
TMPRSS2-ERG confers resistance of prostate cancer to antiandrogens
inferred← citeshttps://doi.org/10.1038/srep23830openalex-snapshot
Molecular Dynamics Simulations Reveal the Mechanisms of Allosteric Activation of Hsp90 by Designed Ligands
inferred← citeshttps://doi.org/10.1038/srep42110openalex-snapshot
Blubber transcriptome response to acute stress axis activation involves transient changes in adipogenesis and lipolysis in a fasting-adapted marine mammal
inferred← citeshttps://doi.org/10.1038/tp.2017.32openalex-snapshot
Integrated transcriptome and methylome analysis in youth at high risk for bipolar disorder: a preliminary analysis
inferred← citeshttps://doi.org/10.1039/bk9781839165986-00278openalex-snapshot
Probing Single Chaperone Substrates
inferred← citeshttps://doi.org/10.1042/bcj20170380openalex-snapshot
Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines
inferred← citeshttps://doi.org/10.1042/bsr20200079openalex-snapshot
2-phenylethynesulfonamide inhibits growth of oral squamous cell carcinoma cells by blocking the function of heat shock protein 70
inferred← citeshttps://doi.org/10.1073/pnas.1508504112openalex-snapshot
Mapping the conformation of a client protein through the Hsp70 functional cycle
inferred← citeshttps://doi.org/10.1073/pnas.1516167113openalex-snapshot
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate
inferred← citeshttps://doi.org/10.1073/pnas.1719969115openalex-snapshot
Functional and physical interaction between yeast Hsp90 and Hsp70
inferred← citeshttps://doi.org/10.1073/pnas.1807618115openalex-snapshot
Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor
inferred← citeshttps://doi.org/10.1073/pnas.1903936116openalex-snapshot
The Hsp70 chaperone is a major player in stress-induced transposable element activation
inferred← citeshttps://doi.org/10.1073/pnas.2118793119openalex-snapshot
The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94
inferred← citeshttps://doi.org/10.1073/pnas.2119076119openalex-snapshot
Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments
inferred← citeshttps://doi.org/10.1073/pnas.2309326121openalex-snapshot
Structural transitions modulate the chaperone activities of Grp94
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