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Hsp90
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06956.xopenalex-snapshot
A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.
inferredcites →https://doi.org/10.1006/jmbi.1998.2349openalex-snapshot
Monomer Arrangement in HSP90 Dimer as Determined by Decoration with N and C-Terminal Region Specific Antibodies
inferredcites →https://doi.org/10.1006/jmbi.1999.3172openalex-snapshot
An unstructured C-terminal region of the hsp90 co-chaperone p23 is important for its chaperone function 1 1Edited by R. Huber
inferredcites →https://doi.org/10.1006/jmbi.2000.4157openalex-snapshot
C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle 1 1Edited by R. Huber
inferredcites →https://doi.org/10.1006/scdb.1999.0320openalex-snapshot
GRP94, an ER chaperone with protein and peptide binding properties
inferredcites →https://doi.org/10.1016/s0014-5793(97)01363-xopenalex-snapshot
In vitro evidence that hsp90 contains two independent chaperone sites
inferredcites →https://doi.org/10.1016/s0021-9258(17)31487-4openalex-snapshot
A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.
inferredcites →https://doi.org/10.1016/s0021-9258(17)37651-2openalex-snapshot
Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with 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/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)80624-8openalex-snapshot
Molecular Chaperones Activate the Drosophila Ecdysone Receptor, an RXR Heterodimer
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)80806-5openalex-snapshot
Getting Newly Synthesized Proteins into Shape
inferredcites →https://doi.org/10.1016/s0092-8674(00)80830-2openalex-snapshot
Structure of TPR Domain–Peptide Complexes
inferredcites →https://doi.org/10.1016/s0092-8674(00)81588-3openalex-snapshot
Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1
inferredcites →https://doi.org/10.1016/s0968-0004(99)01503-0openalex-snapshot
GHKL, an emergent ATPase/kinase superfamily
inferredcites →https://doi.org/10.1038/24550openalex-snapshot
Hsp90 as a capacitor for morphological evolution
inferredcites →https://doi.org/10.1038/33934openalex-snapshot
Dynamic activation of endothelial nitric oxide synthase by Hsp90
inferredcites →https://doi.org/10.1038/348166a0openalex-snapshot
Reduced levels of hsp90 compromise steroid receptor action in vivo
inferredcites →https://doi.org/10.1038/35050509openalex-snapshot
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
inferredcites →https://doi.org/10.1038/35050618openalex-snapshot
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
inferredcites →https://doi.org/10.1038/379225a0openalex-snapshot
Structure and mechanism of DNA topoisomerase II
inferredcites →https://doi.org/10.1038/381571a0openalex-snapshot
Molecular chaperones in cellular protein folding
inferredcites →https://doi.org/10.1038/386414a0openalex-snapshot
An atypical topoisomerase II from archaea with implications for meiotic recombination
inferredcites →https://doi.org/10.1046/j.1365-2184.2000.00189.xopenalex-snapshot
Chaperones in cell cycle regulation and mitogenic signal transduction: a review
inferredcites →https://doi.org/10.1046/j.1365-2958.2000.01951.xopenalex-snapshot
ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
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.90.15.7074openalex-snapshot
Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
inferredcites →https://doi.org/10.1073/pnas.91.18.8324openalex-snapshot
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
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/10.1073/pnas.94.24.12949openalex-snapshot
In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
inferredcites →https://doi.org/10.1073/pnas.95.4.1495openalex-snapshot
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
inferredcites →https://doi.org/10.1073/pnas.96.4.1297openalex-snapshot
The charged region of Hsp90 modulates the function of the N-terminal domain
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.270.41.24585openalex-snapshot
Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association
inferredcites →https://doi.org/10.1074/jbc.271.36.22030openalex-snapshot
Physical Interaction of Mammalian CDC37 with CDK4
inferredcites →https://doi.org/10.1074/jbc.271.50.32315openalex-snapshot
The Tetratricopeptide Repeat Domain of Protein Phosphatase 5 Mediates Binding to Glucocorticoid Receptor Heterocomplexes and Acts as a Dominant Negative Mutant
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.272.30.18694openalex-snapshot
The Function of Steroid Hormone Receptors Is Inhibited by the hsp90-specific Compound Geldanamycin
inferredcites →https://doi.org/10.1074/jbc.272.7.4013openalex-snapshot
The hsp90-binding Antibiotic Geldanamycin Decreases Raf Levels and Epidermal Growth Factor Signaling without Disrupting Formation of Signaling Complexes or Reducing the Specific Enzymatic Activity of Raf Kinase
inferredcites →https://doi.org/10.1074/jbc.273.29.18007openalex-snapshot
Specific Binding of Tetratricopeptide Repeat Proteins to the C-terminal 12-kDa Domain of hsp90
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.274.25.17525openalex-snapshot
The Importance of ATP Binding and Hydrolysis by Hsp90 in Formation and Function of Protein Heterocomplexes
inferredcites →https://doi.org/10.1074/jbc.275.12.9055openalex-snapshot
A Critical Role for the Proteasome Activator PA28 in the Hsp90-dependent Protein Refolding
inferredcites →https://doi.org/10.1074/jbc.275.5.3305openalex-snapshot
The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties
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.m002035200openalex-snapshot
The Molecular Chaperones Hsp90 and Hsc70 Are Both Necessary and Sufficient to Activate Hormone Binding by Glucocorticoid Receptor
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.m007385200openalex-snapshot
Functional Interaction of Human Cdc37 with the Androgen Receptor but Not with the Glucocorticoid Receptor
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/16.8.1961openalex-snapshot
The heat shock protein 83 (Hsp83) is required for Raf‐mediated signalling in Drosophila
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/17.23.6879openalex-snapshot
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
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/10.1093/emboj/19.6.1252openalex-snapshot
Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates
inferredcites →https://doi.org/10.1093/emboj/19.7.1516openalex-snapshot
Hsp90 is required for c‐Mos activation and biphasic MAP kinase activation in Xenopus oocytes
inferredcites →https://doi.org/10.1101/gad.10.12.1491openalex-snapshot
Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4.
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/gad.14.4.422openalex-snapshot
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.001_1.xopenalex-snapshot
Mechanism of Dimer Formation of the 90‐kDa Heat‐Shock Protein
inferredcites →https://doi.org/10.1126/science.268.5219.1888openalex-snapshot
A Scattered-Wave Image of Subduction Beneath the Transverse Ranges
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.286.5446.1888openalex-snapshot
Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins
inferredcites →https://doi.org/10.1128/mcb.18.12.7344openalex-snapshot
CNS1 Encodes an Essential p60/Sti1 Homolog in Saccharomyces cerevisiae That Suppresses Cyclophilin 40 Mutations and Interacts with Hsp90
inferredcites →https://doi.org/10.1128/mcb.18.12.7353openalex-snapshot
Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7Δ Cells
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/10.1128/mcb.20.24.9262-9270.2000openalex-snapshot
Role of HSP90 in Salt Stress Tolerance via Stabilization and Regulation of Calcineurin
inferredcites →https://doi.org/10.1210/edrv.18.3.0303openalex-snapshot
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones
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
inferredcites →https://doi.org/10.1379/1466-1268(1998)003<0118:diopat>2.3.co;2openalex-snapshot
Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/9781118101773.ch11openalex-snapshot
Candidiasis and Less Common Yeast Genera
inferred← citeshttps://doi.org/10.1002/9781118140574.ch3openalex-snapshot
Role of Chaperone Proteins in AHR Function
inferred← citeshttps://doi.org/10.1002/9781118482490.ch7openalex-snapshot
The Pivotal Role of CK2 in the Kinome‐Targeting Hsp90 Chaperone Machinery
inferred← citeshttps://doi.org/10.1002/9781119463665.ch12openalex-snapshot
Plant Molecular Chaperones: Structural Organization and their Roles in Abiotic Stress Tolerance
inferred← citeshttps://doi.org/10.1002/9783527610754.dd03openalex-snapshot
Molecular Chaperones and the Ubiquitin–Proteasome System
inferred← citeshttps://doi.org/10.1002/9783527619320.ch1aopenalex-snapshot
Molecular Chaperones and the Ubiquitin–Proteasome System
inferred← citeshttps://doi.org/10.1002/9783527619498.ch48openalex-snapshot
Regulation of Hsp70 Chaperones by Co‐chaperones
inferred← citeshttps://doi.org/10.1002/9783527619498.ch65openalex-snapshot
Chaperone Systems in Chloroplasts
inferred← citeshttps://doi.org/10.1002/9783527620210.ch1openalex-snapshot
Molecular Chaperones and the Ubiquitin–Proteasome System
inferred← citeshttps://doi.org/10.1002/9783527633883.ch23openalex-snapshot
PlasmodiumHsp90 as an Antimalarial Target
inferred← citeshttps://doi.org/10.1002/9783527694570.ch7openalex-snapshot
Molecular Chaperone: Structure, Function, and Role in Plant Abiotic Stress Tolerance
inferred← citeshttps://doi.org/10.1002/arch.20216openalex-snapshot
Structural characterization of the medfly hsp83 gene and functional analysis of its proximal promoter region in vivo by germ‐line transformation
inferred← citeshttps://doi.org/10.1002/asia.201100145openalex-snapshot
Solid‐Phase Parallel Synthesis of a Tetrahydroindazolone Library Containing Three Unique Core Skeletons
inferred← citeshttps://doi.org/10.1002/bies.20020openalex-snapshot
Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance
inferred← citeshttps://doi.org/10.1002/bies.20107openalex-snapshot
Hop: more than an Hsp70/Hsp90 adaptor protein
inferred← citeshttps://doi.org/10.1002/cbic.200300658openalex-snapshot
NMR Chemical Shift Perturbation Study of the N‐Terminal Domain of Hsp90 upon Binding of ADP, AMP‐PNP, Geldanamycin, and Radicicol
inferred← citeshttps://doi.org/10.1002/eji.200535326openalex-snapshot
A role for the Hsp90 molecular chaperone family in antigen presentation to T lymphocytes via major histocompatibility complex class II molecules
inferred← citeshttps://doi.org/10.1002/hed.21755openalex-snapshot
Novel molecular targeted therapies for refractory thyroid cancer
inferred← citeshttps://doi.org/10.1002/hed.23687openalex-snapshot
DNA aneuploidy‐specific therapy for head and neck squamous cell carcinoma
inferred← citeshttps://doi.org/10.1002/ijc.21717openalex-snapshot
The topoisomerase II–Hsp90 complex: A new chemotherapeutic target?
inferred← citeshttps://doi.org/10.1002/jcp.20327openalex-snapshot
Electromagnetic fields at mobile phone frequency induce apoptosis and inactivation of the multi‐chaperone complex in human epidermoid cancer cells
inferred← citeshttps://doi.org/10.1002/jcp.28614openalex-snapshot
CHIP attenuates lipopolysaccharide‐induced cardiac hypertrophy and apoptosis by promoting NFATc3 proteasomal degradation
inferred← citeshttps://doi.org/10.1002/jcp.30567openalex-snapshot
Autophagy based cellular physiological strategies target oncogenic progression
inferred← citeshttps://doi.org/10.1002/mc.20141openalex-snapshot
Cooperative inhibitory effect of ZD1839 (Iressa) in combination with 17‐AAG on glioma cell growth
inferred← citeshttps://doi.org/10.1002/mc.20152openalex-snapshot
Synergistic interaction between 17‐AAG and phosphatidylinositol 3‐kinase inhibition in human malignant glioma cells
inferred← citeshttps://doi.org/10.1002/med.22114openalex-snapshot
The Hsp90β Isoform: An Attractive Target for Drug Development
inferred← citeshttps://doi.org/10.1002/mrd.20548openalex-snapshot
Expression of stress inducible protein 1 (Stip1) in the mouse testis
inferred← citeshttps://doi.org/10.1002/pmic.200500680openalex-snapshot
Quantitative analysis of 2,3,7,8‐tetrachlorodibenzo‐ p ‐dioxin‐induced proteome alterations in 5L rat hepatoma cells using isotope‐coded protein labels
inferred← citeshttps://doi.org/10.1002/pmic.200700313openalex-snapshot
Alteration of S‐nitrosothiol homeostasis and targets for protein S‐nitrosation in human hepatocytes
inferred← citeshttps://doi.org/10.1002/pmic.201400049openalex-snapshot
In vitro flowering associated protein changes in Dendrocalamus hamiltonii
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.278openalex-snapshot
HOP is a monomer: Investigation of the oligomeric state of the co‐chaperone HOP
inferred← citeshttps://doi.org/10.1002/pro.282openalex-snapshot
Osmolyte‐induced conformational changes in the Hsp90 molecular chaperone
inferred← citeshttps://doi.org/10.1002/pro.3161openalex-snapshot
The chaperone toolbox at the single‐molecule level: From clamping to confining
inferred← citeshttps://doi.org/10.1002/pro.3174openalex-snapshot
Molecular mechanism of bacterial Hsp90 pH‐dependent ATPase activity
inferred← citeshttps://doi.org/10.1002/pros.10255openalex-snapshot
Proteomic analysis of human prostasomes
inferred← citeshttps://doi.org/10.1002/ps.7147openalex-snapshot
Antiviral modes of action of the novel compound GLY ‐15 containing pyrimidine heterocycle and moroxydine skeleton against tobacco mosaic virus
inferred← citeshttps://doi.org/10.1006/cbir.2002.0882openalex-snapshot
EVIDENCE THAT THE NOVOBIOCIN‐SENSITIVE ATP‐BINDING SITE OF THE HEAT SHOCK PROTEIN 90 (HSP90) IS NECESSARY FOR ITS AUTOPHOSPHORYLATION
inferred← citeshttps://doi.org/10.1006/geno.2002.6834openalex-snapshot
A New Gene Family (FAM9) of Low-Copy Repeats in Xp22.3 Expressed Exclusively in Testis: Implications for Recombinations in This Region
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1006/nbdi.2002.0502openalex-snapshot
Chemical Chaperones Reduce Aggregate Formation and Cell Death Caused by the Truncated Machado–Joseph Disease Gene Product with an Expanded Polyglutamine Stretch
inferred← citeshttps://doi.org/10.1007/0-387-30395-2_13openalex-snapshot
Heat Shock Proteins in Brain Function
inferred← citeshttps://doi.org/10.1007/1-4020-5252-9_4openalex-snapshot
The Unfolded Protein Response
inferred← citeshttps://doi.org/10.1007/10_2023_233openalex-snapshot
Cell-Free Protein Synthesis of Metalloproteins
inferred← citeshttps://doi.org/10.1007/4735_90openalex-snapshot
Proteasomal degradation of misfolded proteins
inferred← citeshttps://doi.org/10.1007/7355_2015_96openalex-snapshot
Evaluating Dual Hsp90 and Hsp70 Inhibition as a Cancer Therapy
inferred← citeshttps://doi.org/10.1007/978-0-387-30411-3_23openalex-snapshot
6.2 Mitochondrial-Endoplasmic Reticulum Interactions
inferred← citeshttps://doi.org/10.1007/978-0-387-39717-7_13openalex-snapshot
Up and Down Regulation of the Stress Response by the Co-Chaperone Ubiquitin Ligase CHIP
inferred← citeshttps://doi.org/10.1007/978-0-387-39975-1openalex-snapshot
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
inferred← citeshttps://doi.org/10.1007/978-0-387-39975-1_3openalex-snapshot
Molecular Interaction Network of the Hsp90 Chaperone System
inferred← citeshttps://doi.org/10.1007/978-0-387-49310-7_6openalex-snapshot
UNC-45: A Chaperone for Myosin and a Co-Chaperone for Hsp90
inferred← citeshttps://doi.org/10.1007/978-0-387-69179-4_22openalex-snapshot
Cellular and Molecular Signatures of Androgen Ablation of Prostate Cancer
inferred← citeshttps://doi.org/10.1007/978-1-4020-5963-6_6openalex-snapshot
HSP90 Co-Chaperones in Saccharomyces Cerevisiae
inferred← citeshttps://doi.org/10.1007/978-1-4020-8231-3_1openalex-snapshot
Chaperones and Polyglutamine Expansion Disorders
inferred← citeshttps://doi.org/10.1007/978-1-4020-8231-3_4openalex-snapshot
Heat Shock Proteins as Therapeutic Targets in Amyotrophic Lateral Sclerosis
inferred← citeshttps://doi.org/10.1007/978-1-4419-6260-7_1openalex-snapshot
Physiological Adaptations of Stressed Fish to Polluted Environments: Role of Heat Shock Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4419-7061-9_3openalex-snapshot
Molecular Chaperones as Facilitators of Protein Degradation
inferred← citeshttps://doi.org/10.1007/978-1-4614-5847-0_7openalex-snapshot
Molecular Chaperones and How Addiction Matters in Cancer Therapy
inferred← citeshttps://doi.org/10.1007/978-1-4939-1130-1_8openalex-snapshot
The Candida albicans Hsp90 Chaperone Network Is Environmentally Flexible and Evolutionarily Divergent
inferred← citeshttps://doi.org/10.1007/978-1-59259-680-5_20openalex-snapshot
Chaperone Proteins/Heat Shock Proteins As Anticancer Vaccines
inferred← citeshttps://doi.org/10.1007/978-1-60327-394-7_4openalex-snapshot
Molecular Simulations of Peptides: A Useful Tool for the Development of New Drugs and for the Study of Molecular Recognition
inferred← citeshttps://doi.org/10.1007/978-3-030-03952-3_11openalex-snapshot
Cytosolic Heat Shock Protein 90 in Plant Hormone and Environmental Stress Response
inferred← citeshttps://doi.org/10.1007/978-3-030-03952-3_15openalex-snapshot
Extracellular HSP90α Versus Intracellular HSP90β in Wound Healing and Cancer
inferred← citeshttps://doi.org/10.1007/978-3-030-23158-3_25openalex-snapshot
Hsp90: Is There an Unknown Role in Pain Neurobiology
inferred← citeshttps://doi.org/10.1007/978-3-030-23158-3_27openalex-snapshot
HSP90 et al.: Chaperome and Proteostasis Deregulation in Human Disease
inferred← citeshttps://doi.org/10.1007/978-3-030-73507-4_8openalex-snapshot
Thermotolerant Soil Microbes and Their Role in Mitigation of Heat Stress in Plants
inferred← citeshttps://doi.org/10.1007/978-3-319-28899-4_7openalex-snapshot
Function of Heat-Shock Proteins in Drought Tolerance Regulation of Plants
inferred← citeshttps://doi.org/10.1007/978-3-319-46340-7_13openalex-snapshot
Molecular Chaperones and HSPs in Sugarcane and Eucalyptus
inferred← citeshttps://doi.org/10.1007/978-3-319-46340-7_8openalex-snapshot
The Role of Plant 90-kDa Heat Shock Proteins in Plant Immunity
inferred← citeshttps://doi.org/10.1007/978-3-319-73377-7_10openalex-snapshot
Heat Shock Proteins in Aquaculture Disease Immunology and Stress Response of Crustaceans
inferred← citeshttps://doi.org/10.1007/978-3-319-73377-7_8openalex-snapshot
Physiological Role of Heat Shock Proteins, Molecular Function and Stress Removal in Fishes
inferred← citeshttps://doi.org/10.1007/978-3-319-74715-6_8openalex-snapshot
Molecular Chaperones: Structure-Function Relationship and their Role in Protein Folding
inferred← citeshttps://doi.org/10.1007/978-3-540-39402-0_4openalex-snapshot
Plant responses to heat stress
inferred← citeshttps://doi.org/10.1007/978-3-662-10360-9_5openalex-snapshot
Stress Responses in S. pombe
inferred← citeshttps://doi.org/10.1007/978-94-007-0189-2_10openalex-snapshot
Brassinosteroid action and its relation with heat stress mechanisms in plants
inferred← citeshttps://doi.org/10.1007/978-94-007-6787-4_14openalex-snapshot
Candida albicans Ssa: An Hsp70 Homologue and Virulence Factor
inferred← citeshttps://doi.org/10.1007/978-94-007-6787-4_15openalex-snapshot
Hsp90 Plays a Role in Host-Bacterial Interactions: Insight Gained from Acanthamoeba castellanii
inferred← citeshttps://doi.org/10.1007/978-94-017-9412-1_7openalex-snapshot
A Developmental-Physiological Perspective on the Development and Evolution of Phenotypic Plasticity
inferred← citeshttps://doi.org/10.1007/978-981-15-5136-9_21openalex-snapshot
Molecular Chaperones and Their Applications
inferred← citeshttps://doi.org/10.1007/978-981-19-9159-2_26openalex-snapshot
Biochemical and Molecular Aspects for Plant Improvement Under Climate Stress
inferred← citeshttps://doi.org/10.1007/s00005-020-00573-7openalex-snapshot
Antibodies to Heat Shock Proteins 90α and 90β in Psoriasis
inferred← citeshttps://doi.org/10.1007/s00018-009-9152-0openalex-snapshot
Protein Kinase CK2 in Health and Disease
inferred← citeshttps://doi.org/10.1007/s00239-003-2490-xopenalex-snapshot
Phylogenetic Analysis of Eukaryotes Using Heat-Shock Protein Hsp90
inferred← citeshttps://doi.org/10.1007/s00280-008-0888-2openalex-snapshot
Heat shock protein 90 inhibition abrogates hepatocellular cancer growth through cdc2-mediated G2/M cell cycle arrest and apoptosis
inferred← citeshttps://doi.org/10.1007/s00280-013-2134-9openalex-snapshot
Open-label, dose-escalation, safety, pharmacokinetic, and pharmacodynamic study of intravenously administered CNF1010 (17-(allylamino)-17-demethoxygeldanamycin [17-AAG]) in patients with solid tumors
inferred← citeshttps://doi.org/10.1007/s00294-005-0580-6openalex-snapshot
Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1007/s00425-008-0886-yopenalex-snapshot
Overexpression of AtHsp90.2, AtHsp90.5 and AtHsp90.7 in Arabidopsis thaliana enhances plant sensitivity to salt and drought stresses
inferred← citeshttps://doi.org/10.1007/s00425-010-1341-4openalex-snapshot
Dynamic changes in the leaf proteome of a C3 xerophyte, Citrullus lanatus (wild watermelon), in response to water deficit
inferred← citeshttps://doi.org/10.1007/s00427-002-0212-9openalex-snapshot
HSP90 function is required for morphogenesis in ascidian and echinoid embryos
inferred← citeshttps://doi.org/10.1007/s00427-007-0171-2openalex-snapshot
Developmental expression of Hsp90, Hsp70 and HSF during morphogenesis in the vetigastropod Haliotis asinina
inferred← citeshttps://doi.org/10.1007/s00427-011-0379-zopenalex-snapshot
Post-embryonic functions of HSP90 in Tribolium castaneum include the regulation of compound eye development
inferred← citeshttps://doi.org/10.1007/s00432-012-1247-6openalex-snapshot
HSP90 inhibition results in apoptosis of Philadelphia acute lymphoblastic leukaemia cells: an attractive prospect of new targeted agents
inferred← citeshttps://doi.org/10.1007/s00709-022-01815-5openalex-snapshot
Genome-wide characterization of DcHsp90 gene family in carnation (Dianthus caryophyllus L.) and functional analysis of DcHsp90-6 in heat tolerance
inferred← citeshttps://doi.org/10.1007/s00726-016-2361-6openalex-snapshot
A network biology approach to understanding the importance of chameleon proteins in human physiology and pathology
inferred← citeshttps://doi.org/10.1007/s00775-018-1634-9openalex-snapshot
Novobiocin–ferrocene conjugates possessing anticancer and antiplasmodial activity independent of HSP90 inhibition
inferred← citeshttps://doi.org/10.1007/s10142-019-00695-yopenalex-snapshot
Genome-wide identification and expression analysis of Hsp70, Hsp90, and Hsp100 heat shock protein genes in barley under stress conditions and reproductive development
inferred← citeshttps://doi.org/10.1007/s10254-003-0021-1openalex-snapshot
Hsp70 and Hsp90—a relay team for protein folding
inferred← citeshttps://doi.org/10.1007/s10254-004-0025-5openalex-snapshot
Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies
inferred← citeshttps://doi.org/10.1007/s10330-004-0347-4openalex-snapshot
Characterization of ST13 Protein Expression in Human Colorectal Cancer Tissues
inferred← citeshttps://doi.org/10.1007/s10495-013-0936-1openalex-snapshot
Post-translational regulation of the cellular levels of DAPK
inferred← citeshttps://doi.org/10.1007/s10517-012-1877-3openalex-snapshot
Dependence of Blood Levels of HSP70 and HSP90 on Genotypes of HSP70, GSTT1, and GSTM1 Gene Polymorphism in Individuals Chronically Exposed to Mercury
inferred← citeshttps://doi.org/10.1007/s10545-014-9701-zopenalex-snapshot
Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators
inferred← citeshttps://doi.org/10.1007/s10549-011-1866-7openalex-snapshot
A phase II study of 17-allylamino-17-demethoxygeldanamycin in metastatic or locally advanced, unresectable breast cancer
inferred← citeshttps://doi.org/10.1007/s10620-010-1558-xopenalex-snapshot
Evidence for Enhanced Cytoprotective Function of HSP90-Overexpressing Small Intestinal Epithelial Cells
inferred← citeshttps://doi.org/10.1007/s10637-017-0495-3openalex-snapshot
First-in-human study of the epichaperome inhibitor PU-H71: clinical results and metabolic profile
inferred← citeshttps://doi.org/10.1007/s10646-012-0980-6openalex-snapshot
Bisphenol-A affects the developmental progression and expression of heat-shock protein genes in the moth Sesamia nonagrioides
inferred← citeshttps://doi.org/10.1007/s10695-011-9556-2openalex-snapshot
Cloning and characterization of the HSP90 beta gene from Tanichthys albonubes Lin (Cyprinidae): effect of copper and cadmium exposure
inferred← citeshttps://doi.org/10.1007/s10695-024-01403-9openalex-snapshot
Effects of dietary powdered Ficus deltoidea on the growth and health performance of African catfish, Clarias gariepinus production
inferred← citeshttps://doi.org/10.1007/s10725-008-9306-3openalex-snapshot
Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytica enhances growth rate as well as abiotic stress tolerance of poplar plants
inferred← citeshttps://doi.org/10.1007/s10725-026-01504-wopenalex-snapshot
Unveiling the CpHsp and CpHsf Gene families in the zucchini genome: Evolution, structure, and stress-responsive expression
inferred← citeshttps://doi.org/10.1007/s10811-018-1624-xopenalex-snapshot
Full-length transcriptome sequences obtained by a combination of sequencing platforms applied to heat shock proteins and polyunsaturated fatty acids biosynthesis in Pyropia haitanensis
inferred← citeshttps://doi.org/10.1007/s11010-005-2949-8openalex-snapshot
CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone
inferred← citeshttps://doi.org/10.1007/s11010-005-9045-yopenalex-snapshot
Analysis of interaction partners for perilipin and ADRP on lipid droplets∗
inferred← citeshttps://doi.org/10.1007/s11010-008-9818-1openalex-snapshot
Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37
inferred← citeshttps://doi.org/10.1007/s11010-010-0651-yopenalex-snapshot
Carbamazepine promotes Her-2 protein degradation in breast cancer cells by modulating HDAC6 activity and acetylation of Hsp90
inferred← citeshttps://doi.org/10.1007/s11010-013-1844-yopenalex-snapshot
Association of heat-shock proteins in various neurodegenerative disorders: is it a master key to open the therapeutic door?
inferred← citeshttps://doi.org/10.1007/s11010-019-03645-1openalex-snapshot
Heat shock proteins and their expression in primary murine cardiac cell populations during ischemia and reperfusion
inferred← citeshttps://doi.org/10.1007/s11033-009-9715-zopenalex-snapshot
Molecular cloning and characterization of four heat shock protein genes from Macrocentrus cingulum (Hymenoptera: Braconidae)
inferred← citeshttps://doi.org/10.1007/s11033-013-2630-3openalex-snapshot
The association of SNPs in Hsp90β gene 5′ flanking region with thermo tolerance traits and tissue mRNA expression in two chicken breeds
inferred← citeshttps://doi.org/10.1007/s11033-020-05722-xopenalex-snapshot
Evolutionary history of the heat shock protein 90 (Hsp90) family of 43 plants and characterization of Hsp90s in Solanum tuberosum
inferred← citeshttps://doi.org/10.1007/s11095-010-0234-3openalex-snapshot
Mixed pH-Sensitive Polymeric Micelles for Combination Drug Delivery
inferred← citeshttps://doi.org/10.1007/s11103-008-9322-8openalex-snapshot
Complexity of Hsp90 in organelle targeting
inferred← citeshttps://doi.org/10.1007/s11120-004-2216-yopenalex-snapshot
The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast
inferred← citeshttps://doi.org/10.1007/s11684-007-0048-9openalex-snapshot
Construction of Hsp90β gene specific silencing plasmid and its transfection efficiency
inferred← citeshttps://doi.org/10.1007/s11738-019-2813-1openalex-snapshot
Green algal molecular responses to temperature stress
inferred← citeshttps://doi.org/10.1007/s12035-023-03846-2openalex-snapshot
Molecular Chaperones as Therapeutic Target: Hallmark of Neurodegenerative Disorders
inferred← citeshttps://doi.org/10.1007/s12038-007-0060-xopenalex-snapshot
Complexity of rice Hsp100 gene family: lessons from rice genome sequence data
inferred← citeshttps://doi.org/10.1007/s12192-008-0035-3openalex-snapshot
Significance of heat-shock protein (HSP) 90 expression in acute myeloid leukemia cells
inferred← citeshttps://doi.org/10.1007/s12192-008-0090-9openalex-snapshot
Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica
inferred← citeshttps://doi.org/10.1007/s12192-010-0218-6openalex-snapshot
Expression of hsp90 mediates cytoprotective effects in the gastrodermis of planarians
inferred← citeshttps://doi.org/10.1007/s12192-010-0222-xopenalex-snapshot
Gene expression profiles of cytosolic heat shock proteins Hsp70 and Hsp90 from symbiotic dinoflagellates in response to thermal stress: possible implications for coral bleaching
inferred← citeshttps://doi.org/10.1007/s12192-010-0223-9openalex-snapshot
Expression of heat shock protein-coding genes associated with anhydrobiosis in an African chironomid Polypedilum vanderplanki
inferred← citeshttps://doi.org/10.1007/s12192-014-0500-0openalex-snapshot
Characterizing heat shock protein 90 gene of Apolygus lucorum (Meyer-Dür) and its expression in response to different temperature and pesticide stresses
inferred← citeshttps://doi.org/10.1007/s12192-015-0652-6openalex-snapshot
Geographic variation in thermal tolerance and strategies of heat shock protein expression in the land snail Theba pisana in relation to genetic structure
inferred← citeshttps://doi.org/10.1007/s12272-026-01625-wopenalex-snapshot
eHsp90α enhances breast cancer cell invasion by activating the LRP1-EGFR/AKT-twist/snail signaling axis in cancer-associated fibroblasts
inferred← citeshttps://doi.org/10.1007/s12298-018-0525-4openalex-snapshot
Identification of genes associated with stress tolerance in moth bean [Vigna aconitifolia (Jacq.) Marechal], a stress hardy crop
inferred← citeshttps://doi.org/10.1007/s12298-020-00888-xopenalex-snapshot
Genome-wide analysis of HSP90 gene family in the Mediterranean olive (Olea europaea subsp. europaea) provides insight into structural patterns, evolution and functional diversity
inferred← citeshttps://doi.org/10.1007/s12298-021-00976-6openalex-snapshot
Overexpression of SlHSP90.2 leads to altered root biomass and architecture in tomato (Solanum lycopersicum)
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/s12551-019-00605-3openalex-snapshot
Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function
inferred← citeshttps://doi.org/10.1007/s12562-011-0451-7openalex-snapshot
cDNA cloning and expression analysis of two heat shock protein genes, Hsp90 and Hsp60, from a sterile Ulva pertusa (Ulvales, Chlorophyta)
inferred← citeshttps://doi.org/10.1007/s12562-017-1063-7openalex-snapshot
Heat shock protein 90 is a stress and immune response gene in the giant spiny frog Quasipaa spinosa
inferred← citeshttps://doi.org/10.1007/s13205-022-03422-wopenalex-snapshot
Exploring breast cancer exosomes for novel biomarkers of potential diagnostic and prognostic importance
inferred← citeshttps://doi.org/10.1007/s13273-010-0012-7openalex-snapshot
Toxicoproteomic analysis of phalloidin-induced cholestasis in mouse liver
inferred← citeshttps://doi.org/10.1007/s13277-015-3076-0openalex-snapshot
Glucose-regulated protein 78 mediates the therapeutic efficacy of 17-DMAG in colon cancer cells
inferred← citeshttps://doi.org/10.1007/s13530-017-0335-zopenalex-snapshot
Changes in activity and transcription of antioxidant enzymes and heat shock protein 90 in the water flea, Daphnia magna - exposed to mercury
inferred← citeshttps://doi.org/10.1007/s13562-013-0227-5openalex-snapshot
A potential role of UBC28 interacting RING finger protein TaRF1 in spike development of wheat
inferred← citeshttps://doi.org/10.1007/s13762-023-04971-0openalex-snapshot
Heat shock protein 70 reflected the state of inhabited fish response to water quality within lake ecosystem
inferred← citeshttps://doi.org/10.1016/b978-0-12-370873-1.00027-7openalex-snapshot
Chaperones and Proteases
inferred← citeshttps://doi.org/10.1016/b978-0-12-407697-6.00005-2openalex-snapshot
Extracellular Hsp90 (eHsp90) as the Actual Target in Clinical Trials
inferred← citeshttps://doi.org/10.1016/b978-0-12-800186-8.00002-xopenalex-snapshot
Targeting the Protein Quality Control (PQC) Machinery
inferred← citeshttps://doi.org/10.1016/b978-0-12-801944-3.00002-3openalex-snapshot
Targeting the Protein Quality Control (PQC) Machinery
inferred← citeshttps://doi.org/10.1016/b978-0-443-41553-1.00012-8openalex-snapshot
An overview of proteostasis
inferred← citeshttps://doi.org/10.1016/b978-012369448-5.50017-3openalex-snapshot
Heat shock protein-90 directed therapeutics and target validation
inferred← citeshttps://doi.org/10.1016/b978-012369509-3.50007-xopenalex-snapshot
Protein Misfolding, Chaperone Networks, and the Heat Shock Response in the Nervous System
inferred← citeshttps://doi.org/10.1016/j.aaf.2017.03.001openalex-snapshot
Molecular cloning, sequencing, and expression profiles of heat shock protein 90 ( HSP90 ) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila
inferred← citeshttps://doi.org/10.1016/j.abb.2004.12.020openalex-snapshot
Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions
inferred← citeshttps://doi.org/10.1016/j.abb.2013.04.015openalex-snapshot
Phosphorylation accelerates geldanamycin-induced Akt degradation
inferred← citeshttps://doi.org/10.1016/j.anaerobe.2003.10.003openalex-snapshot
The actin-ADP-ribosylating Clostridium botulinum C2 toxin
inferred← citeshttps://doi.org/10.1016/j.apsb.2012.03.009openalex-snapshot
Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment
inferred← citeshttps://doi.org/10.1016/j.aqrep.2024.102036openalex-snapshot
Transcriptome analysis of sea cucumber (Apostichopus japonicus) in southern China under heat stress
inferred← citeshttps://doi.org/10.1016/j.aquatox.2016.11.020openalex-snapshot
Alteration of development and gene expression induced by in ovo -nanoinjection of 3-hydroxybenzo[ c ]phenanthrene into Japanese medaka ( Oryzias latipes ) embryos
inferred← citeshttps://doi.org/10.1016/j.aquatox.2020.105705openalex-snapshot
Chronic exposure to environmental cadmium affects growth and survival, cellular stress, and glucose metabolism in juvenile channel catfish (Ictalurus punctatus)
inferred← citeshttps://doi.org/10.1016/j.arr.2005.09.002openalex-snapshot
The ubiquitin–proteasome system at the crossroads of stress-response and ageing pathways: A handle for skin care?
inferred← citeshttps://doi.org/10.1016/j.bbagen.2006.03.027openalex-snapshot
Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography
inferred← citeshttps://doi.org/10.1016/j.bbagen.2013.06.037openalex-snapshot
The hormone-dependent function of Hsp90 in the crosstalk between 20-hydroxyecdysone and juvenile hormone signaling pathways in insects is determined by differential phosphorylation and protein interactions
inferred← citeshttps://doi.org/10.1016/j.bbagen.2014.06.008openalex-snapshot
The effect of celastrol, a triterpene with antitumorigenic activity, on conformational and functional aspects of the human 90kDa heat shock protein Hsp90α, a chaperone implicated in the stabilization of the tumor phenotype
inferred← citeshttps://doi.org/10.1016/j.bbagen.2016.01.005openalex-snapshot
Design and biological testing of peptidic dimerization inhibitors of human Hsp90 that target the C-terminal domain
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2004.09.020openalex-snapshot
Cooperation of molecular chaperones with the ubiquitin/proteasome system
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.06.001openalex-snapshot
Accumulation of polyubiquitylated proteins in response to Ala-Ala-Phe-chloromethylketone is independent of the inhibition of tripeptidyl peptidase II
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.09.001openalex-snapshot
The role of Hsp90 in protein complex assembly
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.2011.09.009openalex-snapshot
Secreted heat shock protein-90 (Hsp90) in wound healing and cancer
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.10.013openalex-snapshot
GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.12.001openalex-snapshot
Tom34: A cytosolic cochaperone of the Hsp90/Hsp70 protein complex involved in mitochondrial protein import
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.12.012openalex-snapshot
Molecular mechanism underlying adenosine receptor-mediated mitochondrial targeting of protein kinase C
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.11.014openalex-snapshot
Biogenesis of mitochondrial carrier proteins: Molecular mechanisms of import into mitochondria
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.02.014openalex-snapshot
Hsp90 inhibition by PU-H71 induces apoptosis through endoplasmic reticulum stress and mitochondrial pathway in cancer cells and overcomes the resistance conferred by Bcl-2
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2021.119081openalex-snapshot
Protein quality control of DYRK family protein kinases by the Hsp90-Cdc37 molecular chaperone
inferred← citeshttps://doi.org/10.1016/j.bbrc.2006.04.104openalex-snapshot
F1F0-ATP synthase functions as a co-chaperone of Hsp90–substrate protein complexes
inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.06.112openalex-snapshot
Extracellular heat shock protein HSP90β secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-β1
inferred← citeshttps://doi.org/10.1016/j.bbrc.2011.03.088openalex-snapshot
Hsp90 is involved in the formation of P-bodies and stress granules
inferred← citeshttps://doi.org/10.1016/j.bbrc.2014.09.026openalex-snapshot
BIIB021, a novel Hsp90 inhibitor, sensitizes esophageal squamous cell carcinoma to radiation
inferred← citeshttps://doi.org/10.1016/j.bcp.2008.09.038openalex-snapshot
Indirect participation of Hsp90 in the regulation of the cyclin E turnover
inferred← citeshttps://doi.org/10.1016/j.biopha.2018.03.102openalex-snapshot
Targeted cancer therapy through 17-DMAG as an Hsp90 inhibitor: Overview and current state of the art
inferred← citeshttps://doi.org/10.1016/j.biosystems.2012.05.013openalex-snapshot
Mechanisms of developmental robustness
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2009.01.011openalex-snapshot
Molecular mechanisms of tolerance in tardigrades: New perspectives for preservation and stabilization of biological material
inferred← citeshttps://doi.org/10.1016/j.bmc.2004.07.053openalex-snapshot
Synthesis and biological activities of novel 17-aminogeldanamycin derivatives
inferred← citeshttps://doi.org/10.1016/j.bmcl.2003.11.011openalex-snapshot
Adenine derived inhibitors of the molecular chaperone HSP90—SAR explained through multiple X-ray structures
inferred← citeshttps://doi.org/10.1016/j.bmcl.2012.01.137openalex-snapshot
Discovery of novel aminoquinazolin-7-yl 6,7-dihydro-indol-4-ones as potent, selective inhibitors of heat shock protein 90
inferred← citeshttps://doi.org/10.1016/j.bmcl.2016.11.059openalex-snapshot
Virtual screening and biophysical studies lead to HSP90 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.canlet.2009.01.018openalex-snapshot
TRAP1, a novel mitochondrial chaperone responsible for multi-drug resistance and protection from apoptotis in human colorectal carcinoma cells
inferred← citeshttps://doi.org/10.1016/j.cbd.2019.02.009openalex-snapshot
Label-free quantification of protein expression in the rainbow trout (Oncorhynchus mykiss) in response to short-term exposure to heat stress
inferred← citeshttps://doi.org/10.1016/j.cbpa.2010.03.019openalex-snapshot
Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy
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