Protein Kinase CK2 in Health and Disease: CK2: The kinase controlling the Hsp90 chaperone machinery

HSP90 and the chaperoning of cancer

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Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*

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One‐thousand‐and‐one substrates of protein kinase CK2?

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Protein kinase CK2: structure, regulation and role in cellular decisions of life and death

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Pathways of chaperone-mediated protein folding in the cytosol

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Heat shock proteins in cancer: chaperones of tumorigenesis

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Hsp90

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Heat-shock protein 90, a chaperone for folding and regulation

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Akt Forms an Intracellular Complex with Heat Shock Protein 90 (Hsp90) and Cdc37 and Is Destabilized by Inhibitors of Hsp90 Function

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Hsp90 & Co. – a holding for folding

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Heat shock protein 90 as a molecular target for cancer therapeutics

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Hsp90: Chaperoning signal transduction

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The Hsp90 Chaperone Machinery

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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 · see citing works

THE SELECTION OF S. CEREVISIAE MUTANTS DEFECTIVE IN THE START EVENT OF CELL DIVISION

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A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells

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

Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg108 · Cited by 353 · see citing works

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

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Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation

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The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity.

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Inhibitors of the HSP90 Molecular Chaperone: Current Status

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Structure of an Hsp90-Cdc37-Cdk4 Complex

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Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila

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

Siligardi, G., Panaretou, B., Meyer, P., Singh, S., Woolfson, D. N., Piper, P. W., Pearl, L. H., & Prodromou, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201287200 · Cited by 272 · see citing works

Structure and Functional Relationships of Hsp90

Prodromou, C., & Pearl, L. H. (2003) · Current Cancer Drug Targets · doi:10.2174/1568009033481877 · Cited by 262 · see citing works

p50cdc37 Acting in Concert with Hsp90 Is Required for Raf-1 Function

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Chaperoning of Glucocorticoid Receptors

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Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone

Workman, P. (2003) · Cancer Letters · doi:10.1016/j.canlet.2003.08.032 · Cited by 245 · see citing works

Hsp90 and Cdc37 – a chaperone cancer conspiracy

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Clinical Development of 17-Allylamino, 17-Demethoxygeldanamycin

Sausville, E. A., Tomaszewski, J. E., & Ivy, P. S. (2003) · Current Cancer Drug Targets · doi:10.2174/1568009033481831 · Cited by 225 · see citing works

Physiological role for the cochaperone FKBP52 in androgen receptor signaling

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Molecular chaperones: assisting assembly in addition to folding

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Cdc37 is a molecular chaperone with specific functions in signal transduction.Preprint

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Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37

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Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II

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Altered states: selectively drugging the Hsp90 cancer chaperone

Workman, P. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2003.12.005 · Cited by 195 · see citing works

Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases

Schiene-Fischer, C., & Yu, C. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02326-2 · Cited by 190 · see citing works

Chaperoning steroid hormone action

Picard, D. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.06.003 · Cited by 186 · see citing works

Molecular chaperones and protein kinase quality control

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The Human Double-stranded DNA-activated Protein Kinase Phosphorylates the 90-kDa Heat-shock Protein, hsp90α at Two NH2-terminal Threonine Residues

Lees‐Miller, S. P., & Anderson, C. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71488-9 · Cited by 182 · see citing works

Hsp90: A Novel Target for Cancer Therapy

Solit, D. B., & Rosen, N. X. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606777812068 · Cited by 171 · see citing works

Essential role for co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiology

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CK2 Controls Multiple Protein Kinases by Phosphorylating a Kinase-Targeting Molecular Chaperone, Cdc37

Miyata, Y., & Nishida, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.4065-4074.2004 · Cited by 149 · see citing works

Protein phosphatase 5

Hinds, T. D., & Sánchez, E. R. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.08.010 · Cited by 149 · see citing works

Inhibition of Hsp90: a new strategy for inhibiting protein kinases

Sreedhar, A. S., Sőti, C., & Csermely, P. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.027 · Cited by 148 · see citing works

Hsp90 Inhibitor Geldanamycin and Its Derivatives as Novel Cancer Chemotherapeutic Agents

Miyata, Y. (2005) · Current Pharmaceutical Design · doi:10.2174/1381612053507585 · Cited by 147 · see citing works

Immunophilin Chaperones in Steroid Receptor Signalling

Ratajczak, T., Ward, B. K., & Minchin, R. F. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033451934 · Cited by 137 · see citing works

Targeting the oncogene and kinome chaperone CDC37

Gray, P. J., Prince, T. L., Cheng, J., Stevenson, M. A., & Calderwood, S. K. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2420 · Cited by 136 · see citing works

Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins.

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Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors

Smith, J. R., Clarke, P. A., de Billy, E., & Workman, P. (2008) · Oncogene · doi:10.1038/onc.2008.380 · Cited by 134 · see citing works

Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52

Miyata, Y., Chambraud, B., Radanyi, C., Leclerc, J., Lebeau, M.-C., Renoir, J.-M., Shirai, R., Catelli, M.-G., Yahara, I., & Baulieu, E.-E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14500 · Cited by 121 · see citing works

Protein kinase CK2: a new view of an old molecular complex

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Interaction between casein kinase II and the 90-kDa stress protein, HSP90

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p23, a simple protein with complex activities

Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116 · see citing works

Cdc37: a protein kinase chaperone?

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A filamentous form of Drosophila casein kinase II.

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Phosphorylation of Serine 13 Is Required for the Proper Function of the Hsp90 Co-chaperone, Cdc37

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Targeting Cdc37 Inhibits Multiple Signaling Pathways and Induces Growth Arrest in Prostate Cancer Cells

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Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation

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A Positive Feedback Loop between Protein Kinase CKII and Cdc37 Promotes the Activity of Multiple Protein Kinases

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Possible Role for Serine/Threonine Phosphorylation in the Regulation of the Heteroprotein Complex between the hsp90 Stress Protein and the pp60v-src Tyrosine Kinase

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Hsp90 Phosphorylation Is Linked to Its Chaperoning Function

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CK2A Protein Kinase in Need of Control

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The Oncoprotein Kinase Chaperone CDC37 Functions as an Oncogene in Mice and Collaborates with Both c- myc and Cyclin D1 in Transformation of Multiple Tissues

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Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified Chaperones

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Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia

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Functional Dissection of Cdc37: Characterization of Domain Structure and Amino Acid Residues Critical for Protein Kinase Binding

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Hsp90 Regulates p50 Function during the Biogenesis of the Active Conformation of the Heme-regulated eIF2α Kinase

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Natural Product Origins of Hsp90 Inhibitors

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Chaperoning Oncogenes: Hsp90 as a Target of Geldanamycin

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Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90

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Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors

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CDC37 is required for p60v-src activity in yeast.

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A 50 Kilodalton Protein Associated with Raf and pp60v-src Protein Kinases Is a Mammalian Homolog of the Cell Cycle Control Protein cdc37

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The Cdc37 protein kinase–binding domain is sufficient for protein kinase activity and cell viability

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Cdc37p Is Required for Stress-Induced High-Osmolarity Glycerol and Protein Kinase C Mitogen-Activated Protein Kinase Pathway Functionality by Interaction with Hog1p and Slt2p (Mpk1p)

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The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 .alpha. subunit by the heme-sensitive kinase

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FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity

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Genes and Proteins Governing the Cellular Sensitivity to HSP90 Inhibitors: A Mechanistic Perspective

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The molecular chaperone Cdc37 is required for Ste11 function and pheromone‐induced cell cycle arrest

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A Proteomic Screen Identified Stress-Induced Chaperone Proteins as Targets of Akt Phosphorylation in Mesangial Cells

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Heat-Shock Protein 90 Inhibitors in Cancer Therapy: 17AAG and Beyond

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Differential In Vivo Regulation of Steroid Hormone Receptor Activation by Cdc37p

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Cdc37 enhances proliferation and is necessary for normal human prostate epithelial cell survival.

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Signal transduction: Gyrating protein kinases

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Analysis of the CK2‐dependent phosphorylation of serine 13 in Cdc37 using a phospho‐specific antibody and phospho‐affinity gel electrophoresis

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Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37

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Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat‐shock protein 90

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Casein kinases and their protein substrates in rat liver cytosol: Evidence for their participation in multimolecular systems

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Multiple Kinases and System Robustness: A Link Between Cdc37 and Genome Integrity

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Supervision of Multiple Signaling Protein Kinases by the CK2‐Cdc37 Couple, a Possible Novel Cancer Therapeutic Target

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Targeting the dynamic HSP90 complex in cancer

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The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

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Protein kinase CK2: a potential therapeutic target for diverse human diseases

Borgo, C., D’Amore, C., Sarno, S., Salvi, M., & Ruzzene, M. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00567-7 · Cited by 369 · see citing works

Mechanisms of Hsp90 regulation

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

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C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances

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Heat Shock Protein 90 Inhibitors: An Update on Achievements, Challenges, and Future Directions

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Hybrid Drugs—A Strategy for Overcoming Anticancer Drug Resistance?

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Emergence of protein kinase CK2 as a key target in cancer therapy

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Hsp90: Breaking the Symmetry

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Targeting Protein Kinase CK2 Suppresses Prosurvival Signaling Pathways and Growth of Glioblastoma

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Apigenin inhibits proliferation and induces apoptosis in human multiple myeloma cells through targeting the trinity of CK2, Cdc37 and Hsp90

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Role of protein kinase CK2 in antitumor drug resistance

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CK2—An Emerging Target for Neurological and Psychiatric Disorders

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Dual action antifungal small molecule modulates multidrug efflux and TOR signaling

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Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment

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CK2 Inhibitor CX-4945 Suppresses DNA Repair Response Triggered by DNA-Targeted Anticancer Drugs and Augments Efficacy: Mechanistic Rationale for Drug Combination Therapy

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches

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Protein Kinase CK2 Inhibition Down Modulates the NF-κB and STAT3 Survival Pathways, Enhances the Cellular Proteotoxic Stress and Synergistically Boosts the Cytotoxic Effect of Bortezomib on Multiple Myeloma and Mantle Cell Lymphoma Cells

Manni, S., Brancalion, A., Mandato, E., Tubi, L. Q., Colpo, A., Pizzi, M., Cappellesso, R., Zaffino, F., Maggio, S. A. D., Cabrelle, A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075280 · Cited by 92 · see citing works

Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy

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Protein Kinase CK2 Protects Multiple Myeloma Cells from ER Stress–Induced Apoptosis and from the Cytotoxic Effect of HSP90 Inhibition through Regulation of the Unfolded Protein Response

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Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90

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Cellular regulators of protein kinase CK2

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Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress

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Phosphoproteomic Analysis Reveals Site-Specific Changes in GFAP and NDRG2 Phosphorylation in Frontotemporal Lobar Degeneration

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Combined inhibition of EGFR and CK2 augments the attenuation of PI3K-Akt-mTOR signaling and the killing of cancer cells

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Potential Use of Selective and Nonselective Pim Kinase Inhibitors for Cancer Therapy

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ck2-Dependent Phosphorylation of Progesterone Receptors (PR) on Ser81 Regulates PR-B Isoform-Specific Target Gene Expression in Breast Cancer Cells

Hagan, C. R., Regan, T. M., Dressing, G. E., & Lange, C. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01246-10 · Cited by 69 · see citing works

Small molecules targeting protein–protein interactions for cancer therapy

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Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity

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Hsp90 in Cancer

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Alternative approaches to Hsp90 modulation for the treatment of cancer

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Simultaneous blockade of interacting CK2 and EGFR pathways by tumor-targeting nanobioconjugates increases therapeutic efficacy against glioblastoma multiforme

Chou, S., Patil, R., Galstyan, A., Gangalum, P. R., Cavenee, W. K., Furnari, F. B., Ljubimov, V. A., Chesnokova, A., Kramerov, A. A., Ding, H., et al. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.11.001 · Cited by 53 · see citing works

Single-Step Inline Hydroxyapatite Enrichment Facilitates Identification and Quantitation of Phosphopeptides from Mass-Limited Proteomes with MudPIT

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A CK2-targeted Pt(IV) prodrug to disrupt DNA damage response

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Antitumoral activity of allosteric inhibitors of protein kinase CK2

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CK2 and the Hallmarks of Cancer

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Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration

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Role of protein kinases CK1α and CK2 in multiple myeloma: regulation of pivotal survival and stress-managing pathways

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Protein kinase CK2 is widely expressed in follicular, Burkitt and diffuse large B-cell lymphomas and propels malignant B-cell growth

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Identification of Leishmania‐ specific protein phosphorylation sites by LC‐ESI‐MS/MS and comparative genomics analyses

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Protein kinase CK2 inhibition as a pharmacological strategy

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Targeting CK2-driven non-oncogene addiction in B-cell tumors

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Isoform-Specific Phosphorylation in Human Hsp90β Affects Interaction with Clients and the Cochaperone Cdc37

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Reversal of cisplatin resistance in human gastric cancer cells by a wogonin-conjugated Pt(IV) prodrug via attenuating Casein Kinase 2-mediated Nuclear Factor-κB pathways

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Casein Kinase 2 (CK2)-mediated Phosphorylation of Hsp90β as a Novel Mechanism of Rifampin-induced MDR1 Expression

Kim, S. W., Hasanuzzaman, M., Cho, M., Heo, Y. R., Ryu, M., Ha, N.-Y., Park, H. J., Park, H., & Shin, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624106 · Cited by 34 · see citing works

LPS induces pp60 c-src -mediated tyrosine phosphorylation of Hsp90 in lung vascular endothelial cells and mouse lung

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Chaperones and multitasking proteins in the nucleolus: networking together for survival?

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Regulatory Mechanisms of Hsp90

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Autophagosome-Mediated EGFR Down-Regulation Induced by the CK2 Inhibitor Enhances the Efficacy of EGFR-TKI on EGFR-Mutant Lung Cancer Cells with Resistance by T790M

So, K. S., Kim, C. H., Rho, J. K., Kim, S. Y., Choi, Y. J., Song, J. S., Kim, W. S., Choi, C., Chun, Y. J., & Lee, J. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114000 · Cited by 29 · see citing works

Protein kinase CK2 inhibition is associated with the destabilization of HIF-1α in human cancer cells

Guerra, B., Rasmussen, T., Schnitzler, A., Jensen, H. H., Boldyreff, B., Miyata, Y., Marcussen, N., Niefind, K., & Issinger, O. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.10.026 · Cited by 28 · see citing works

Nuclear localization of the CK2α-subunit correlates with poor prognosis in clear cell renal cell carcinoma

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Signaling Pathways, Chemical and Biological Modulators of Nucleotide Excision Repair: The Faithful Shield against UV Genotoxicity

Kobaisi, F., Fayyad, N., Rezvani, H. R., Fayyad‐Kazan, M., Sulpice, E., Badran, B., Fayyad‐Kazan, H., Gidrol, X., & Rachidi, W. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/4654206 · Cited by 27 · see citing works

Targeting Protein Kinases in Blood Cancer: Focusing on CK1α and CK2

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Endocrine disrupting chemicals interfere with decidualization of human primary endometrial stromal cells in vitro

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Protein kinase CK2 accumulation in “oncophilic” cells: causes and effects

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The kinase inhibitor D11 induces caspase-mediated cell death in cancer cells resistant to chemotherapeutic treatment

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Functional Role and Hierarchy of the Intermolecular Interactions in Binding of Protein Kinase Clients to the Hsp90–Cdc37 Chaperone: Structure-Based Network Modeling of Allosteric Regulation

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BIRC6 mediates imatinib resistance independently of Mcl-1

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The driver of malignancy in KG-1a leukemic cells, FGFR1OP2–FGFR1, encodes an HSP90 addicted oncoprotein

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The Interactome of Protein Kinase CK2

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AhR promotes phosphorylation of ARNT isoform 1 in human T cell malignancies as a switch for optimal AhR activity

Bourner, L. A., Muro, I., Cooper, A. M., Choudhury, B. K., Bailey, A. O., Russell, W. K., Khanipov, K., Golovko, G., & Wright, C. W. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114336119 · Cited by 15 · see citing works

Modulation of transcriptional mineralocorticoid receptor activity by casein kinase 2

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Genetic analysis of Hsp70 phosphorylation sites reveals a role in Candida albicans cell and colony morphogenesis

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Protein kinase CK2 regulates redox homeostasis through NF-κB and Bcl-xL in cardiomyoblasts

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Chemical proteomics and functional proteomics strategies for protein kinase inhibitor validation and protein kinase substrate identification: Applications to protein kinase CK2

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Phosphorylated and Unphosphorylated Serine 13 of CDC37 Stabilize Distinct Interactions between Its Client and HSP90 Binding Domains

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Modulation of the Glucocorticoid Receptor Activity by Post-Translational Modifications

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Phosphotyrosine Confers Client Specificity to Hsp90

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The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis

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Interactions between subunits of protein kinase CK2 and their protein substrates influences its sensitivity to specific inhibitors

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Casein kinase 2, a versatile regulator of cell surviva

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Casein kinase II–dependent phosphorylation of DNA topoisomerase II suppresses the effect of a catalytic topo II inhibitor, ICRF-193, in fission yeast

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P23 Acts as Functional RBP in the Macrophage Inflammation Response

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Structure‐Based Pharmacophore Modeling from Multicomplex: a Comprehensive Pharmacophore Generation of Protein Kinase CK2 and Virtual Screening Based on it for Novel Inhibitors

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Systematic identification of novel SLE related autoantibodies responsible for type I IFN production in human plasmacytoid dendritic cells

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Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity

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Chaperones and Multitasking Proteins in the Nucleolus

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D11-Mediated Inhibition of Protein Kinase CK2 Impairs HIF-1α-Mediated Signaling in Human Glioblastoma Cells

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CK2: The master regulator in tumor immune-microenvironment - A crucial target in oncotherapy

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Analyzing the interactome of human CK2β in prostate carcinoma cells reveals HSP70 ‐1 and Rho guanin nucleotide exchange factor 12 as novel interaction partners

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Overview of Molecular Chaperones in Health and Disease

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Effects of CK2 inhibition in cultured fibroblasts from Type 1 Diabetic patients with or without nephropathy

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Stimulation of CK2-dependent Grp94 phosphorylation by the nuclear localization signal peptide

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Genomic regions associated with bovine respiratory disease in pacific northwest Holstein cattle

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CK2 as a Logical Target in Cancer Therapy: Potential for Combining CK2 Inhibitors with Various Classes of Cancer Therapeutic Agents

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Circumventing drug resistance through a CK2-targeted combination via attenuating endogenous AhR-TLS-promoted genomic instability in human colorectal cancer cells

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Structure-Guided Discovery of Adenosine Triphosphate-Competitive Casein Kinase 2 Inhibitors

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The Pivotal Role of CK2 in the Kinome‐Targeting Hsp90 Chaperone Machinery

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Defining the role of HSP90 in the stability of FGFR3 and as a drug target for the treatment of skeletal diseases and cancer

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Sensitivity of Protein Kinase CK2 to ATP/GTP and Specific Inhibitors Depends on Complexity of Interacting Proteins

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Screening Technique for Heat Shock Protein 90 Inhibitors from Natural Products

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Signalomics : unsupervised and global strategies to explore mechanisms of radioresistence in lung cancer cells

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The Cancer Super-chaperone Hsp90: Drug Targeting and Post-translational Regulation

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Utilizing a Microbial Natural Product to Investigate Cellular Circuitry Governing Fungal Drug Resistance and Morphogenesis

Shekhar‐Guturja, T. (2016) · TSpace (University of Toronto)

Investigation of Hsp90 Regulation by the Aha-type Co-chaperones: Mechanistic Insight into Two Conserved Motifs

Mercier, R. J. (2019) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3-tms0-be49

RNAi and Chemical-Based High Content Screening for the Normalization of XPC Phenotyope

Kobaisi, F. (2021) · theses.fr (ABES) · doi:10.70675/e34b8c43z081az4c41zad64z8e0c753e5c20

BindingDB Entry 50009294: Heat Shock Protein 90 Inhibitors: An Update on Achievements, Challenges, and Future Directions.

BindingDB (2021) · UC San Diego · doi:10.7270/q23x8b3c

BindingDB Entry 50040677: Potential use of selective and nonselective Pim kinase inhibitors for cancer therapy.

BindingDB (2013) · UC San Diego · doi:10.7270/q2930v9t

CK2 Inhibitors and the DYRK Family Protein Kinases

Miyata, Y. (2015) · Springer eBooks · doi:10.1007/978-3-319-14544-0_19

CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone

Miyata, Y., & Nishida, E. (2005) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-005-2949-8 · Cited by 50 · see citing works

Hsp90 and Cdc37 – a chaperone cancer conspiracy

Pearl, L. H. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.011 · Cited by 241 · see citing works

CK2 Controls Multiple Protein Kinases by Phosphorylating a Kinase-Targeting Molecular Chaperone, Cdc37

Miyata, Y., & Nishida, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.4065-4074.2004 · Cited by 149 · see citing works

Cdk2: A Genuine Protein Kinase Client of Hsp90 and Cdc37

Prince, T. L., Sun, L., & Matts, R. L. (2005) · Biochemistry · doi:10.1021/bi051423m · Cited by 58 · see citing works

Cdc37 as a Co-chaperone to Hsp90

Prince, T. L., Lang, B. J., Okusha, Y., Eguchi, T., & Calderwood, S. K. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_5 · Cited by 12 · see citing works