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Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0061(199608)12:10<943::aid-yea997>3.0.co;2-3openalex-snapshot
Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth
inferredcites →https://doi.org/10.1002/1097-0061(20000630)16:9<857::aid-yea561>3.0.co;2-bopenalex-snapshot
Rapid and reliable protein extraction from yeast
inferredcites →https://doi.org/10.1002/mabi.201000075openalex-snapshot
SEDVIEW, Real‐time Sedimentation Analysis
inferredcites →https://doi.org/10.1002/yea.1142openalex-snapshot
A versatile toolbox for PCR‐based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
inferredcites →https://doi.org/10.1007/978-1-4939-7477-1_28openalex-snapshot
Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding
inferredcites →https://doi.org/10.1007/s00294-014-0432-3openalex-snapshot
Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones
inferredcites →https://doi.org/10.1007/s12192-008-0058-9openalex-snapshot
Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
inferredcites →https://doi.org/10.1016/b978-0-12-420070-8.00005-2openalex-snapshot
In Vivo [35 S]-Methionine Incorporation
inferredcites →https://doi.org/10.1016/j.bbamcr.2011.09.003openalex-snapshot
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
inferredcites →https://doi.org/10.1016/j.bbamcr.2011.09.020openalex-snapshot
Evolution and function of diverse Hsp90 homologs and cochaperone proteins
inferredcites →https://doi.org/10.1016/j.bcp.2004.06.024openalex-snapshot
Using yeast to screen for inhibitors of protein tyrosine phosphatase 1B
inferredcites →https://doi.org/10.1016/j.cell.2004.12.024openalex-snapshot
Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone
inferredcites →https://doi.org/10.1016/j.cell.2005.08.031openalex-snapshot
Exploration of the Function and Organization of the Yeast Early Secretory Pathway through an Epistatic Miniarray Profile
inferredcites →https://doi.org/10.1016/j.cell.2006.09.027openalex-snapshot
Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements
inferredcites →https://doi.org/10.1016/j.cell.2006.09.043openalex-snapshot
Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
inferredcites →https://doi.org/10.1016/j.cell.2007.07.036openalex-snapshot
Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches
inferredcites →https://doi.org/10.1016/j.cell.2012.06.047openalex-snapshot
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
inferredcites →https://doi.org/10.1016/j.cell.2014.04.038openalex-snapshot
Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles
inferredcites →https://doi.org/10.1016/j.celrep.2015.07.004openalex-snapshot
c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells
inferredcites →https://doi.org/10.1016/j.celrep.2017.08.074openalex-snapshot
Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping
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.2005.11.085openalex-snapshot
The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins
inferredcites →https://doi.org/10.1016/j.jmb.2018.05.026openalex-snapshot
Dancing with the Diva: Hsp90–Client Interactions
inferredcites →https://doi.org/10.1016/j.molcel.2010.01.006openalex-snapshot
Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1
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.molcel.2016.04.005openalex-snapshot
Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37
inferredcites →https://doi.org/10.1016/j.molcel.2016.09.040openalex-snapshot
Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler
inferredcites →https://doi.org/10.1016/j.molcel.2017.08.004openalex-snapshot
The Plasticity of the Hsp90 Co-chaperone System
inferredcites →https://doi.org/10.1016/j.molcel.2018.03.028openalex-snapshot
Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System
inferredcites →https://doi.org/10.1016/j.molcel.2019.02.011openalex-snapshot
The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2
inferredcites →https://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
inferredcites →https://doi.org/10.1016/j.molcel.2019.03.032openalex-snapshot
Hsp70- and Hsp90-Mediated Regulation of the Conformation of p53 DNA Binding Domain and p53 Cancer Variants
inferredcites →https://doi.org/10.1016/j.tem.2011.08.001openalex-snapshot
FKBP51 and FKBP52 in signaling and disease
inferredcites →https://doi.org/10.1016/s0006-3495(00)76713-0openalex-snapshot
Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
inferredcites →https://doi.org/10.1016/s0014-5793(00)01134-0openalex-snapshot
The molecular chaperone Cdc37 is required for Ste11 function and pheromone‐induced cell cycle arrest
inferredcites →https://doi.org/10.1016/s0021-9258(17)31486-2openalex-snapshot
Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae.
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/s1097-2765(00)80184-7openalex-snapshot
SGT1 Encodes an Essential Component of the Yeast Kinetochore Assembly Pathway and a Novel Subunit of the SCF Ubiquitin Ligase Complex
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/10.1038/348166a0openalex-snapshot
Reduced levels of hsp90 compromise steroid receptor action in vivo
inferredcites →https://doi.org/10.1038/37108openalex-snapshot
Test of synergistic interactions among deleterious mutations in bacteria
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/emboj.2012.37openalex-snapshot
Dynamics of the regulation of Hsp90 by the co‐chaperone Sti1
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/nature05649openalex-snapshot
Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map
inferredcites →https://doi.org/10.1038/nature19807openalex-snapshot
The epichaperome is an integrated chaperome network that facilitates tumour survival
inferredcites →https://doi.org/10.1038/ncomms12037openalex-snapshot
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
inferredcites →https://doi.org/10.1038/ncomms15328openalex-snapshot
An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
inferredcites →https://doi.org/10.1038/ncomms7655openalex-snapshot
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules
inferredcites →https://doi.org/10.1038/nmeth.2089openalex-snapshot
NIH Image to ImageJ: 25 years of image analysis
inferredcites →https://doi.org/10.1038/nprot.2007.13openalex-snapshot
High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method
inferredcites →https://doi.org/10.1038/nsmb.1965openalex-snapshot
Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
inferredcites →https://doi.org/10.1038/s41568-018-0020-9openalex-snapshot
Adapting to stress — chaperome networks in cancer
inferredcites →https://doi.org/10.1038/s41586-018-0409-3openalex-snapshot
Genetic and transcriptional evolution alters cancer cell line drug response
inferredcites →https://doi.org/10.1038/s41587-019-0037-yopenalex-snapshot
Multi-omic measurements of heterogeneity in HeLa cells across laboratories
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/10.1038/sj.emboj.7600930openalex-snapshot
The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
inferredcites →https://doi.org/10.1038/srep15377openalex-snapshot
High variability of genomic instability and gene expression profiling in different HeLa clones
inferredcites →https://doi.org/10.1039/c7mo00142hopenalex-snapshot
Systems analysis of the genetic interaction network of yeast molecular chaperones
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.1424342112openalex-snapshot
Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90
inferredcites →https://doi.org/10.1073/pnas.1719969115openalex-snapshot
Functional and physical interaction between yeast Hsp90 and Hsp70
inferredcites →https://doi.org/10.1073/pnas.1807618115openalex-snapshot
Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor
inferredcites →https://doi.org/10.1073/pnas.84.13.4455openalex-snapshot
Characterization of avian and viral p60src proteins expressed in yeast.
inferredcites →https://doi.org/10.1073/pnas.90.15.7074openalex-snapshot
Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
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.94.24.12949openalex-snapshot
In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
inferredcites →https://doi.org/10.1073/pnas.96.4.1409openalex-snapshot
Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation
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.271.22.12833openalex-snapshot
Reconstitution of the Steroid Receptor·hsp90 Heterocomplex Assembly System of Rabbit Reticulocyte Lysate
inferredcites →https://doi.org/10.1074/jbc.271.45.28697openalex-snapshot
Hsp90 Regulates Androgen Receptor Hormone Binding Affinity in Vivo
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.273.6.3679openalex-snapshot
Hop Modulates hsp70/hsp90 Interactions in Protein Folding
inferredcites →https://doi.org/10.1074/jbc.275.14.9986openalex-snapshot
A Stretch of Positively Charged Amino Acids at the N Terminus ofHansenula polymorpha Pex3p Is Involved in Incorporation of the Protein into the Peroxisomal Membrane
inferredcites →https://doi.org/10.1074/jbc.m005251200openalex-snapshot
Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins from Saccharomyces cerevisiae, Differ in Their Functional Properties
inferredcites →https://doi.org/10.1074/jbc.m110.138263openalex-snapshot
The Pih1-Tah1 Cochaperone Complex Inhibits Hsp90 Molecular Chaperone ATPase Activity
inferredcites →https://doi.org/10.1074/jbc.m112.439257openalex-snapshot
Cdc37 (Cell Division Cycle 37) Restricts Hsp90 (Heat Shock Protein 90) Motility by Interaction with N-terminal and Middle Domain Binding Sites
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.m213094200openalex-snapshot
Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase
inferredcites →https://doi.org/10.1074/jbc.m410562200openalex-snapshot
Co-chaperone Regulation of Conformational Switching in the Hsp90 ATPase Cycle
inferredcites →https://doi.org/10.1074/jbc.m512613200openalex-snapshot
Hsp90 Recognizes a Common Surface on Client Kinases
inferredcites →https://doi.org/10.1083/jcb.200210121openalex-snapshot
The Cdc37 protein kinase–binding domain is sufficient for protein kinase activity and cell viability
inferredcites →https://doi.org/10.1091/mbc.02-04-0051openalex-snapshot
Overexpression of Yeast Hsp110 Homolog Sse1p Suppressesydj1-151Thermosensitivity and Restores Hsp90-dependent Activity
inferredcites →https://doi.org/10.1091/mbc.7.1.91openalex-snapshot
The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast.
inferredcites →https://doi.org/10.1091/mbc.9.11.3071openalex-snapshot
Hsp90 Is Required for Pheromone Signaling in Yeast
inferredcites →https://doi.org/10.1091/mbc.e09-12-1017openalex-snapshot
Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis
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/cdg108openalex-snapshot
The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
inferredcites →https://doi.org/10.1101/cshperspect.a034017openalex-snapshot
Structure, Function, and Regulation of the Hsp90 Machinery
inferredcites →https://doi.org/10.1101/gad.11.14.1775openalex-snapshot
Cdc37 is a molecular chaperone with specific functions in signal transduction.
inferredcites →https://doi.org/10.1101/gr.1239303openalex-snapshot
Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks
inferredcites →https://doi.org/10.1126/science.1065810openalex-snapshot
Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants
inferredcites →https://doi.org/10.1126/science.274.5293.1713openalex-snapshot
A Cyclophilin Function in Hsp90-Dependent Signal Transduction
inferredcites →https://doi.org/10.1126/science.274.5293.1715openalex-snapshot
Chaperone Function of Hsp90-Associated Proteins
inferredcites →https://doi.org/10.1126/science.274.5293.1718openalex-snapshot
Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23
inferredcites →https://doi.org/10.1126/science.3511530openalex-snapshot
An Ancient Developmental Induction: Heat-Shock Proteins Induced in Sporulation and Oogenesis
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/10.1126/science.aaf1420openalex-snapshot
A global genetic interaction network maps a wiring diagram of cellular function
inferredcites →https://doi.org/10.1126/science.aaf5023openalex-snapshot
Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
inferredcites →https://doi.org/10.1126/science.aag0219openalex-snapshot
Countering the Zika epidemic in Latin America
inferredcites →https://doi.org/10.1126/science.aao1729openalex-snapshot
Systematic analysis of complex genetic interactions
inferredcites →https://doi.org/10.1128/ec.00170-14openalex-snapshot
The Hsp90 Cochaperones Cpr6, Cpr7, and Cns1 Interact with the Intact Ribosome
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.19.3.1661openalex-snapshot
p50cdc37 Acting in Concert with Hsp90 Is Required for Raf-1 Function
inferredcites →https://doi.org/10.1128/mcb.7.6.2180openalex-snapshot
Expression of Rous sarcoma virus transforming protein pp60v-src in Saccharomyces cerevisiae cells.
inferredcites →https://doi.org/10.1146/annurev.biochem.75.103004.142738openalex-snapshot
Structure and Mechanism of the Hsp90 Molecular Chaperone Machinery
inferredcites →https://doi.org/10.1210/me.2006-0547openalex-snapshot
FK506-Binding Protein 52 Phosphorylation: A Potential Mechanism for Regulating Steroid Hormone Receptor Activity
inferredcites →https://doi.org/10.1210/me.7.1.4openalex-snapshot
Steroid receptors and their associated proteins
inferredcites →https://doi.org/10.1371/journal.pone.0026044openalex-snapshot
An Interaction Network Predicted from Public Data as a Discovery Tool: Application to the Hsp90 Molecular Chaperone Machine
inferredcites →https://doi.org/10.1385/1-59259-958-3:171openalex-snapshot
Synthetic Genetic Array Analysis in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1515/bc.2002.152openalex-snapshot
The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically
inferredcites →https://doi.org/10.15252/embj.201796700openalex-snapshot
Tumor suppressor Tsc1 is a new Hsp90 co‐chaperone that facilitates folding of kinase and non‐kinase clients
inferredcites →https://doi.org/10.1534/genetics.104.036871openalex-snapshot
Mechanisms of Haploinsufficiency Revealed by Genome-Wide Profiling in Yeast
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4172121openalex-extracted
Cellular Protein TTC4 and its Cofactor HSP90 are Pro-Viral for Bovine Herpesvirus 1
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_7openalex-snapshot
Role of Heat Shock Proteins in Immune Modulation in Malaria
inferred← citeshttps://doi.org/10.1007/978-3-031-14740-1_6openalex-snapshot
p23 and Aha1: Distinct Functions Promote Client Maturation
inferred← citeshttps://doi.org/10.1007/s00204-021-03070-8openalex-snapshot
The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response
inferred← citeshttps://doi.org/10.1007/s00401-022-02491-8openalex-snapshot
Stress-inducible phosphoprotein 1 (HOP/STI1/STIP1) regulates the accumulation and toxicity of α-synuclein in vivo
inferred← citeshttps://doi.org/10.1007/s12192-020-01167-0openalex-snapshot
Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions
inferred← citeshttps://doi.org/10.1016/j.cbpb.2022.110777openalex-snapshot
Gene expression and functional analysis of Aha1a and Aha1b in stress response in zebrafish
inferred← citeshttps://doi.org/10.1016/j.celrep.2022.111039openalex-snapshot
A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand
inferred← citeshttps://doi.org/10.1016/j.cstres.2025.100118openalex-snapshot
Hsp70 and Hsp90 post-translational modifications and translating the chaperone code
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.127486openalex-snapshot
DnaJs are enriched in tau regulators
inferred← citeshttps://doi.org/10.1016/j.jbc.2026.113292openalex-snapshot
An isotype-specific phosphorylation of Hsp90 rewires co-chaperone regulations
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.2022.03.040openalex-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.2023.07.028openalex-snapshot
A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle
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.virusres.2022.198927openalex-snapshot
1 Cellular protein TTC4 and its cofactor HSP90 are pro-viral for bovine herpesvirus 1
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/acs.jpcb.6c03220openalex-snapshot
Electron Paramagnetic Resonance (EPR) Spectroscopy Reveals Nucleotide- and Partner-Dependent Conformational Ensembles in Hsp90
inferred← citeshttps://doi.org/10.1038/s41467-021-21063-0openalex-snapshot
Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle
inferred← citeshttps://doi.org/10.1038/s41580-023-00640-9openalex-snapshot
Structural and functional complexity of HSP90 in cellular homeostasis and disease
inferred← citeshttps://doi.org/10.1042/ebc20220224openalex-snapshot
Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function
inferred← citeshttps://doi.org/10.1073/pnas.2309326121openalex-snapshot
Structural transitions modulate the chaperone activities of Grp94
inferred← citeshttps://doi.org/10.1093/genetics/iyab009openalex-snapshot
Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects
inferred← citeshttps://doi.org/10.1186/s40478-021-01159-wopenalex-snapshot
Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice
inferred← citeshttps://doi.org/10.1371/journal.pgen.1010442openalex-snapshot
Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation
inferred← citeshttps://doi.org/10.1371/journal.pgen.1010772openalex-snapshot
Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle
inferred← citeshttps://doi.org/10.1371/journal.pgen.1011508openalex-snapshot
Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function
inferred← citeshttps://doi.org/10.18632/oncotarget.28653openalex-snapshot
Molecular chaperones: Guardians of tumor suppressor stability and function
inferred← citeshttps://doi.org/10.3389/fmolb.2021.787260openalex-snapshot
Mutations in Hsp90 Cochaperones Result in a Wide Variety of Human Disorders
inferred← citeshttps://doi.org/10.3389/fmolb.2022.938099openalex-snapshot
Host cell stress response as a predictor of COVID-19 infectivity and disease progression
inferred← citeshttps://doi.org/10.3389/fmolb.2024.1325590openalex-snapshot
Insights into Hsp90 mechanism and in vivo functions learned from studies in the yeast, Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.3390/biom12070928openalex-snapshot
Emerging Link between Tsc1 and FNIP Co-Chaperones of Hsp90 and Cancer
inferred← citeshttps://doi.org/10.3390/cells10112849openalex-snapshot
Inhibitors of the Plasmodium falciparum Hsp90 towards Selective Antimalarial Drug Design: The Past, Present and Future
inferred← citeshttps://doi.org/10.3390/jof7030209openalex-snapshot
Chaperone Networks in Fungal Pathogens of Humans
inferred← citeshttps://doi.org/10.6084/m9.figshare.14391487openalex-snapshot
Additional file 1 of Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice
inferred← citeshttps://doi.org/10.7554/elife.102666openalex-snapshot
The known unknowns of the Hsp90 chaperone
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