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Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
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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
inferredcites →https://doi.org/10.1016/j.bmcl.2005.05.046openalex-snapshot
The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors
inferredcites →https://doi.org/10.1016/j.canlet.2003.08.032openalex-snapshot
Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone
inferredcites →https://doi.org/10.1016/j.chembiol.2004.03.033openalex-snapshot
Structure-Activity Relationships in Purine-Based Inhibitor Binding to HSP90 Isoforms
inferredcites →https://doi.org/10.1016/j.gde.2004.12.011openalex-snapshot
Hsp90 and Cdc37 – a chaperone cancer conspiracy
inferredcites →https://doi.org/10.1016/j.jmb.2004.05.007openalex-snapshot
Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90
inferredcites →https://doi.org/10.1016/j.jmb.2004.07.064openalex-snapshot
The Co-chaperone Sba1 Connects the ATPase Reaction of Hsp90 to the Progression of the Chaperone Cycle
inferredcites →https://doi.org/10.1016/j.jmb.2004.09.055openalex-snapshot
Independent ATPase Activity of Hsp90 Subunits Creates a Flexible Assembly Platform
inferredcites →https://doi.org/10.1016/j.str.2004.03.020openalex-snapshot
The Crystal Structure of the Carboxy-Terminal Dimerization Domain of htpG, the Escherichia coli Hsp90, Reveals a Potential Substrate Binding Site
inferredcites →https://doi.org/10.1016/j.str.2004.12.018openalex-snapshot
Structures of the N-Terminal and Middle Domains of E. coli Hsp90 and Conformation Changes upon ADP Binding
inferredcites →https://doi.org/10.1016/s0092-8674(00)80203-2openalex-snapshot
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent
inferredcites →https://doi.org/10.1016/s0092-8674(00)80314-1openalex-snapshot
Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone
inferredcites →https://doi.org/10.1016/s0092-8674(00)80717-5openalex-snapshot
Transformation of MutL by ATP Binding and Hydrolysis
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(03)01027-4openalex-snapshot
The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37
inferredcites →https://doi.org/10.1016/s1043-2760(98)00059-9openalex-snapshot
Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor–hsp90 Heterocomplex Assembly
inferredcites →https://doi.org/10.1016/s1097-2765(02)00785-2openalex-snapshot
Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1
inferredcites →https://doi.org/10.1016/s1097-2765(03)00065-0openalex-snapshot
Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions
inferredcites →https://doi.org/10.1021/jm980403yopenalex-snapshot
Structural Basis for Inhibition of the Hsp90 Molecular Chaperone by the Antitumor Antibiotics Radicicol and Geldanamycin
inferredcites →https://doi.org/10.1038/351624a0openalex-snapshot
Crystal structure of an N-terminal fragment of the DNA gyrase B protein
inferredcites →https://doi.org/10.1038/nsb0697-477openalex-snapshot
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
inferredcites →https://doi.org/10.1038/sj.emboj.7600060openalex-snapshot
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
inferredcites →https://doi.org/10.1038/sj.emboj.7600141openalex-snapshot
Erratum: Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
inferredcites →https://doi.org/10.1042/bj20041283openalex-snapshot
Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation
inferredcites →https://doi.org/10.1073/pnas.220430297openalex-snapshot
Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90
inferredcites →https://doi.org/10.1073/pnas.90.23.11424openalex-snapshot
Isolation of Hsp90 mutants by screening for decreased steroid receptor function.
inferredcites →https://doi.org/10.1073/pnas.93.24.13937openalex-snapshot
Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast
inferredcites →https://doi.org/10.1073/pnas.93.25.14536openalex-snapshot
Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90
inferredcites →https://doi.org/10.1074/jbc.271.37.22796openalex-snapshot
Polyubiquitination and Proteasomal Degradation of the p185c-B-2 Receptor Protein-tyrosine Kinase Induced by Geldanamycin
inferredcites →https://doi.org/10.1074/jbc.272.12.8007openalex-snapshot
Nucleotides and Two Functional States of hsp90
inferredcites →https://doi.org/10.1074/jbc.m003410200openalex-snapshot
Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone
inferredcites →https://doi.org/10.1074/jbc.m201287200openalex-snapshot
Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50
inferredcites →https://doi.org/10.1074/jbc.m208457200openalex-snapshot
N-terminal Residues Regulate the Catalytic Efficiency of the Hsp90 ATPase Cycle
inferredcites →https://doi.org/10.1074/jbc.m212761200openalex-snapshot
Aha1 Binds to the Middle Domain of Hsp90, Contributes to Client Protein Activation, and Stimulates the ATPase Activity of the Molecular Chaperone
inferredcites →https://doi.org/10.1074/jbc.m305960200openalex-snapshot
Genetic Dissection of p23, an Hsp90 Cochaperone, Reveals a Distinct Surface Involved in Estrogen Receptor Signaling
inferredcites →https://doi.org/10.1074/jbc.m405253200openalex-snapshot
Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone
inferredcites →https://doi.org/10.1074/jbc.m410562200openalex-snapshot
Co-chaperone Regulation of Conformational Switching in the Hsp90 ATPase Cycle
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/emboj/17.16.4829openalex-snapshot
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
inferredcites →https://doi.org/10.1093/emboj/18.3.754openalex-snapshot
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)‐domain co‐chaperones
inferredcites →https://doi.org/10.1093/emboj/19.16.4383openalex-snapshot
The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains
inferredcites →https://doi.org/10.1093/emboj/19.21.5930openalex-snapshot
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23
inferredcites →https://doi.org/10.1128/mcb.15.7.3917openalex-snapshot
Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
inferredcites →https://doi.org/10.1128/mcb.18.7.3727openalex-snapshot
SBA1 Encodes a Yeast Hsp90 Cochaperone That Is Homologous to Vertebrate p23 Proteins
inferredcites →https://doi.org/10.1210/me.9.6.670openalex-snapshot
Binding of p23 and hsp90 during assembly with the progesterone receptor
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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SENP1‐Mediated HSP90ab1 DeSUMOylation in Cardiomyocytes Prevents Myocardial Fibrosis by Paracrine Signaling
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ATP Hydrolysis by α‐Synuclein Amyloids is Mediated by Enclosing β‐Strand
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Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies
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Co(II), Ni(II), and Zn(II) complexes of 5‐methyl‐1,3,4‐oxadiazol‐2‐amine Schiff base as potential heat shock protein 90 inhibitors: Spectroscopic, biological activity, density functional theory, and molecular docking studies
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Hsp90 and co‐chaperones twist the functions of diverse client proteins
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ATP‐driven molecular chaperone machines
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Review: The HSP90 molecular chaperone—an enigmatic ATPase
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The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90
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Targeting the Hsp90 Chaperone: Synthesis of Novel Resorcylic Acid Macrolactone Inhibitors of Hsp90
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Inhibition of Hsp90 with Resorcylic Acid Macrolactones: Synthesis and Binding Studies
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Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands
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Identification of Limonol Derivatives as Heat Shock Protein 90 (Hsp90) Inhibitors through a Multidisciplinary Approach
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A Convergent Approach to Resorcinolic Macrolides to Expand Structural Diversity
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Hsp90 as a Target for Drug Development
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Structure‐Based and in silico Design of Hsp90 Inhibitors
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The Prospect of FKBP51 as a Drug Target
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Effects of Inhibitors on Hsp90′s Conformational Dynamics, Cochaperone and Client Interactions
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From Natural Compounds to Bioactive Molecules through NMR and In Silico Methodologies
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Chemical and Biophysical Approaches to Allosteric Modulation
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Computational Studies of Allosteric Regulation in the Hsp90 Molecular Chaperone: From Functional Dynamics and Protein Structure Networks to Allosteric Communications and Targeted Anti‐Cancer Modulators
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Inhibition of HSP90α protects cultured neurons from oxygen‐glucose deprivation induced necroptosis by decreasing RIP3 expression
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Potentiation of chemotherapeutics by the Hsp90 antagonist geldanamycin requires a steady serum condition
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Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities
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Targeting the HSP90–CDC37–kinase chaperone cycle: A promising therapeutic strategy for cancer
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An integrative proteome analysis of different seedling organs in tolerant and sensitive wheat cultivars under drought stress and recovery
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Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide
inferred← citeshttps://doi.org/10.1002/pro.2103openalex-snapshot
The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis
inferred← citeshttps://doi.org/10.1002/pro.282openalex-snapshot
Osmolyte‐induced conformational changes in the Hsp90 molecular chaperone
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The chaperone toolbox at the single‐molecule level: From clamping to confining
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Pan‐HSP90 ligand binding reveals isoform‐specific differences in plasticity and water networks
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Molecular mechanisms of chaperone‐directed protein folding: Insights from atomistic simulations
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Ordered ATP hydrolysis in the Hsp90 chaperone is regulated by Aha1 and a conserved post‐translational modification
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Ligand‐driven modulation of chaperone–cochaperone networks shapes proteostasis outcomes
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Unperturbed hydration structure involves ADP recognition in the N‐terminal domain of human heat shock protein 90α
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A Novel Class of Hsp90 C-Terminal Modulators Have Pre-Clinical Efficacy in Prostate Tumor Cells Without Induction of a Heat Shock Response
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Structure of the ATP‐binding domain of Plasmodium falciparum Hsp90
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Computational Elucidation of Possible Contributors to Formation and Stabilization of ATP ‐Lid Down‐Conformation in the N‐Terminal Domain of Hsp90
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Molecular dynamics analyses of the dissociation process of ADP from Hsp90
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Targeting Hsp90 Function to Treat Cancer: Much More to Be Learned
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Drugging the Hsp90 molecular chaperone machine for cancer treatment
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Cdc37 and protein kinase folding
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HSP90 Inhibition as an Anticancer Strategy: Novel Approaches and Future Directions
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The Interaction Networks of Hsp70 and Hsp90 in the Plasmodium and Leishmania Parasites
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The Interaction Network of the Hsp90 Molecular Chaperone
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The Candida albicans Hsp90 Chaperone Network Is Environmentally Flexible and Evolutionarily Divergent
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Emergence and Characterization of the p23 Molecular Chaperone
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Bacterial Hsp90 ATPase Assays
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Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding
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Hsp90 and Client Protein Maturation
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The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function
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Hsp90 and Its Role in Heme-Maturation of Client Proteins: Implications for Human Diseases
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Functions of SGT1, a Co-chaperone
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Sti1/Hop Plays a Pivotal Role in Hsp90 Regulation Beyond Bridging Hsp70
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HSP90-Based Heterocomplex as Essential Regulator for Cancer Disease
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Role of Hsp90 Interacting Molecular Chaperones on Tau and Aß Processing in Alzheimer’s Disease
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General Structural and Functional Features of Molecular Chaperones
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Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity
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CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome
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HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease
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p23 and Aha1: Distinct Functions Promote Client Maturation
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Effects of Anthropogenic Chemicals on Hermatypic Corals with Special Reference to Gene Expression
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CHIP: A Co-chaperone for Degradation by the Proteasome
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“Tuning” the ATPase Activity of Hsp90
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Molecular Chaperones and HSPs in Sugarcane and Eucalyptus
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Molecular Chaperones: Structure-Function Relationship and their Role in Protein Folding
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General Structural and Functional Features of Molecular Chaperones
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Chaperones and Proteases of Plasmodium falciparum
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Role of Heat Shock Protein 90 in Diabetes and Pancreatic Cancer Management
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Small-Molecule Inhibitors of Protein–Protein Interactions as Therapeutics
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Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90
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The Hsp70–Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration
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The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response
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Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones
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S100A6 mediates nuclear translocation of Sgt1: a heat shock-regulated protein
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HSP90 and the cancer transcriptome: a comprehensive review of inhibitors and mechanistic insights
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Improved delivery of Mcl-1 and survivin siRNA combination in breast cancer cells with additive siRNA complexes
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The chaperone system in cancer therapies: Hsp90
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NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13C-methyl alanine
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Molecular chaperones and their denaturing effect on client proteins
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Recent progress in the development of HSP90 inhibitors: structure–activity relationship and biological evaluation studies
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The Potential of Targeting P53 and HSP90 Overcoming Acquired MAPKi-Resistant Melanoma
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Mechanism of Inhibition of Hsp90 Dimerization by Gyrase B Inhibitor Coumermycin A1 (C–A1) Revealed by Molecular Dynamics Simulations and Thermodynamic Calculations
inferred← citeshttps://doi.org/10.1007/s12038-007-0052-xopenalex-snapshot
Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: molecular modelling approach to rational drug design against malaria
inferred← citeshttps://doi.org/10.1007/s12192-008-0058-9openalex-snapshot
Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
inferred← citeshttps://doi.org/10.1007/s12192-009-0115-zopenalex-snapshot
Novel Hsp90 partners discovered using complementary proteomic approaches
inferred← citeshttps://doi.org/10.1007/s12192-010-0182-1openalex-snapshot
Characterization of plant p23-like proteins for their co-chaperone activities
inferred← citeshttps://doi.org/10.1007/s12192-011-0299-xopenalex-snapshot
Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
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Studying heat shock proteins through single-molecule mechanical manipulation
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Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions
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Combination therapy involving HSP90 inhibitors for combating cancer: an overview of clinical and preclinical progress
inferred← citeshttps://doi.org/10.1007/s12551-016-0194-xopenalex-snapshot
A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
inferred← citeshttps://doi.org/10.1007/s12551-023-01127-9openalex-snapshot
The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly
inferred← citeshttps://doi.org/10.1007/s13361-015-1290-zopenalex-snapshot
Characterization of the Saccharomyces cerevisiae ATP-Interactome using the iTRAQ-SPROX Technique
inferred← citeshttps://doi.org/10.1007/s13361-016-1457-2openalex-snapshot
Thermodynamic Analysis of the Geldanamycin–Hsp90 Interaction in a Whole Cell Lysate Using a Mass Spectrometry-Based Proteomics Approach
inferred← citeshttps://doi.org/10.1007/s13762-026-07295-xopenalex-snapshot
Multi-level toxicity assessment of sub-lethal mercury exposure in Clarias batrachus
inferred← citeshttps://doi.org/10.1007/s40242-026-6078-0openalex-snapshot
Disease-anchored Network Analysis and Molecular Dynamics Prioritize HSP90AB1 as a Doxorubicin-binding Hub Across Cancers
inferred← citeshttps://doi.org/10.1007/s42485-026-00209-yopenalex-snapshot
Nutrient-driven regulation of the heat shock response: implications for proteostasis and cellular homeostasis
inferred← citeshttps://doi.org/10.1016/b978-0-08-100098-4.00002-8openalex-snapshot
Structure-Based Ligand Design I
inferred← citeshttps://doi.org/10.1016/b978-0-12-374920-8.00313-1openalex-snapshot
3.10 Chaperones and Protein Folding
inferred← citeshttps://doi.org/10.1016/b978-0-12-394387-3.00007-0openalex-snapshot
HDAC Inhibitors and Chaperone Function
inferred← citeshttps://doi.org/10.1016/b978-0-12-396521-9.00009-7openalex-snapshot
Exploiting Cancer Dependence on Molecular Chaperones
inferred← citeshttps://doi.org/10.1016/b978-0-12-397927-8.00015-4openalex-snapshot
HSP90 Inhibitors for Cancer Therapy and Overcoming Drug Resistance
inferred← citeshttps://doi.org/10.1016/b978-0-12-803699-0.00020-7openalex-snapshot
Protein Structure and Folding
inferred← citeshttps://doi.org/10.1016/b978-0-12-811913-6.00003-5openalex-snapshot
Phosphorylation and Acetylation of Proteins as Posttranslational Modification: Implications in Human Health and Associated Diseases
inferred← citeshttps://doi.org/10.1016/b978-0-12-818549-0.00016-9openalex-snapshot
Miscellaneous small- molecule and biological approaches to targeted cancer therapy
inferred← citeshttps://doi.org/10.1016/b978-0-12-821430-5.00023-7openalex-snapshot
Molecular chaperones, proteases, and unfolded protein responses
inferred← citeshttps://doi.org/10.1016/b978-0-444-52824-7.00009-3openalex-snapshot
Drugs That Inhibit Signalling Pathways for Tumor Cell Growth and Proliferation
inferred← citeshttps://doi.org/10.1016/b978-0-444-62649-3.00011-9openalex-snapshot
Other Nonbiological Approaches to Targeted Cancer Chemotherapy
inferred← citeshttps://doi.org/10.1016/b978-012369448-5.50016-1openalex-snapshot
HSP90 inhibitors: targeting the cancer chaperone for combinatorial blockade of oncogenic pathways
inferred← citeshttps://doi.org/10.1016/bs.acc.2024.04.002openalex-snapshot
Proteostasis in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1016/bs.acr.2015.12.001openalex-snapshot
Anticancer Inhibitors of Hsp90 Function
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2018.09.003openalex-snapshot
Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2018.10.001openalex-snapshot
Functional principles and regulation of molecular chaperones
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2025.08.013openalex-snapshot
Proteostasis and pathogenesis: Unraveling the complexity of protein misfolding disorders
inferred← citeshttps://doi.org/10.1016/bs.armc.2018.08.005openalex-snapshot
X-ray Crystallography Contributions to Drug Discovery Against Parasite
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.08.024openalex-snapshot
A Multicolor Single-Molecule FRET Approach to Study Protein Dynamics and Interactions Simultaneously
inferred← citeshttps://doi.org/10.1016/bs.mie.2021.01.040openalex-snapshot
Characteristics of Gd(III) spin labels for the study of protein conformations
inferred← citeshttps://doi.org/10.1016/j.ab.2013.03.026openalex-snapshot
Functional characterization of heat shock protein 90 targeted compounds
inferred← citeshttps://doi.org/10.1016/j.ab.2025.115903openalex-snapshot
Influence of experimental conditions on the adsorption of disease biomarker proteins to InP/ZnS quantum dots
inferred← citeshttps://doi.org/10.1016/j.abb.2008.02.035openalex-snapshot
Photophysical properties of popular fluorescent adenosine nucleotide analogs used in enzyme mechanism probing
inferred← citeshttps://doi.org/10.1016/j.abb.2011.06.015openalex-snapshot
Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90kDa heat shock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70
inferred← citeshttps://doi.org/10.1016/j.abb.2014.10.015openalex-snapshot
The C-terminal region of the human p23 chaperone modulates its structure and function
inferred← citeshttps://doi.org/10.1016/j.abb.2023.109599openalex-snapshot
Despite their structural similarities, the cytosolic isoforms of human Hsp90 show different behaviour in thermal unfolding due to their conformation: An FTIR study
inferred← citeshttps://doi.org/10.1016/j.antiviral.2013.12.010openalex-snapshot
Chikungunya virus nsP3 & nsP4 interacts with HSP-90 to promote virus replication: HSP-90 inhibitors reduce CHIKV infection and inflammation in vivo
inferred← citeshttps://doi.org/10.1016/j.apsb.2020.01.018openalex-snapshot
Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery
inferred← citeshttps://doi.org/10.1016/j.apsb.2020.11.015openalex-snapshot
The disruption of protein−protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition
inferred← citeshttps://doi.org/10.1016/j.arr.2016.09.004openalex-snapshot
Targeting chaperones, heat shock factor-1, and unfolded protein response: Promising therapeutic approaches for neurodegenerative disorders
inferred← citeshttps://doi.org/10.1016/j.bbagen.2015.05.002openalex-snapshot
Macromolecular crowding: Macromolecules friend or foe
inferred← citeshttps://doi.org/10.1016/j.bbagen.2017.05.006openalex-snapshot
Targeting the Hsp90 C-terminal domain to induce allosteric inhibition and selective client downregulation
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2013.02.010openalex-snapshot
Regulation of molecular chaperones through post-translational modifications: Decrypting the chaperone code
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.03.002openalex-snapshot
Mutations that increase both Hsp90 ATPase activity in vitro and Hsp90 drug resistance in vivo
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.07.018openalex-snapshot
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.07.020openalex-snapshot
The ‘active life’ of Hsp90 complexes
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.09.003openalex-snapshot
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.09.016openalex-snapshot
The HSP90 complex of plants
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.09.020openalex-snapshot
Evolution and function of diverse Hsp90 homologs and cochaperone proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.11.009openalex-snapshot
Hsp90 structure and function studied by NMR spectroscopy
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.03.014openalex-snapshot
Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2018.03.008openalex-snapshot
Regulation of the Hsp90 system
inferred← citeshttps://doi.org/10.1016/j.bbamem.2008.02.012openalex-snapshot
Membrane-associated stress proteins: More than simply chaperones
inferred← citeshttps://doi.org/10.1016/j.bbamem.2018.11.009openalex-snapshot
Interaction of Hsp90AA1 with phospholipids stabilizes membranes under stress conditions
inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.08.004openalex-snapshot
Structural and functional studies of Leishmania braziliensis Hsp90
inferred← citeshttps://doi.org/10.1016/j.bbapap.2015.07.003openalex-snapshot
Hsp90 oligomerization process: How can p23 drive the chaperone machineries?
inferred← citeshttps://doi.org/10.1016/j.bbapap.2018.04.008openalex-snapshot
Dynamics-based community analysis and perturbation response scanning of allosteric interaction networks in the TRAP1 chaperone structures dissect molecular linkage between conformational asymmetry and sequential ATP hydrolysis
inferred← citeshttps://doi.org/10.1016/j.bbapap.2021.140719openalex-snapshot
Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70)
inferred← citeshttps://doi.org/10.1016/j.bcp.2010.01.031openalex-snapshot
A simple yeast-based system for analyzing inhibitor resistance in the human cancer drug targets Hsp90α/β
inferred← citeshttps://doi.org/10.1016/j.bcp.2010.07.030openalex-snapshot
Modulation of cell sensitivity to antitumor agents by targeting survival pathways
inferred← citeshttps://doi.org/10.1016/j.bcp.2019.03.012openalex-snapshot
Penicisulfuranol A, a novel C-terminal inhibitor disrupting molecular chaperone function of Hsp90 independent of ATP binding domain
inferred← citeshttps://doi.org/10.1016/j.bcp.2020.114218openalex-snapshot
Fungal mycotoxin penisuloxazin A, a novel C-terminal Hsp90 inhibitor and characteristics of its analogues on Hsp90 function related to binding sites
inferred← citeshttps://doi.org/10.1016/j.bcp.2022.115376openalex-snapshot
Dipyridamole interacts with the N-terminal domain of HSP90 and antagonizes the function of the chaperone in multiple cancer cell lines
inferred← citeshttps://doi.org/10.1016/j.biochi.2016.05.018openalex-snapshot
Hsp90: Friends, clients and natural foes
inferred← citeshttps://doi.org/10.1016/j.biomaterials.2021.120817openalex-snapshot
Targeted delivery of heat shock protein 90 inhibitors prevents growth of HER2-positive tumor
inferred← citeshttps://doi.org/10.1016/j.bioorg.2023.106721openalex-snapshot
Small-molecule dual inhibitors targeting heat shock protein 90 for cancer targeted therapy
inferred← citeshttps://doi.org/10.1016/j.bioorg.2025.108782openalex-snapshot
Recent advances in HSP90 inhibitors as targeted cancer therapy: Chemical scaffolds, isoform selectivity, and clinical progress
inferred← citeshttps://doi.org/10.1016/j.bmc.2008.04.070openalex-snapshot
Synthesis of Hsp90 inhibitor dimers as potential antitumor agents
inferred← citeshttps://doi.org/10.1016/j.bmc.2010.05.075openalex-snapshot
Efficient synthesis of Hsp90 inhibitor dimers as potential antitumor agents
inferred← citeshttps://doi.org/10.1016/j.bmc.2010.07.042openalex-snapshot
Design and synthesis of Hsp90 inhibitors: Exploring the SAR of Sansalvamide A derivatives
inferred← citeshttps://doi.org/10.1016/j.bmc.2012.03.043openalex-snapshot
A highly selective Hsp90 affinity chromatography resin with a cleavable linker
inferred← citeshttps://doi.org/10.1016/j.bmc.2014.06.006openalex-snapshot
Potential C-terminal-domain inhibitors of heat shock protein 90 derived from a C-terminal peptide helix
inferred← citeshttps://doi.org/10.1016/j.bmc.2019.115080openalex-snapshot
C-terminal modulators of heat shock protein of 90 kDa (HSP90): State of development and modes of action
inferred← citeshttps://doi.org/10.1016/j.bmcl.2020.127303openalex-snapshot
Synthesis of paramagnetic ligands that target the C-terminal binding site of Hsp90
inferred← citeshttps://doi.org/10.1016/j.bmcl.2022.129111openalex-snapshot
Recent advances toward the development of Hsp90 C-terminal inhibitors
inferred← citeshttps://doi.org/10.1016/j.bpj.2012.06.018openalex-snapshot
Molecular and Thermodynamic Insights into the Conformational Transitions of Hsp90
inferred← citeshttps://doi.org/10.1016/j.bpj.2012.09.008openalex-snapshot
Force Distribution Reveals Signal Transduction in E. coli Hsp90
inferred← citeshttps://doi.org/10.1016/j.bpj.2012.11.2162openalex-snapshot
Structural Basis for Ternary Complex Formation between Tau, Hsp90, and FKBP51
inferred← citeshttps://doi.org/10.1016/j.bpj.2016.08.023openalex-snapshot
Single-Molecule Analysis beyond Dwell Times: Demonstration and Assessment in and out of Equilibrium
inferred← citeshttps://doi.org/10.1016/j.bpj.2017.08.032openalex-snapshot
Cooperative Nucleotide Binding in Hsp90 and Its Regulation by Aha1
inferred← citeshttps://doi.org/10.1016/j.bpj.2023.07.020openalex-snapshot
Aha1 regulates Hsp90’s conformation and function in a stoichiometry-dependent way
inferred← citeshttps://doi.org/10.1016/j.bpj.2023.12.005openalex-snapshot
C-terminal domain dimerization in yeast Hsp90 is moderately modulated by the other domains
inferred← citeshttps://doi.org/10.1016/j.canlet.2009.07.010openalex-snapshot
Geldanamycin and its anti-cancer activities
inferred← citeshttps://doi.org/10.1016/j.canlet.2014.05.014openalex-snapshot
SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation
inferred← citeshttps://doi.org/10.1016/j.cell.2006.09.027openalex-snapshot
Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements
inferred← citeshttps://doi.org/10.1016/j.cell.2012.05.036openalex-snapshot
Systematic Functional Prioritization of Protein Posttranslational Modifications
inferred← citeshttps://doi.org/10.1016/j.cell.2014.01.037openalex-snapshot
Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action
inferred← citeshttps://doi.org/10.1016/j.cell.2014.04.038openalex-snapshot
Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles
inferred← citeshttps://doi.org/10.1016/j.cell.2019.08.020openalex-snapshot
A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity
inferred← citeshttps://doi.org/10.1016/j.cellsig.2016.07.003openalex-snapshot
Extracellular heat shock protein 90 binding to TGFβ receptor I participates in TGFβ-mediated collagen production in myocardial fibroblasts
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