Hsp90: Structure and Function

The Pathophysiology of Mitochondrial Cell Death

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Adapting Proteostasis for Disease Intervention

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Hsp90 as a capacitor for morphological evolution

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HSP90 at the hub of protein homeostasis: emerging mechanistic insights

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Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*

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Targeting the dynamic HSP90 complex in cancer

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A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

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Hsp90 as a capacitor of phenotypic variation

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Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent

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Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone

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Structure of TPR Domain–Peptide Complexes

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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

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Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

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Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.

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Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

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Hsp90 Molecular Chaperone Inhibitors: Are We There Yet?

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The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

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Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone

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Reduced levels of hsp90 compromise steroid receptor action in vivo

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

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ER chaperones in mammalian development and human diseases

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The role of the unfolded protein response in tumour development: friend or foe?

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Molecular Identification of Cytosolic Prostaglandin E2 Synthase That Is Functionally Coupled with Cyclooxygenase-1 in Immediate Prostaglandin E2Biosynthesis

Tanioka, T., Nakatani, Y., Semmyo, N., Murakami, M., & Kudo, I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003504200 · Cited by 708

Hsp90 Potentiates the Rapid Evolution of New Traits: Drug Resistance in Diverse Fungi

Cowen, L. E., & Lindquist, S. (2005) · Science · doi:10.1126/science.1118370 · Cited by 698

The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

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FK506-binding Proteins 51 and 52 Differentially Regulate Dynein Interaction and Nuclear Translocation of the Glucocorticoid Receptor in Mammalian Cells

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In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis

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Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis

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PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1

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Functional proteomic screens reveal an essential extracellular role for hsp90α in cancer cell invasiveness

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The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

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Stress protein systems of mammalian cells

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Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1

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The common 90-kd protein component of non-transformed ‘8S’ steroid receptors is a heat-shock protein.

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OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD

Christianson, J. C., Shaler, T. A., Tyler, R. E., & Kopito, R. R. (2008) · Nature Cell Biology · doi:10.1038/ncb1689 · Cited by 509

The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains

Prodromou, C., Panaretou, B., Chohan, S., Siligardi, G., O'Brien, R., Ladbury, J. E., Roe, S. M., Piper, P. W., & Pearl, L. H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4383 · Cited by 492

Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491

Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.

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The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin

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Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches

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CHIP: a link between the chaperone and proteasome systems

McDonough, H., & Patterson, C. (2003) · Cell Stress & Chaperones · doi:10.1379/1466-1268(2003)008<0303:calbtc>2.0.co;2 · Cited by 468

Chaperones increase association of tau protein with microtubules

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Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers

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Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

Shiau, A. K., Harris, S. F., Southworth, D. R., & Agard, D. A. (2006) · Cell · doi:10.1016/j.cell.2006.09.027 · Cited by 455

The Hsp90 molecular chaperone: an open and shut case for treatment

Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447

4,5-Diarylisoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents for the Treatment of Cancer

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Regulation of Tumor Cell Mitochondrial Homeostasis by an Organelle-Specific Hsp90 Chaperone Network

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Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease

Sittler, A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.12.1307 · Cited by 442 · cited 1×

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

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NLR functions in plant and animal immune systems: so far and yet so close

Maekawa, T., Kufer, T. A., & Schulze-Lefert, P. (2011) · Nature Immunology · doi:10.1038/ni.2083 · Cited by 424

Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase

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Chaperoned Ubiquitylation—Crystal Structures of the CHIP U Box E3 Ubiquitin Ligase and a CHIP-Ubc13-Uev1a Complex

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Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

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An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function

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Successful Applications of Computer Aided Drug Discovery: Moving Drugs from Concept to the Clinic

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Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER

Stefanovic, S., & Hegde, R. S. (2007) · Cell · doi:10.1016/j.cell.2007.01.036 · Cited by 406

Novobiocin and Related Coumarins and Depletion of Heat Shock Protein 90-Dependent Signaling Proteins

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GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum

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The HSP90-SGT1 Chaperone Complex for NLR Immune Sensors

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Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro

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Glucose depletion accounts for the induction of two transformation-sensitive membrane proteinsin Rous sarcoma virus-transformed chick embryo fibroblasts.

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The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties

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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

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The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo

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The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37

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Hsp90 and Environmental Stress Transform the Adaptive Value of Natural Genetic Variation

Jarosz, D. F., & Lindquist, S. (2010) · Science · doi:10.1126/science.1195487 · Cited by 346

Rational design of shepherdin, a novel anticancer agent

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Microglial activation and amyloid‐β clearance induced by exogenous heat‐shock proteins

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Regulation of survivin function by Hsp90

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Structure and in vivo function of Hsp90

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Novobiocin and Additional Inhibitors of the Hsp90 C-Terminal Nucleotide- binding Pocket

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Update on Hsp90 Inhibitors in Clinical Trial

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Conformational dynamics of the molecular chaperone Hsp90

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A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.

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Structure of an Hsp90-Cdc37-Cdk4 Complex

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Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

Meyer, P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600141 · Cited by 291

Evolution and function of diverse Hsp90 homologs and cochaperone proteins

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Post-translational modifications of Hsp90 and their contributions to chaperone regulation

Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288

Targeting Hsp90: small-molecule inhibitors and their clinical development

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Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones

Dollins, D. E., Warren, J. J., Immormino, R. M., & Gewirth, D. T. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.024 · Cited by 281

Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies

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FK506 Binding Protein 5 Shapes Stress Responsiveness: Modulation of Neuroendocrine Reactivity and Coping Behavior

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Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50

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Structure-Activity Relationships in Purine-Based Inhibitor Binding to HSP90 Isoforms

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Identification of a Protein with Homology to hsp90 That Binds the Type 1 Tumor Necrosis Factor Receptor

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Discovery of (2,4-Dihydroxy-5-isopropylphenyl)-[5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl]methanone (AT13387), a Novel Inhibitor of the Molecular Chaperone Hsp90 by Fragment Based Drug Design

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Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance

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Structure and Functional Relationships of Hsp90

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Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90

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Protein Phosphatase 5 Is a Major Component of Glucocorticoid Receptor·hsp90 Complexes with Properties of an FK506-binding Immunophilin

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The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

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The Stress of Protein Misfolding: From Single Cells to Multicellular Organisms

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Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance

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Hsp90 and co‐chaperones twist the functions of diverse client proteins

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Heat shock protein 90 in neurodegenerative diseases

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Versatile TPR domains accommodate different modes of target protein recognition and function

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Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.

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Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

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Role of molecular chaperones in steroid receptor action

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Hsp90 and Cdc37 – a chaperone cancer conspiracy

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Novobiocin: Redesigning a DNA Gyrase Inhibitor for Selective Inhibition of Hsp90

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Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne

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Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90

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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

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Nucleotides and Two Functional States of hsp90

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Aha1 Binds to the Middle Domain of Hsp90, Contributes to Client Protein Activation, and Stimulates the ATPase Activity of the Molecular Chaperone

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Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen

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Systems Analysis of Protein Modification and Cellular Responses Induced by Electrophile Stress

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Hop: more than an Hsp70/Hsp90 adaptor protein

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The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop

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Novel, Potent Small-Molecule Inhibitors of the Molecular Chaperone Hsp90 Discovered through Structure-Based Design

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Akt and CHIP coregulate tau degradation through coordinated interactions

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Broad action of Hsp90 as a host chaperone required for viral replication

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The involvement of FK506-binding protein 51 (FKBP5) in the behavioral and neuroendocrine effects of chronic social defeat stress

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Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle

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Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins

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The Tetratricopeptide Repeat Domain of Protein Phosphatase 5 Mediates Binding to Glucocorticoid Receptor Heterocomplexes and Acts as a Dominant Negative Mutant

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Transforming Growth Factor α (TGFα)-Stimulated Secretion of HSP90α: Using the Receptor LRP-1/CD91 To Promote Human Skin Cell Migration against a TGFβ-Rich Environment during Wound Healing

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The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors

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CHIP: a quality-control E3 ligase collaborating with molecular chaperones

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The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules

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A Nucleotide-dependent Molecular Switch Controls ATP Binding at the C-terminal Domain of Hsp90

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Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways

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Ubiquitin–proteasome system and Parkinson's disease

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Coordinated ATP Hydrolysis by the Hsp90 Dimer

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Four Intracisternal Calcium-binding Glycoproteins from Rat Liver Microsomes with High Affinity for Calcium

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The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity

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Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage

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The Crystal Structure of the Carboxy-Terminal Dimerization Domain of htpG, the Escherichia coli Hsp90, Reveals a Potential Substrate Binding Site

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Crystal Structure and Molecular Modeling of 17-DMAG in Complex with Human Hsp90

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The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins

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Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function

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Cytoplasmic Localization of Pregnane X Receptor and Ligand-dependent Nuclear Translocation in Mouse Liver

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Heat Shock Protein 75 (TRAP1) Antagonizes Reactive Oxygen Species Generation and Protects Cells from Granzyme M-mediated Apoptosis

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Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone

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Fragment-Based Drug Discovery Applied to Hsp90. Discovery of Two Lead Series with High Ligand Efficiency

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NLR sensors meet at the SGT1–HSP90 crossroad

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Differential Control of Glucocorticoid Receptor Hormone-Binding Function by Tetratricopeptide Repeat (TPR) Proteins and the Immunosuppressive Ligand FK506

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A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion

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Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses

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Minireview: The Intersection of Steroid Receptors with Molecular Chaperones: Observations and Questions

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Combining Hit Identification Strategies: Fragment-Based and in Silico Approaches to Orally Active 2-Aminothieno[2,3-d]pyrimidine Inhibitors of the Hsp90 Molecular Chaperone

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Hsp90 Inhibitors Identified from a Library of Novobiocin Analogues

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Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis

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Targeting Wide-Range Oncogenic Transformation via PU24FCl, a Specific Inhibitor of Tumor Hsp90

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Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular Chaperone

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