C. Prodromou

发表

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

S. Landas, W. Stetler-Stevenson, L. Neckers, 2015, Cell reports.

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

Alessandro Gori, Marina Cretich, Giorgio Colombo, 2020, Chemistry.

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

M. Korbonits, F. D’Acquisto, R. Morgan, 2018, Oncotarget.

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

L. Pearl, P. Piper, J. Ladbury, 1997, Cell.

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

L. Pearl, P. Piper, S. Roe, 2006, Nature.

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

L. Pearl, P. Workman, C. Prodromou, 2008, The Biochemical journal.

The ‘active life’ of Hsp90 complexes☆

C. Prodromou, 2012, Biochimica et biophysica acta.

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

L. Pearl, P. Piper, J. Ladbury, 1999, Journal of medicinal chemistry.

A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s

L. Pearl, P. Piper, C. Prodromou, 2009, The FEBS journal.

Structure and mechanism of the Hsp90 molecular chaperone machinery.

L. Pearl, C. Prodromou, 2006, Annual review of biochemistry.

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

L. Pearl, P. Piper, S. Roe, 2004, Cell.

4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer.

Mike Wood, Brian Dymock, Xavier Barril, 2007, Journal of medicinal chemistry.

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.

Paul Workman, Rainer Cramer, Chrisostomos Prodromou, 2002, Molecular cell.

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.

Chrisostomos Prodromou, Bin Hu, Philippe Meyer, 2003, Molecular cell.

Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.

L. Pearl, P. Piper, W. Stetler-Stevenson, 2010, Molecular cell.

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

M. Michaelides, J. Bellingham, C. Prodromou, 2017, Human molecular genetics.

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

M. Michaelides, J. Bellingham, C. Prodromou, 2018, Human molecular genetics.

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

W. Linehan, L. Schmidt, T. Haystead, 2019, Cell reports.

Expression and crystallization of the yeast Hsp82 chaperone, and preliminary x‐ray diffraction studies of the amino‐terminal domain

L. Pearl, P. Piper, C. Prodromou, 1996, Proteins.

“Tuning” the ATPase Activity of Hsp90

R. Morgan, C. Prodromou, 2016 .

Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50 cdc37 *

L. Pearl, P. Piper, D. Woolfson, 2002, The Journal of Biological Chemistry.

Mps 1 Mediated Phosphorylation of Hsp 90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp 90 Inhibitors Graphical

S. Landas, W. Stetler-Stevenson, L. Neckers, 2016 .

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

S. Landas, W. Stetler-Stevenson, L. Neckers, 2016, Cell reports.

Differential Regulation of G 1 CDK Complexes by the Hsp 90-Cdc 37 Chaperone System

L. Pearl, M. Noble, J. Endicott, 2019 .

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

L. Pearl, M. Noble, J. Endicott, 2017, Cell reports.

NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis.

L. Pearl, X. Barril, M. Drysdale, 2008, Cancer research.

HECTD 3 Mediates an HSP 90-Dependent Degradation Pathway for Protein Kinase Clients Graphical

L. Pearl, C. Prodromou, Zhaobo Li, 2017 .

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

L. Pearl, C. Prodromou, Zhaobo Li, 2017, Cell reports.

Targeting the Hsp90 molecular chaperone with novel macrolactams. Synthesis, structural, binding, and cellular studies.

L. Pearl, P. Workman, W. Aherne, 2011, ACS chemical biology.

A simple yeast-based system for analyzing inhibitor resistance in the human cancer drug targets Hsp90alpha/beta.

P. Piper, C. Prodromou, S. Millson, 2010, Biochemical pharmacology.

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

Paul Workman, Edward McDonald, Chrisostomos Prodromou, 2005, Bioorganic & medicinal chemistry letters.

The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases.

P. Artymiuk, C. Prodromou, J. Guest, 1992, European journal of biochemistry.

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

L. Pearl, S. Roe, R. Morgan, 2014, Acta crystallographica. Section D, Biological crystallography.

Molecular characterization of macbecin as an Hsp90 inhibitor.

Christine J. Martin, M. Gregory, S. Gaisser, 2008, Journal of medicinal chemistry.

CDK-Dependent Hsp 70 Phosphorylation Controls G 1 Cyclin Abundance and Cell-Cycle Progression

Gary W. Jones, K. Kristjánsdóttir, S. Kron, 2012 .

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

Philip F. Hughes, L. Schmidt, T. Haystead, 2016, Nature Communications.

Letter to the Editor: Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone

L. Pearl, R. Salek, Mark A. Williams, 2002, Journal of Biomolecular NMR.

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited.Thislicens

L. Pearl, C. Prodromou, B. Panaretou, 2008 .

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes

L. Pearl, K. Shirasu, C. Prodromou, 2008, The EMBO journal.

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

R. Morgan, C. Prodromou, J. Oberoi, 2022, bioRxiv.

Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins

L. Pearl, P. Workman, P. Clarke, 2013, Oncogene.

The Hsp90 mosaic: a picture emerges

J. Frydman, M. Mayer, C. Prodromou, 2009, Nature Structural &Molecular Biology.

Regulatory mechanisms of Hsp 90

C. Prodromou, 2019 .

Regulatory Mechanisms of Hsp90

C. Prodromou, 2017, Biochemistry & molecular biology journal.

Advances towards Understanding the Mechanism of Action of the Hsp90 Complex

C. Prodromou, Dennis M. Bjorklund, 2022, Biomolecules.

Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism

L. Pearl, H. Neuweiler, C. Prodromou, 2016, Nature chemical biology.

Post-translational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors

D. Bolon, L. Neckers, Tony Taldone, 2013, Oncotarget.

Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors.

D. Bolon, L. Neckers, Tony Taldone, 2013 .

Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors

L. Pearl, K. Shirasu, C. Prodromou, 2010, Molecular cell.

Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors.

L. Pearl, P. Piper, A. Truman, 2003, Gene.

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

L. Pearl, P. Piper, L. Neckers, 2008, Molecular cell.

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

Y. Miyata, L. Neckers, J. Trepel, 2012, Molecular cell.

Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1

L. Pearl, S. Roe, C. Prodromou, 2014, Structure.

The structure-function relationship of oncogenic LMTK3

L. Pearl, R. Owens, H. Lenz, 2020, Science Advances.

A combinatorial method to enable detailed investigation of protein-protein interactions.

L. Pearl, K. Maclagan, P. Driscoll, 2011, Future medicinal chemistry.

Cloning of theHIS3 gene ofYarrowia lipolytica

C. Prodromou, I. Evans, E. Bevan, 1991, Antonie van Leeuwenhoek.

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

D. Gutmann, D. Bourboulia, A. Blanden, 2017, The EMBO journal.

Synthesis of a modified gene encoding human ornithine transcarbamylase for expression in mammalian mitochondrial and universal translation systems: a novel approach towards correction of a genetic defect.

L. Pearl, R. Williamson, C. Prodromou, 1996, Gene.

AlphaFold predicted structure of the Hsp90-like domains of the neurodegeneration linked protein sacsin reveals key residues for ATPase activity

G. Colombo, C. Prodromou, Matteo Castelli, 2022, bioRxiv.

Inhibition of Hsp90 with resorcylic acid macrolactones: synthesis and binding studies.

L. Pearl, P. Workman, W. Aherne, 2010, Chemistry.

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

L. Pearl, G. Degliesposti, Rebecca F. Thompson, 2020, bioRxiv.

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

L. Pearl, G. Degliesposti, D. Gil-Carton, 2017, Structure.

Structural basis of the radicicol resistance displayed by a fungal hsp90.

L. Pearl, P. Piper, P. Workman, 2009, ACS chemical biology.

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

L. Pearl, C. Prodromou, O. Llorca, 2018, Advances in experimental medicine and biology.

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

R. Morgan, C. Prodromou, J. Oberoi, 2022, bioRxiv.

Regulation of Hsp 90 ATPase Activity by the Co-chaperone Cdc 37 p / p 50 cdc 37

L. Pearl, P. Piper, D. Woolfson, 2002 .

Strategies for stalling malignancy: targeting cancer's addiction to Hsp90.

C. Prodromou, 2009, Current topics in medicinal chemistry.

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

M. Korbonits, S. Roe, R. Morgan, 2012, PloS one.

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

David Siegel, William Lewis, Chrisostomos Prodromou, 2013, Nature chemistry.

Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol.

Paul Workman, Chrisostomos Prodromou, Laurence H Pearl, 2006, Chemistry & biology.

High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity.

L. Pearl, P. Workman, W. Aherne, 2004, Analytical biochemistry.

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

L. Pearl, G. Degliesposti, D. Gil-Carton, 2018, Nature Communications.

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

L. Pearl, C. Prodromou, O. Llorca, 2019, Science Advances.

Chaperone ligand-discrimination by the TPR-domain protein Tah1

L. Pearl, P. Piper, C. Prodromou, 2008, The Biochemical journal.

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

I. Horváth, Z. Török, C. Prodromou, 2018, Front. Mol. Biosci..

A Two-Hybrid Screen of the Yeast Proteome for Hsp90 Interactors Uncovers a Novel Hsp90 Chaperone Requirement in the Activity of a Stress-Activated Mitogen-Activated Protein Kinase, Slt2p (Mpk1p)

L. Pearl, P. Piper, A. Truman, 2005, Eukaryotic Cell.

Mechanisms of Hsp 90 regulation

C. Prodromou, 2017 .

Mechanisms of Hsp90 regulation

C. Prodromou, 2016, The Biochemical journal.

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

W. Stetler-Stevenson, L. Neckers, D. Bourboulia, 2014, Molecular cell.

Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast.

Chrisostomos Prodromou, Mehdi Mollapour, Giuliano Siligardi, 2003, European journal of biochemistry.

Structure and in vivo function of Hsp90.

L. Pearl, C. Prodromou, Laurence H. Pearl, 2000, Current opinion in structural biology.

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

L. Pearl, P. Piper, J. Ladbury, 1998, The EMBO journal.

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

Chrisostomos Prodromou, Ronan O'Brien, Giuliano Siligardi, 2000, The EMBO journal.

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

L. Pearl, S. Roe, C. Prodromou, 2017, PloS one.

Features of the Streptomyces hygroscopicus HtpG reveal how partial geldanamycin resistance can arise with mutation to the ATP binding pocket of a eukaryotic Hsp90

L. Pearl, P. Piper, S. Roe, 2011, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Structure of an Hsp90-Cdc37-Cdk4 complex.

L. Pearl, C. Robinson, H. Saibil, 2006, Molecular cell.

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

Chrisostomos Prodromou, Lynne Regan, Ronan O'Brien, 1999, The EMBO journal.

Structure, function, and mechanism of the Hsp90 molecular chaperone.

L. Pearl, C. Prodromou, Laurence H. Pearl, 2001, Advances in protein chemistry.

Synthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90.

S. Roe, C. Prodromou, C. Moody, 2014, Organic & biomolecular chemistry.

Structure of an Hsp 90-Cdc 37-Cdk 4 complex

L. Pearl, C. Robinson, H. Saibil, 2017 .

Optimizing natural products by biosynthetic engineering: discovery of nonquinone Hsp90 inhibitors.

Mohammad Nur-E-Alam, Christine J. Martin, Sabine Gaisser, 2008, Journal of medicinal chemistry.

In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors.

L. Pearl, P. Workman, R. Marais, 2007, Cancer research.

Expressed in the Yeast Saccharomyces cerevisiae, Human ERK5 Is a Client of the Hsp90 Chaperone That Complements Loss of the Slt2p (Mpk1p) Cell Integrity Stress-Activated Protein Kinase

L. Pearl, P. Piper, A. Truman, 2006, Eukaryotic Cell.

Expressed in yeast , human ERK 5 is a client of the Hsp 90 chaperone that complements loss of the Slt 2 ( Mpk 1 ) p cell integrity stress-activated protein kinase

L. Pearl, P. Piper, A. Truman, 2006 .

Combinatorial Domain Hunting: An effective approach for the identification of soluble protein domains adaptable to high‐throughput applications

L. Pearl, K. Maclagan, P. Driscoll, 2006, Protein science : a publication of the Protein Society.

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

M. Korbonits, F. D’Acquisto, R. Morgan, 2016, The Journal of clinical endocrinology and metabolism.

In vivo bioassay to test the pathogenicity of missense human AIP variants

Benjamin Klapholz, M. Korbonits, C. Prodromou, 2018, Journal of Medical Genetics.

Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach

L. Pearl, P. Piper, A. Truman, 2004, Cell stress & chaperones.

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

Paul Workman, Chrisostomos Prodromou, Laurence H Pearl, 2013, Nature chemical biology.

Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain

L. Neckers, J. Buchner, M. Mayer, 2009, Nature Structural &Molecular Biology.

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

Laurence H. Pearl, Chrisostomos Prodromou, L. Pearl, 1997, Nature Structural Biology.

In the Yeast Heat Shock Response, Hsf1-Directed Induction of Hsp90 Facilitates the Activation of the Slt2 (Mpk1) Mitogen-Activated Protein Kinase Required for Cell Integrity

P. Piper, A. Truman, C. Prodromou, 2007, Eukaryotic Cell.

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis

Stephen W. Wilson, Thomas A. Hawkins, W. Talbot, 2008, Development.

Co-chaperone Regulation of Conformational Switching in the Hsp90 ATPase Cycle*

L. Pearl, P. Piper, C. Prodromou, 2004, Journal of Biological Chemistry.

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

C. Prodromou, G. Siligardi, Minghao Zhang, 2018, Front. Mol. Biosci..

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

L. Pearl, P. Piper, C. Liao, 2004, The EMBO journal.

DNA fragmentation-based combinatorial approaches to soluble protein expression Part I. Generating DNA fragment libraries.

P. Driscoll, R. Savva, C. Prodromou, 2007, Drug discovery today.

DNA fragmentation based combinatorial approaches to soluble protein expression Part II: library expression, screening and scale-up.

P. Driscoll, R. Savva, C. Prodromou, 2007, Drug discovery today.

The ‘Complex World’ of the Hsp90 Co-chaperone R2TP

C. Prodromou, 2019, Heat Shock Proteins.

Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.

P. Cohen, L. Pearl, M. Peggie, 2005, Molecular cell.

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

L. Pearl, P. Piper, L. Neckers, 2011, Molecular cell.

Structural and Functional Analysis of the Middle Segment of Hsp 90 : Implications for ATP Hydrolysis and Client

L. Pearl, P. Piper, S. Roe, 2003 .

Qri2/Nse4, a component of the essential Smc5/6 DNA repair complex

L. Pearl, P. Piper, C. Liao, 2005, Molecular microbiology.

Recursive PCR: a novel technique for total gene synthesis.

L. Pearl, C. Prodromou, L H Pearl, 1992, Protein engineering.

Structure and functional relationships of Hsp90.

L. Pearl, C. Prodromou, 2003, Current cancer drug targets.

Editorial: The Role of Heat Shock Proteins in Neuroprotection

C. Prodromou, H. Durham, M. Santha, 2020, Frontiers in Pharmacology.

The PTPIP51 TPR-Domain: A Novel Lipid Transfer Domain?

C. Prodromou, F. Giordano, 2021, Contact (Thousand Oaks (Ventura County, Calif.)).

Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues

L. Pearl, X. Barril, M. Drysdale, 2007, Molecular Cancer Therapeutics.

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

G. Balogh, Á. Hunya, P. Hooper, 2016, Journal of Alzheimer's disease : JAD.

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

M. Michaelides, A. Roux, C. Prodromou, 2020, Scientific Reports.

Identification of endogenously S-nitrosylated proteins in Arabidopsis plantlets : Effect of cold stress on cysteine nitrosylation level

Ailan Guo, Soichiro Yoshida, Chrisostomos Prodromou, 2014 .

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

L. Pearl, G. Degliesposti, J. Skehel, 2018, Nature Communications.

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

H. Neuweiler, C. Prodromou, Jonathan Schubert, 2021, Nature Communications.

Co-Crystalization and In Vitro Biological Characterization of 5-Aryl-4-(5-Substituted-2-4-Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors

P. Workman, S. Roe, C. Prodromou, 2012, PloS one.

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

L. Neckers, M. Mayer, C. Prodromou, 2012, Proceedings of the National Academy of Sciences.

CDK-Dependent Hsp70 Phosphorylation Controls G1 Cyclin Abundance and Cell-Cycle Progression

Hong Zhang, Chrisostomos Prodromou, Andrew W. Truman, 2012, Cell.

The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer’s Disease

Z. Török, J. Spencer, S. Roe, 2023, bioRxiv.

Activation of autophagy depends on Atg1/Ulk1-mediated phosphorylation and inhibition of the Hsp90 chaperone machinery

D. Bourboulia, C. Prodromou, B. Panaretou, 2023, Cell Reports.

Catalytic inhibitor of Protein Phosphatase 5 activates the extrinsic apoptotic pathway by disrupting complex II in kidney cancer.

D. Bourboulia, A. Blanden, C. Prodromou, 2023, Cell chemical biology.

Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insights

M. Mayer, B. Freeman, C. Prodromou, 2014, Front. Mol. Biosci..

The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn).

C. Prodromou, J. Guest, M. Haynes, 1991, Journal of general microbiology.

First Virtual International Congress on Cellular and Organismal Stress Responses, November 5–6, 2020

H. Kampinga, A. Edkins, A. Zhuravleva, 2021, Cell Stress and Chaperones.

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

L. Pearl, P. Workman, P. Clarke, 2013, Nature chemical biology.

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

L. Pearl, P. Workman, P. Clarke, 2013 .

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

M. Korbonits, F. D’Acquisto, R. Morgan, 2016, The Journal of clinical endocrinology and metabolism.

Second international symposium on the chaperone code, 2023

L. Gierasch, W. Houry, D. Bourboulia, 2024, Cell stress & chaperones.

A simple yeast-based system for analyzing inhibitor resistance in the human cancer drug targets Hsp90alpha/beta.

P. Piper, C. Prodromou, S. Millson, 2010, Biochemical pharmacology.

Targeting the Hsp90 molecular chaperone with novel macrolactams. Synthesis, structural, binding, and cellular studies.

P. Workman, W. Aherne, F. Raynaud, 2011, ACS chemical biology.