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Sub-Cellular Biochemistry|December 15, 2022
HSP70-HSP90 Chaperone Networking in Protein-Misfolding DiseaseChrisostomos Prodromou, Xavi Aran-Guiu, Jasmeen Oberoi, et al.
Plos One|September 18, 2012
Co-crystalization and in vitro biological characterization of 5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitorsSwee Y Sharp, S Mark Roe, Egidijus Kazlauskas, et al.
Molecular Cell|November 26, 2005
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complexMinghao Zhang, Mark Windheim, S Mark Roe, et al.
Frontiers in Molecular Biosciences|January 30, 2023
AlphaFold predicted structure of the Hsp90-like domains of the neurodegeneration linked protein sacsin reveals key residues for ATPase activityLaura Perna, Matteo Castelli, Elena Frasnetti, et al.
European Journal of Biochemistry|November 19, 2003
Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeastPeter W Piper, Stefan H Millson, Mehdi Mollapour, et al.
The EMBO Journal|September 27, 2008
Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexesMinghao Zhang, Marta Botër, Kuoyu Li, et al.
Biomolecules|July 29, 2023
The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer's DiseaseS Mark Roe, Zsolt Török, Andrew McGown, et al.
Gene|January 16, 2003
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 inhibitorsPeter W Piper, Barry Panaretou, Stefan H Millson, et al.
Cell Stress & Chaperones|December 5, 2025
The dihydropyridine LA1011 modulates multiple Hsp90-co-chaperone interactions relevant to Alzheimer's diseaseXavier Jeanne, Jasmeen Oberoi, Mark S Roe, et al.
Science Advances|May 4, 2019
Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EMHugo Muñoz-Hernández, Mohinder Pal, Carlos F Rodríguez, et al.
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