Chrisostomos Prodromou

School of Life Sciences, University of Sussex

Research Area

Biography

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JoVE Journal Publications

ArticleTotal : 1	Year
Publication title Cited by 5	2023

Other Publications

Article	Year
Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors. Molecular cell\| PubMed ID: 20670895	2010
Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity. Molecular cell\| PubMed ID: 21419342	2011
The 'active life' of Hsp90 complexes. Biochimica et biophysica acta\| PubMed ID: 21840346	2012
Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity. Proceedings of the National Academy of Sciences of the United States of America\| PubMed ID: 22315411	2012
Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine. Molecular cell\| PubMed ID: 22727666	2012
Co-crystalization and in vitro biological characterization of 5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors. PloS one\| PubMed ID: 22984537	2012
CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression. Cell\| PubMed ID: 23217712	2012
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. PloS one\| PubMed ID: 23300914	2012
ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system. Nature chemical biology\| PubMed ID: 23502424	2013
Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90. Nature chemistry\| PubMed ID: 23511419	2013
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors. Molecular cell\| PubMed ID: 24462205	2014
Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993)\| PubMed ID: 24794838	2014
Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes. Acta crystallographica. Section D, Biological crystallography\| PubMed ID: 25945584	2015
c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells. Cell reports\| PubMed ID: 26235616	2015
Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors. Cell reports\| PubMed ID: 26804907	2016
Dihydropyridine Derivatives Modulate Heat Shock Responses and have a Neuroprotective Effect in a Transgenic Mouse Model of Alzheimer's Disease. Journal of Alzheimer's disease : JAD\| PubMed ID: 27163800	2016
Rapid Proteasomal Degradation of Mutant Proteins Is the Primary Mechanism Leading to Tumorigenesis in Patients With Missense AIP Mutations. The Journal of clinical endocrinology and metabolism\| PubMed ID: 27253664	2016
Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism. Nature chemical biology\| PubMed ID: 27322067	2016
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Nature communications\| PubMed ID: 27353360	2016
Mechanisms of Hsp90 regulation. The Biochemical journal\| PubMed ID: 27515256	2016
The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90. PloS one\| PubMed ID: 28278223	2017
HECTD3 Mediates an HSP90-Dependent Degradation Pathway for Protein Kinase Clients. Cell reports\| PubMed ID: 28636940	2017
The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System. Structure (London, England : 1993)\| PubMed ID: 28648606	2017
The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6. Human molecular genetics\| PubMed ID: 28973376	2017
Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System. Cell reports\| PubMed ID: 29091774	2017
Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients. The EMBO journal\| PubMed ID: 29127155	2017
The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6. Human molecular genetics\| PubMed ID: 29351602	2018
The Stoichiometric Interaction of the Hsp90-Sgt1-Rar1 Complex by CD and SRCD Spectroscopy. Frontiers in molecular biosciences\| PubMed ID: 29387685	2017
Multi-chaperone function modulation and association with cytoskeletal proteins are key features of the function of AIP in the pituitary gland. Oncotarget\| PubMed ID: 29507682	2018
bioassay to test the pathogenicity of missense human variants. Journal of medical genetics\| PubMed ID: 29632148	2018
RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nature communications\| PubMed ID: 29662061	2018
Dihydropyridines Allosterically Modulate Hsp90 Providing a Novel Mechanism for Heat Shock Protein Co-induction and Neuroprotection. Frontiers in molecular biosciences\| PubMed ID: 29930942	2018
Author Correction: RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nature communications\| PubMed ID: 30065299	2018
Advances on the Structure of the R2TP/Prefoldin-like Complex. Advances in experimental medicine and biology\| PubMed ID: 30484153	2018
Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90. Cell reports\| PubMed ID: 30699359	2019
Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM. Science advances\| PubMed ID: 31049401	2019
Chemical Perturbation of Oncogenic Protein Folding: from the Prediction of Locally Unstable Structures to the Design of Disruptors of Hsp90-Client Interactions. Chemistry (Weinheim an der Bergstrasse, Germany)\| PubMed ID: 32167602	2020
Editorial: The Role of Heat Shock Proteins in Neuroprotection. Frontiers in pharmacology\| PubMed ID: 32848805	2020
Clinical and functional analyses of AIPL1 variants reveal mechanisms of pathogenicity linked to different forms of retinal degeneration. Scientific reports\| PubMed ID: 33067476	2020
The structure-function relationship of oncogenic LMTK3. Science advances\| PubMed ID: 33188023	2020
Structure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone. Cell reports\| PubMed ID: 34233195	2021
Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics. Nature communications\| PubMed ID: 34845214	2021
Advances towards Understanding the Mechanism of Action of the Hsp90 Complex. Biomolecules\| PubMed ID: 35625528	2022
Recognition of BRAF by CDC37 and Re-Evaluation of the Activation Mechanism for the Class 2 BRAF-L597R Mutant. Biomolecules\| PubMed ID: 35883461	2022
HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease. Sub-cellular biochemistry\| PubMed ID: 36520314	2023