Explanipedia

Ex vivo qualitative and quantitative analysis of fluorescently-labeled Hsp90 drug in human tumors Open

Sarah J. Backe, Dimitra Bourboulia, Mark R. Woodford, Mehdi Mollapour · 2025

Heat shock protein 90 (Hsp90) stabilizes numerous oncogenic proteins making it a key therapeutic target in cancer. This protocol details an ex vivo method using freshly resected human renal cell carcinoma tissues to evaluate fluorescently …

Coordinated regulation of the metaboproteome by Hsp90 chaperones controls metabolic plasticity Open

R. Felipe Perez, Gianna Mochi, Julia K Burkacki, Landon D Arcadi, Sarah J. Backe , et al. · 2025

Heat shock protein 90 (Hsp90) chaperones participate in the stabilization and activation of hundreds of proteins, thereby acting as signaling hubs. A mitochondrial subpopulation of Hsp90 has been previously described; however, little is kn…

Design of multi-target peptide modulators for protein chaperone networks Open

Luca Torielli, Matteo Castelli, F Milani, Jennifer A. Heritz, Sara J Cayaban , et al. · 2025

Essential chaperones heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) collaborate in oncoprotein folding. Dual inhibition of these chaperones has shown synergy in preclinical studies but remains challenging to achieve. Using…

Integrating deep learning for post-translational modifications crosstalk on Hsp90 and drug binding Open

Jennifer Heritz, Katherine A. Meluni, Sarah J. Backe, Sara J Cayaban, Laura A Wengert , et al. · 2025

Flow cytometry FRET reveals post-translational modifications drive Protein Phosphatase-5 conformational changes in mammalian cells Open

Rebecca Sager, Sarah J. Backe, Jennifer Heritz, Mark R. Woodford, Dimitra Bourboulia , et al. · 2024

SUMOylation of protein phosphatase 5 regulates phosphatase activity and substrate release Open

Rebecca Sager, Sarah J. Backe, Diana M. Dunn, Jennifer Heritz, Elham Ahanin , et al. · 2024

Mitochondrial Chaperone Code: Just warming up Open

R. Felipe Perez, Gianna Mochi, Ariba Khan, Mark R. Woodford · 2024

Second international symposium on the chaperone code, 2023 Open

Johannes Büchner, Milad J. Alasady, Sarah J. Backe, Brian S. J. Blagg, Richard L. Carpenter , et al. · 2024

Editorial: A new chapter for Cell Stress and Chaperones Open

Dimitra Bourboulia, Laura J. Blair, Melody S. Clark, Adrienne L. Edkins, Lawrence E. Hightower , et al. · 2024

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

Sarah J. Backe, Rebecca Sager, Jennifer A. Heritz, Laura A. Wengert, Katherine A. Meluni , et al. · 2024

Epichaperomics reveals dysfunctional chaperone protein networks Open

Mark R. Woodford, Dimitra Bourboulia, Mehdi Mollapour · 2023

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

Elham Ahanin, Rebecca Sager, Sarah J. Backe, Diana M. Dunn, Natela Dushukyan , et al. · 2023

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

Sarah J. Backe, Rebecca Sager, Jennifer A. Heritz, Laura A. Wengert, Katherine A. Meluni , et al. · 2023

Extracellular HSP90 warms up integrins for an irisin workout Open

Dimitra Bourboulia, Mark R. Woodford, Mehdi Mollapour · 2023

PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling Open

Sarah J. Backe, SarahBeth D. Votra, Matthew P. Stokes, Endre Sebestyén, Matteo Castelli , et al. · 2023

<i>Saccharomyces cerevisiae</i> as a tool for deciphering Hsp90 molecular chaperone function Open

Sarah J. Backe, Mehdi Mollapour, Mark R. Woodford · 2023

Yeast is a valuable model organism for their ease of genetic manipulation, rapid growth rate, and relative similarity to higher eukaryotes. Historically, Saccharomyces cerevisiae has played a major role in discovering the function of compl…

Detecting Posttranslational Modifications of Hsp90 Isoforms Open

Rebecca Sager, Sarah J. Backe, Len Neckers, Mark R. Woodford, Mehdi Mollapour · 2023

Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8–9, 2022 Open

Patricija van Oosten‐Hawle, Sarah J. Backe, Anat Ben‐Zvi, Dimitra Bourboulia, Mara Brancaccio , et al. · 2023

The Second International Symposium on Cellular and Organismal Stress Responses took place virtually on September 8-9, 2022. This meeting was supported by the Cell Stress Society International (CSSI) and organized by Patricija Van Oosten-Ha…

Sumoylation of Protein Phosphatase 5 Regulates Phosphatase Activity And Substrate Release Open

Rebecca Sager, Sarah J. Backe, Diana M. Dunn, Jennifer A. Heritz, Elham Ahanin , et al. · 2023

Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity Open

Sarah J. Backe, Mark R. Woodford, Elham Ahanin, Rebecca Sager, Dimitra Bourboulia , et al. · 2022

Targeting extracellular Hsp90: A unique frontier against cancer Open

Rebecca Sager, Farzana Khan, Lorenzo Toneatto, SarahBeth D. Votra, Sarah J. Backe , et al. · 2022

The molecular chaperone Heat Shock Protein-90 (Hsp90) is known to interact with over 300 client proteins as well as regulatory factors (eg. nucleotide and proteins) that facilitate execution of its role as a chaperone and, ultimately, clie…

O-GlcNAcylation suppresses TRAP1 activity and promotes mitochondrial respiration Open

Seungchan Kim, Sarah J. Backe, Laura A. Wengert, Anna E. Johnson, Roman V. Isakov , et al. · 2022

A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand Open

Sarah J. Backe, Rebecca Sager, Bethany R. Regan, Julian Sit, Lauren Major , et al. · 2022

Heat shock protein-90 (Hsp90) chaperone machinery is involved in the stability and activity of its client proteins. The chaperone function of Hsp90 is regulated by co-chaperones and post-translational modifications. Although structural evi…

Emerging Link between Tsc1 and FNIP Co-Chaperones of Hsp90 and Cancer Open

Sarah J. Backe, Rebecca Sager, Katherine A. Meluni, Mark R. Woodford, Dimitra Bourboulia , et al. · 2022

Heat shock protein-90 (Hsp90) is an ATP-dependent molecular chaperone that is tightly regulated by a group of proteins termed co-chaperones. This chaperone system is essential for the stabilization and activation of many key signaling prot…

TRAP1 Chaperones the Metabolic Switch in Cancer Open

Laura A. Wengert, Sarah J. Backe, Dimitra Bourboulia, Mehdi Mollapour, Mark R. Woodford · 2022

Mitochondrial function is dependent on molecular chaperones, primarily due to their necessity in the formation of respiratory complexes and clearance of misfolded proteins. Heat shock proteins (Hsps) are a subset of molecular chaperones th…

Therapeutic potential of CDK4/6 inhibitors in renal cell carcinoma Open

Rebecca Sager, Sarah J. Backe, Elham Ahanin, Garrett Smith, Imad Nsouli , et al. · 2022

Seventh BHD international symposium: recent scientific and clinical advancement Open

Mark R. Woodford, Avgi Andreou, Masaya Baba, Irma van de Beek, Chiara Di Malta , et al. · 2022

The 7th Birt-Hogg-Dubé (BHD) International Symposium convened virtually in October 2021. The meeting attracted more than 200 participants internationally and highlighted recent findings in a variety of areas, including genetic insight and …

Hsp90 chaperone code and the tumor suppressor VHL cooperatively regulate the mitotic checkpoint Open

Mark R. Woodford, Sarah J. Backe, Laura A. Wengert, Diana M. Dunn, Dimitra Bourboulia , et al. · 2021

The tumor suppressor folliculin inhibits lactate dehydrogenase A and regulates the Warburg effect Open

Mark R. Woodford, Alexander J. Baker-Williams, Rebecca Sager, Sarah J. Backe, Adam R. Blanden , et al. · 2021

Post-translational modifications of Hsp90 and translating the chaperone code Open

Sarah J. Backe, Rebecca Sager, Mark R. Woodford, Alan M. Makedon, Mehdi Mollapour · 2020

Cells have a remarkable ability to synthesize large amounts of protein in a very short period of time. Under these conditions, many hydrophobic surfaces on proteins may be transiently exposed, and the likelihood of deleterious interactions…

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