B. Panaretou

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.

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

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

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

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

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.

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.

Effect of pre- and post-heat shock temperature on the persistence of thermotolerance and heat shock-induced proteins in Listeria monocytogenes.

B. Panaretou, S. Knøchel, P. J. Stephens, 1996, The Journal of applied bacteriology.

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

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

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.

Plasma-membrane ATPase action affects several stress tolerances of Saccharomyces cerevisiae and Schizosaccharomyces pombe as well as the extent and duration of the heat shock response

P. Piper, B. Panaretou, 1990 .

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.

ADAM8 signaling drives neutrophil migration and ARDS severity

N. Suttorp, A. Zarbock, A. Margraf, 2022, JCI insight.

Isolation of yeast plasma membranes.

P. Piper, B. Panaretou, 1996, Methods in molecular biology.

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.

Human phenylalanine monooxygenase and thioether metabolism

B. Panaretou, S. Mitchell, B. Forbes, 2009, The Journal of pharmacy and pharmacology.

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

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

A Mini HIP HOP Assay Uncovers a Central Role for Copper and Zinc in the Antifungal Mode of Action of Allicin.

B. Panaretou, T. Prescott, 2017, Journal of agricultural and food chemistry.

A yeast chemical genetics approach identifies the compound 3,4,5‐trimethoxybenzyl isothiocyanate as a calcineurin inhibitor

M. Simmonds, B. Panaretou, T. Prescott, 2014, FEBS letters.

Chaperone ligand-discrimination by the TPR-domain protein Tah1

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

Eukaryotic integral membrane protein expression utilizing the Escherichia coli glycerol-conducting channel protein (GlpF)

Jayne Lawrence, D. Barlow, B. Panaretou, 2007, Applied Microbiology and Biotechnology.

Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold.

P. Piper, H. Boucherie, B. Panaretou, 1994, Microbiology.

The plasma membrane of yeast acquires a novel heat-shock protein (hsp30) and displays a decline in proton-pumping ATPase levels in response to both heat shock and the entry to stationary phase.

P. Piper, B. Panaretou, Peter W. Piper, 1992, European journal of biochemistry.

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.

The Hsp90 of Candida albicans can confer Hsp90 functions in Saccharomyces cerevisiae: a potential model for the processes that generate immunogenic fragments of this molecular chaperone in C. albicans infections.

L. Pearl, P. Piper, B. Panaretou, 1999, Microbiology.

The heat shock proteins: Their roles as multi-component machines for protein folding

B. Panaretou, C. Zhai, 2008 .

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 function of ORAOV1/LTO1, a gene that is overexpressed frequently in cancer: essential roles in the function and biogenesis of the ribosome

B. Panaretou, C. Grant, K. Li, 2014, Oncogene.

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

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

Emw1p/YNL313cp is essential for maintenance of the cell wall in Saccharomyces cerevisiae.

B. Panaretou, C. Zhai, Tatjana Sipling, 2011, Microbiology.

A simplified and easy‐to‐use HIP HOP assay provides insights into chalcone antifungal mechanisms of action

B. Panaretou, A. Maxwell, T. Prescott, 2022, FEBS letters.

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.

Genomic Screening in Vivo Reveals the Role Played by Vacuolar H+ ATPase and Cytosolic Acidification in Sensitivity to DNA-Damaging Agents Such as Cisplatin

M. Arno, C. Liao, B. Panaretou, 2007, Molecular Pharmacology.

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.

Ypp1/YGR198w plays an essential role in phosphoinositide signalling at the plasma membrane.

B. Panaretou, K. Bowers, J. Phelan, 2008, The Biochemical journal.

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

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

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

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

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

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

Expressed as the sole Hsp90 of yeast, the α and β isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90β generates sensitivity to the Hsp90 inhibitor radicicol

P. Piper, A. Truman, B. Panaretou, 2007 .

Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol.

P. Piper, A. Truman, B. Panaretou, 2007, The FEBS journal.

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.

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

Ailan Guo, Soichiro Yoshida, Chrisostomos Prodromou, 2014 .

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.

Bolaamphiphile Analogues of 12-bis-THA Cl2 Are Potent Antimicrobial Therapeutics with Distinct Mechanisms of Action against Bacterial, Mycobacterial, and Fungal Pathogens

M. McArthur, P. Langford, B. Panaretou, 2022, mSphere.

Increasing Saccharomyces cerevisiae stress resistance, through the overactivation of the heat shock response resulting from defects in the Hsp90 chaperone, does not extend replicative life span but can be associated with slower chronological ageing of nondividing cells

P. Piper, B. Panaretou, M. MacLean, 2001, Molecular Genetics and Genomics.

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.

Yeast models for amyloid disease.

B. Panaretou, G. Jones, 2014, Essays in biochemistry.