Chrisostomos Prodromou

Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors.

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity.

The 'active life' of Hsp90 complexes.

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity.

Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.

Co-crystalization and in vitro biological characterization of 5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors.

CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression.

Structure of the TPR domain of AIP: lack of client protein interaction with the C-terminal α-7 helix of the TPR domain of AIP is sufficient for pituitary adenoma predisposition.

ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.

Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90.

Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.

Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.

Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.

c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.

Dihydropyridine Derivatives Modulate Heat Shock Responses and have a Neuroprotective Effect in a Transgenic Mouse Model of Alzheimer's Disease.

Rapid Proteasomal Degradation of Mutant Proteins Is the Primary Mechanism Leading to Tumorigenesis in Patients With Missense AIP Mutations.

Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.

Mechanisms of Hsp90 regulation.

The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90.

HECTD3 Mediates an HSP90-Dependent Degradation Pathway for Protein Kinase Clients.

The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System.

The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6.

Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System.

Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.

The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6.

The Stoichiometric Interaction of the Hsp90-Sgt1-Rar1 Complex by CD and SRCD Spectroscopy.

Multi-chaperone function modulation and association with cytoskeletal proteins are key features of the function of AIP in the pituitary gland.

bioassay to test the pathogenicity of missense human variants.

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.

Dihydropyridines Allosterically Modulate Hsp90 Providing a Novel Mechanism for Heat Shock Protein Co-induction and Neuroprotection.

Author Correction: RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.

Advances on the Structure of the R2TP/Prefoldin-like Complex.

Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90.

Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM.

Chemical Perturbation of Oncogenic Protein Folding: from the Prediction of Locally Unstable Structures to the Design of Disruptors of Hsp90-Client Interactions.

Editorial: The Role of Heat Shock Proteins in Neuroprotection.

Clinical and functional analyses of AIPL1 variants reveal mechanisms of pathogenicity linked to different forms of retinal degeneration.

The structure-function relationship of oncogenic LMTK3.

Structure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone.

Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics.

Advances towards Understanding the Mechanism of Action of the Hsp90 Complex.

Recognition of BRAF by CDC37 and Re-Evaluation of the Activation Mechanism for the Class 2 BRAF-L597R Mutant.

HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease.