Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

Karagöz, G. Elif, Duarte, Afonso M.S., Akoury, Elias, Ippel, Hans, Biernat, Jacek, Morán Luengo, Tania, Radli, Martina, Didenko, Tatiana +8 more·2014·Cell

Cited by (321)

Items 101–200 of 321

  1. The Bacterial Hsp90 Chaperone: Cellular Functions and Mechanism of Action
    Sue Wickner, Thu-Lan Lily Nguyen, Olivier Genest · 2021 · Annual Review of Microbiology
  2. A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
    Rehn, Alexandra, Lawatscheck, Jannis, Jokisch, Marie-Lena, Mader, Sophie L., Luo, Qi, Tippel, Franziska, Blank, Birgit, Richter, Klaus, Lang, Kathrin, Kaila, Ville R. I. et al. · 2020 · Nature Communications
  3. The multiple roles of chronic stress and glucocorticoids in Alzheimer's disease pathogenesis
    Mia R Burke, Ioannis Sotiropoulos, Clarissa L. Waites · 2024 · Trends in Neurosciences
  4. Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II
    Jinghui Luo, Sebastian K.T.S. Wärmländer, Astrid Gräslund, Jan Pieter Abrahams · 2016 · ACS Chemical Neuroscience
  5. The active Hsc70/tau complex can be exploited to enhance tau turnover without damaging microtubule dynamics
    Sarah N. Fontaine, Mackenzie D. Martin, Elias Akoury, Victoria A. Assimon, Sergiy I. Borysov, Bryce A. Nordhues, Jonathan J. Sabbagh, Matt Cockman, Jason E. Gestwicki, Markus Zweckstetter et al. · 2015 · Human Molecular Genetics
  6. Aging as a Precipitating Factor in Chronic Restraint Stress-Induced Tau Aggregation Pathology, and the Protective Effects of Rosmarinic Acid
    Shan Ye, Dandan Wang, Yuxia Xu, Chu Wang, Lan Cao, Yunsheng Liu, Cuiqing Zhu · 2015 · Journal of Alzheimer s Disease
  7. Isotope-labeling strategies for solution NMR studies of macromolecular assemblies
    Heyi Zhang, Hugo van Ingen · 2016 · Current Opinion in Structural Biology
  8. Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation
    Rina Rosenzweig, Lewis E. Kay · 2015 · Journal of the American Chemical Society
  9. Modulation of Molecular Chaperones in Huntington’s Disease and Other Polyglutamine Disorders
    Sara Reis, Brígida R. Pinho, Jorge M. A. Oliveira · 2016 · Molecular Neurobiology
  10. The penalty of stress ‐ Epichaperomes negatively reshaping the brain in neurodegenerative disorders
    Stephen D. Ginsberg, Suhasini Joshi, Sahil Sharma, Gianny Guzman, Tai Wang, Ottavio Arancio, Gabriela Chiosis · 2021 · Journal of Neurochemistry
  11. Substrate specificity in the context of molecular chaperones
    Dipayan Bose, Abhijit Chakrabarti · 2017 · IUBMB Life
  12. Dihydropyridines Allosterically Modulate Hsp90 Providing a Novel Mechanism for Heat Shock Protein Co-induction and Neuroprotection
    Stephen Mark Roe, Ben Wahab, Zsolt Török, Ibolya Horváth, László Vı́gh, Chrisostomos Prodromou · 2018 · Frontiers in Molecular Biosciences
  13. NMR Meets Tau: Insights into Its Function and Pathology
    Guy M. Lippens, Isabelle Landrieu, Caroline Smet‐Nocca, Isabelle Huvent, Neha S. Gandhi, Benoı̂t Gigant, Clément Despres, Haoling Qi, Juan M. Lopez · 2016 · Biomolecules
  14. Isoform-Specific Phosphorylation in Human Hsp90β Affects Interaction with Clients and the Cochaperone Cdc37
    Minh Tú Nguyễn, Robert A. Knieß, Soumya Daturpalli, Laura Le Breton, Xiangyu Ke, Xuemei Chen, Matthias P. Mayer · 2017 · Journal of Molecular Biology
  15. Alzheimer Cells on Their Way to Derailment Show Selective Changes in Protein Quality Control Network
    Koopman, Margreet B., Rüdiger, Stefan G. D. · 2020 · Frontiers in Molecular Biosciences
  16. Carboxy Terminus Heat Shock Protein 70 Interacting Protein Reduces Tau-Associated Degenerative Changes
    Laiq-Jan Saidi, Manuela Polydoro, Kevin R. Kay, Laura Sanchez, Eva‐Maria Mandelkow, Bradley T. Hyman, Tara L. Spires‐Jones · 2015 · Journal of Alzheimer s Disease
  17. Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains
    Josh Czemeres, Kurt Buse, Gennady M. Verkhivker · 2017 · PLoS ONE
  18. Management of Hsp90-Dependent Protein Folding by Small Molecules Targeting the Aha1 Co-Chaperone
    Jay K. Singh, Darren M. Hutt, Bradley D. Tait, Naihsuan C. Guy, Jeffrey C. Sivils, Nina R. Ortiz, Ashley N. Payan, Shravan Kumar Komaragiri, Jazzmin Jovonna Owens, David S. Culbertson et al. · 2020 · Cell chemical biology
  19. The metamorphic nature of the Tau protein: dynamic flexibility comes at a cost
    Sabbagh, Jonathan J., Dickey, Chad A. · 2016 · Frontiers in Neuroscience
  20. The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90
    López, Abraham, Elimelech, Annika R., Klimm, Karolin, Sattler, Michael · 2021 · ChemBioChem
  21. Heat Shock Protein 90 Associates with the Per-Arnt-Sim Domain of Heme-free Soluble Guanylate Cyclase
    Anindya Sarkar, Yue Dai, Mohammad Mahfuzul Haque, Franziska Seeger, Arnab Ghosh, Elsa D. Garcin, W.R. Montfort, Stanley L. Hazen, Saurav Misra, Dennis J. Stuehr · 2015 · Journal of Biological Chemistry
  22. Changes in proteome solubility indicate widespread proteostatic disruption in mouse models of neurodegenerative disease
    Michael C. Pace, Guilian M. Xu, Susan Fromholt, John Clair Howard, Keith W. Crosby, Benoit I. Giasson, Jada M. Lewis, David Borchelt · 2018 · Acta Neuropathologica
  23. A Two-Component Adhesive: Tau Fibrils Arise from a Combination of a Well-Defined Motif and Conformationally Flexible Interactions
    ShengQi Xiang, Natalia Kulminskaya, Birgit Habenstein, Jacek Biernat, Katharina Tepper, Maria Paulat, Christian Griesinger, Stefan Becker, Adam Lange, Eckhard Mandelkow� et al. · 2017 · Journal of the American Chemical Society
  24. Colostrum oxytocin modulates cellular stress response, inflammation, and autophagy markers in newborn rat gut villi
    Klein, Benjamin Y., Tamir, Hadassah, Ludwig, Robert J., Glickstein, Sara B., Welch, Martha G. · 2017 · Biochemical and Biophysical Research Communications
  25. Therapeutic Strategies for Restoring Tau Homeostasis
    Zapporah T. Young, Sue‐Ann Mok, Jason E. Gestwicki · 2017 · Cold Spring Harbor Perspectives in Medicine
  26. Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling
    Loïc Salmon, Logan S. Ahlstrom, Scott A. Horowitz, Alex Dickson, Charles L. Brooks, James C.A. Bardwell · 2016 · Journal of the American Chemical Society
  27. The known unknowns of the Hsp90 chaperone
    Laura‐Marie Silbermann, Benjamin Vermeer, Sonja Schmid, Katarzyna M. Tych · 2024 · eLife
  28. Hsp90 directly interacts, in vitro, with amyloid structures and modulates their assembly and disassembly
    Claire Schirmer, Eléonore Lepvrier, Laurence Duchesne, Olivier Decaux, Daniel Thomas, Christian Delamarche, Cyrille Garnier · 2016 · Biochimica et Biophysica Acta (BBA) - General Subjects
  29. Molecular chaperones biochemistry and role in neurodegenerative diseases
    Ali Châari · 2019 · International Journal of Biological Macromolecules
  30. HSP90 Interacts with the Fibronectin N-terminal Domains and Increases Matrix Formation
    Abir Chakraborty, Natasha Marie-Eraine Boel, Adrienne Lesley Edkins · 2020 · Cells
  31. Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP
    Francesca Munari, Luca Mollica, Carlo Valente, Francesca Parolini, Elham Ataie Kachoie, Giorgio Arrigoni, Mariapina D’Onofrio, Stefano Capaldi, Michael Assfalg · 2022 · Angewandte Chemie International Edition
  32. Mechanistic Asymmetry in Hsp90 Dimers
    Julia M. Flynn, Parul Mishra, Daniel N. A. Bolon · 2015 · Journal of Molecular Biology
  33. Hsp90 inhibitor HSP990 in very low dose upregulates EAAT2 and exerts potent antiepileptic activity
    Longze Sha, Ting Chen, Yu Deng, Tingfu Du, Kaili Ma, Wanwan Zhu, Yan Shen, Qi Xu · 2020 · Theranostics
  34. How do Chaperones Bind (Partly) Unfolded Client Proteins?
    Iva Sučec, Beate Bersch, Paul Schanda · 2021 · Frontiers in Molecular Biosciences
  35. Assembly mechanism of early Hsp90-Cdc37-kinase complexes
    Dimitra Keramisanou, M.V. Vasantha Kumar, Nicole Boose, Rinat R. Abzalimov, Ioannis Gelis · 2022 · Science Advances
  36. Increased Aggregation Tendency of Alpha-Synuclein in a Fully Disordered Protein Complex
    David Adrian Merle, Anja Witternigg, Carmen Tam‐Amersdorfer, Christoph Hartlmüller, Emil Spreitzer, Evelyne Schrank, Sabine Wagner-Lichtenegger, Oliver Werzer, Klaus Zangger, Andreas J. Kungl et al. · 2019 · Journal of Molecular Biology
  37. The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding
    Xiaozhan Qu, Simin Wang, Shuo Zhao, Chanjuan Wan, Weiya Xu, Chengdong Huang · 2024 · Nature Communications
  38. Molecular basis of the interaction of Hsp90 with its co‐chaperone Hop
    Antonia Lott, Javier Oroz, Markus Zweckstetter · 2020 · Protein Science
  39. The Mitochondrial Hsp90 TRAP1 and Alzheimer’s Disease
    Françoise A. Dekker, Stefan Rüdiger · 2021 · Frontiers in Molecular Biosciences
  40. The molecular network of the proteasome machinery inhibition response is orchestrated by HSP70, revealing vulnerabilities in cancer cells
    Magdalena Oroń, Marcin Grochowski, Akanksha Jaiswar, Justyna Legierska, Kamil Jastrzębski, Magdalena Nowak-Niezgoda, Małgorzata Kołos, Wojciech Kaźmierczak, Tomasz Olesiński, Małgorzata Lenarcik et al. · 2022 · Cell Reports
  41. Structures of Hsp90α and Hsp90β bound to a purine‐scaffold inhibitor reveal an exploitable residue for drug selectivity
    John D. Huck, Nanette L. S. Que, Sahil Sharma, Tony Taldone, Gabriela Chiosis, Daniel T. Gewirth · 2019 · Proteins Structure Function and Bioinformatics
  42. Proteomic interrogation of HSP90 and insights for medical research
    Lorenz Weidenauer, Tai Wang, Suhasini Joshi, Gabriela Chiosis, Manfredo Quadroni · 2017 · Expert Review of Proteomics
  43. Upregulated levels and pathological aggregation of abnormally phosphorylated Tau-protein in children with neurodevelopmental disorders
    Marija Rankovic, Markus Zweckstetter · 2018 · Neuroscience & Biobehavioral Reviews
  44. Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins
    Daturpalli, Soumya, Knieß, Robert A., Lee, Chung-Tien, Mayer, Matthias P. · 2017 · Journal of Molecular Biology
  45. Hsp90, a team player in protein quality control and the stress response in bacteria
    Anushka C. Wickramaratne, Sue Wickner, Andrea N. Kravats · 2024 · Microbiology and Molecular Biology Reviews
  46. Modulation of hippocampal neuronal resilience during aging by the Hsp70/Hsp90 co‐chaperone STI1
    Rachel E. Lackie, Abdul R. Razzaq, Sali M.K. Farhan, Lily R. Qiu, Gilli Moshitzky, Flávio H. Beraldo, Marilene Hohmuth Lopes, Andrzej Maciejewski, Robert Gros, Jue Fan et al. · 2019 · Journal of Neurochemistry
  47. Sequence features governing aggregation or degradation of prion-like proteins
    Sean M. Cascarina, Kacy R. Paul, Satoshi Machihara, Eric D. Ross · 2018 · PLoS Genetics
  48. Structural transitions modulate the chaperone activities of Grp94
    Amankwah, Yaa S., Fleifil, Yasmeen, Unruh, Erin, Collins, Preston, Wang, Yi, Vitou, Katherine, Bates, Alison, Obaseki, Ikponwmosa, Sugoor, Meghana, Alao, John Paul et al. · 2024 · Proceedings of the National Academy of Sciences
  49. Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity
    Xiang Zhang, Shengnan Zhang, Li Zhang, Jinxia Lu, Chunyu Zhao, Feng Luo, Dan Li, Xueming Li, Cong Liu · 2019 · Journal of Biological Chemistry
  50. Revisiting silibinin as a novobiocin-like Hsp90 C-terminal inhibitor: Computational modeling and experimental validation
    Elisabet Cuyàs, Sara Verdura, Vicente Micol, Jorge Joven, Joaquim Bosch‐Barrera, José Antonio Encinar, Javier Abel Menéndez · 2019 · Food and Chemical Toxicology
  51. Chaperone-mediated heterotypic phase separation regulates liquid-to-solid phase transitions of tau into amyloid fibrils
    Sandeep K. Rai, Roopali Khanna, Anusha Sarbahi, Ashish Joshi, Samrat Mukhopadhyay · 2025 · Science Advances
  52. Molecular insights into the interaction of Hsp90 with allosteric inhibitors targeting the C-terminal domain
    Vasantha Kumar MV, Radwan Ebna Noor, Rachel E. Davis, Zheng Zhang, Edvinas Sipavicius, Dimitra Keramisanou, Brian S. J. Blagg, Ioannis Gelis · 2018 · MedChemComm
  53. The molecular basis of chaperone-mediated interleukin 23 assembly control
    Susanne Meier, Sina Bohnacker, Carolin J. Klose, Abraham López, Christian A. Choe, Philipp W. N. Schmid, Nicolas Bloemeke, Florian Rührnößl, Martin Haslbeck, Julia Esser‐von Bieren et al. · 2019 · Nature Communications
  54. Non-equilibrium conformational dynamics in the function of molecular chaperones
    Alessandro Barducci, Paolo De Los Rios · 2015 · Current Opinion in Structural Biology
  55. Chaperone–client complexes: A dynamic liaison
    Sebastian Hiller, Björn M. Burmann · 2018 · Journal of Magnetic Resonance
  56. The role of the FKBP51–Hsp90 complex in Alzheimer’s disease: An emerging new drug target
    Xavier Jeanne, Zsolt Török, László Vı́gh, Chrisostomos Prodromou · 2024 · Cell Stress and Chaperones
  57. Dynamics-based community analysis and perturbation response scanning of allosteric interaction networks in the TRAP1 chaperone structures dissect molecular linkage between conformational asymmetry and sequential ATP hydrolysis
    Gennady M. Verkhivker · 2018 · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
  58. The Potential of Targeting P53 and HSP90 Overcoming Acquired MAPKi-Resistant Melanoma
    Chi–Che Hsieh, Che‐Hung Shen · 2019 · Current Treatment Options in Oncology
  59. Molecular Chaperones as Therapeutic Target: Hallmark of Neurodegenerative Disorders
    Aditi Sharma, Om Prakash Shah, Lalit Kumar Sharma, Monica Gulati, Tapan Behl, Asaad Khalid, Syam Mohan, Asim Najmi, Khalid A. Zoghebi · 2023 · Molecular Neurobiology
  60. Stressing Out Hsp90 in Neurotoxic Proteinopathies
    Carmen Inda, Alexander Bolaender, Tai Wang, Srinivasa R. Gandu, John Koren · 2016 · Current Topics in Medicinal Chemistry
  61. Key Physicochemical and Biological Factors of the Phase Behavior of Tau
    Geewoo Nam, Yuxi Lin, Mi Hee Lim, Young‐Ho Lee · 2020 · Chem
  62. Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy
    Theodoros K. Karamanos, G. Marius Clore · 2022 · Annual Review of Biophysics
  63. Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding
    Marc B. Cox, Jill L. Johnson · 2017 · Methods in molecular biology
  64. Human chaperones untangle fibrils of the Alzheimer protein Tau
    Luca Ferrari, Willie J. C. Geerts, Marloes D. van Wezel, Renate Kos, Aikaterini Konstantoulea, Laura S. van Bezouwen, Friedrich G. Förster, Stefan Rüdiger · 2018 · bioRxiv (Cold Spring Harbor Laboratory)
  65. Recombinant production and purification of the human protein Tau
    Luca Ferrari, Stefan Rüdiger · 2018 · Protein Engineering Design and Selection
  66. Chaperoning of specific tau structure by immunophilin FKBP12 regulates the neuronal resilience to extracellular stress
    Lulu Jiang, Pijush Chakraborty, Lushuang Zhang, Melissa Wong, Shannon E. Hill, Chelsea Joy Webber, Jenna Libera, Laura J. Blair, Benjamin L. Wolozin, Markus Zweckstetter · 2023 · Science Advances
  67. Simple model systems reveal conserved mechanisms of Alzheimer’s disease and related tauopathies
    Yuwei Jiang, Lesley T. MacNeil · 2023 · Molecular Neurodegeneration
  68. Structural basis for the dynamic chaperoning of disordered clients by Hsp90
    Xiaozhan Qu, Shuo Zhao, Chanjuan Wan, Lei Zhu, Tuo Ji, Paolo Rossi, Junfeng Wang, Charalampos G. Kalodimos, Chao Wang, Weiya Xu et al. · 2024 · Nature Structural & Molecular Biology
  69. NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13C-methyl alanine
    Kari Pederson, Gordon R. Chalmers, Qi Gao, Daniel Elnatan, Theresa A. Ramelot, Li-Chung Ma, Gaetano Thomas Montelione, Michael A. Kennedy, David A. Agard, James H. Prestegard · 2017 · Journal of Biomolecular NMR
  70. Flexible Stoichiometry and Asymmetry of the PIDDosome Core Complex by Heteronuclear NMR Spectroscopy and Mass Spectrometry
    Lily A. Nematollahi, Acely Garza-Garcı́a, Chérine Bechara, Diego Esposito, Nina Morgner, Carol V. Robinson, Paul C. Driscoll · 2014 · Journal of Molecular Biology
  71. ATP Impedes the Inhibitory Effect of Hsp90 on Aβ40 Fibrillation
    Hongzhi Wang, Max Lallemang, Bianca A. Hermann, Cecilia Wallin, Rolf Antonie Loch, Alain Blanc, Bizan N. Balzer, Thorsten Hugel, Jinghui Luo · 2020 · Journal of Molecular Biology
  72. Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I
    José Ángel Fernández-Higuero, Isabel Betancor-Fernández, Noel Mesa‐Torres, Arturo Muga, EDUARDO C. SALIDO, Angel Luis Pey · 2018 · Advances in protein chemistry and structural biology
  73. FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story
    Béatrice Chambraud, Cillian Byrne, Geri Méduri, E.E. Baulieu, Julien Giustiniani · 2022 · International Journal of Molecular Sciences
  74. Selective nitration of Hsp90 acts as a metabolic switch promoting tumor cell proliferation
    Isabelle E. Logan, Kyle T. Nguyen, Tilottama Chatterjee, Bhagyashree Manivannan, Ngozi P. Paul, Sharon Kim, Evelyn Sixta, Lydia P. Bastian, Carrie L. Marean‐Reardon, Matthias A. Karajannis et al. · 2024 · Redox Biology
  75. HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease
    Chrisostomos Prodromou, Xavier Aran-Guiu, Jasmeen Oberoi, Laura Perna, J. Paul Chapple, Jacqueline van der Spuy · 2022 · Sub-cellular biochemistry/Subcellular biochemistry
  76. HEAT SHOCK PROTEIN 90.6 interacts with carbon and nitrogen metabolism components during seed development
    Jianghai Xu, Zhijia Yang, Xiaohong Fei, Meiling Zhang, Yang Cui, Xiangbo Zhang, Kaiwen Tan, E Lizhu, Haiming Zhao, Jinsheng Lai et al. · 2023 · PLANT PHYSIOLOGY
  77. The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer’s Disease
    Stephen Mark Roe, Zsolt Török, Andrew McGown, Ibolya Horváth, John Spencer, Tamás Pázmány, László Vı́gh, Chrisostomos Prodromou · 2023 · Biomolecules
  78. Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects
    Hadeel Alyenbaawi, W. Ted Allison, Sue‐Ann Mok · 2020 · Biomolecules
  79. The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers
    Yi Jin, Judy L.M. Kotler, Shiyu Wang, Bin Huang, Jackson C. Halpin, Timothy O. Street · 2021 · Journal of Molecular Biology
  80. Establishing Order Through Disorder by the Hsp90 Molecular Chaperone
    Neethu L. Babu, Brian Freeman · 2024 · Journal of Molecular Biology
  81. Heat shock proteins regulates Tau protein aggregation in Alzheimer’s disease
    Subashchandrabose Chinnathambi · 2024 · Advances in protein chemistry and structural biology
  82. Characterization of the Grp94/OS-9 Chaperone–Lectin Complex
    Paul M. Seidler, Stephen A. Shinsky, Feng Hong, Zihai Li, Michael S. Cosgrove, Daniel T. Gewirth · 2014 · Journal of Molecular Biology
  83. Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity
    Wei He, Jiayin Zhang, Veronika Sachsenhauser, Lili Wang, James C.A. Bardwell, Shu Quan · 2020 · Journal of Biological Chemistry
  84. The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway
    Deepika Gaur, Prashant R. Singh, Jyoti Guleria, Arpit Gupta, Satinderdeep Kaur, Deepak Sharma · 2020 · Genetics
  85. Molecular hallmarks of excitatory and inhibitory neuronal resilience to Alzheimer’s disease
    Isabel Castanho, Pourya Naderi Yeganeh, Carles A. Boix, Sarah L. Morgan, Hansruedi Mathys, Dmitry Prokopenko, Bartholomew White, Larisa M. Soto, Giulia Pegoraro, Saloni A. Shah et al. · 2025 · Molecular Neurodegeneration
  86. DJ-1 Molecular Chaperone Activity Depresses Tau Aggregation Propensity through Interaction with Monomers
    Daniela Jimenez-Harrison, Carol J. Huseby, Claire N. Hoffman, Steven Sher, Dalton T. Snyder, Brayden Seal, Chunhua Yuan, Hongjun Fu, Vicki Hopper Wysocki, Flaviano Giorgini et al. · 2023 · Biochemistry
  87. Exploring Mechanisms of Allosteric Regulation and Communication Switching in the Multiprotein Regulatory Complexes of the Hsp90 Chaperone with Cochaperones and Client Proteins: Atomistic Insights from Integrative Biophysical Modeling and Network Analysis of Conformational Landscapes
    Gennady M. Verkhivker · 2022 · Journal of Molecular Biology
  88. Structural ensemble-based docking simulation and biophysical studies discovered new inhibitors of Hsp90 N-terminal domain
    Hyun-Hwi Kim, Ja-Shil Hyun, Joonhyeok Choi, Kwang-Eun Choi, Jun‐Goo Jee, Sung Jean Park · 2018 · Scientific Reports
  89. The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau
    Chen Lyu, Stefano Da Vela, Youssra K. Al‐Hilaly, Karen E. Marshall, Richard Thorogate, Dmitri I. Svergun, Louise C. Serpell, Annalisa Pastore, Diane P. Hanger · 2021 · Frontiers in Molecular Biosciences
  90. Chaperone-Mediated Regulation of Tau Phase Separation, Fibrillation, and Toxicity
    Cecilia Mörman, Axel Leppert, Giusy Pizzirusso, Zihan Zheng, Xun Sun, Rakesh Kumar, Henrik Biverstål, Michael Landreh, Jan Johansson, Luis Enrique Arroyo‐García et al. · 2025 · Journal of the American Chemical Society
  91. Microtubule‐affinity regulating kinase family members distinctively affect tau phosphorylation and promote its toxicity in a Drosophila model
    Grigorii Sultanakhmetov, Iori Kato, Akiko Asada, Taro Saito, Kanae Ando · 2024 · Genes to Cells
  92. Microtubule Organization and Microtubule-Associated Proteins (MAPs)
    Elena Tortosa, Lukas C. Kapitein, Casper C. Hoogenraad · 2016 · Springer eBooks
  93. Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?
    Emelie E. Aspholm, Irena Matečko‐Burmann, Björn M. Burmann · 2020 · Life
  94. Synthetic chaperone based on Hsp90-Tau interaction inhibits Tau aggregation and rescues physiological Tau-Microtubule interaction
    Davide Di Lorenzo, Nicolò Bisi, J. Kaffy, L. Ramirez, M. Zweckstetter, Olivier Lequin, Irene Garfagnini, Jinghui Luo, Yvonne Hannappel, Inga Ennen et al. · 2024 · bioRxiv
  95. Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin
    Ricarda Törner, Tatsiana Kupreichyk, Lothar Gremer, Elisa Colas Debled, Daphna Fenel, Sarah Schemmert, Pierre Gans, Dieter Willbold, Guy Schoehn, Wolfgang Hoyer et al. · 2022 · Nature Communications
  96. The role of heat shock proteins in preventing amyloid toxicity
    Ricarda Törner, Tatsiana Kupreichyk, Wolfgang Hoyer, Jérôme Boisbouvier · 2022 · Frontiers in Molecular Biosciences
  97. Molecular determinants of Hsp90 dependence of Src kinase revealed by deep mutational scanning
    Vanessa Nguyen, Ethan Ahler, Katherine A. Sitko, Jason J. Stephany, Dustin J. Maly, Douglas M. Fowler · 2023 · Protein Science
  98. Small molecules targeting molecular chaperones for tau regulation: Achievements and challenges
    Chenxi He, Jinying Gu, Danni Wang, Keran Wang, Yuxuan Wang, Qidong You, Lei Wang · 2023 · European Journal of Medicinal Chemistry
  99. Conformational Dynamics and Mechanisms of Client Protein Integration into the Hsp90 Chaperone Controlled by Allosteric Interactions of Regulatory Switches: Perturbation-Based Network Approach for Mutational Profiling of the Hsp90 Binding and Allostery
    Gennady M. Verkhivker · 2022 · The Journal of Physical Chemistry B
  100. Direct observation of Hsp90-induced compaction in a protein chain
    Alireza Mashaghi, Fatemeh Moayed, Eline J. Koers, Yang Zheng, Katharina Till, Günter Kramer, Matthias P. Mayer, Sander J. Tans · 2022 · Cell Reports