CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374

Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein

Lewis, J., McGowan, E., Rockwood, J., Melrose, H., Nacharaju, P., Van Slegtenhorst, M., Gwinn-Hardy, K., Murphy, M. P., Baker, M., Yu, X., et al. (2000) · Nature Genetics · doi:10.1038/78078 · Cited by 1,371

Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1

Zou, J., Guo, Y., Guettouche, T., Smith, D. F., & Voellmy, R. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81588-3 · Cited by 1,232

Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease

Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134

Tau protein aggregation: A therapeutic target for neurodegenerative diseases

Duggal, A., Mahindru, D., Baghel, K., Mehrotra, S., & Prajapati, V. K. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.012 · Cited by 2

Molecular Mechanisms and Therapeutic Potential of Degron-Mediated Proteostasis Regulation in Neurodegenerative Diseases

Nishanth, D. S., Sinha, U., Verma, T., Kalidass, B., Thirumuruganandham, S. P., & Muthukaliannan, G. K. (2026) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01659-6 · Cited by 2

Molecular and environmental drivers of tau post-translational modifications and tau pathology

Price, T. M., Tucker, A. E., & Funk, K. E. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103223 · Cited by 2

Protein clearance mechanisms and their demise in age-related neurodegenerative diseases

Sáez, I., & Vı́lchez, D. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.1.1 · Cited by 2

Heat Shock Proteins, Unfolded Protein Response Chaperones and Alzheimer’s Disease

Magrané, J., & Querfurth, H. W. (2008) · Springer eBooks · doi:10.1007/978-1-4020-8231-3_2 · Cited by 2

Chaperone Suppression of Aggregated Protein Toxicity

Wacker, J. L., & Muchowski, P. J. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_8 · Cited by 2

The Amyloid _-Protein and Alzheimer's Disease

Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2

Astrocytes as Targets for Neurological Gene Therapy

Imura, T., & Sofroniew, M. V. (2006) · CRC Press eBooks · doi:10.3109/9781420016390-8 · Cited by 2

Targeting Proteasomal Degradation of Soluble, Misfolded Proteins

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00003-5 · Cited by 2

Contrôle des voies métaboliques par les enzymes E3 ligases : une opportunité de ciblage thérapeutique

Taillandier, D. (2021) · Biologie Aujourd hui · doi:10.1051/jbio/2021006 · Cited by 2

Frontotemporal lobar degeneration

Kim, B., Viera-Ortiz, A., Phan, J. M., Irwin, D. J., & Lee, E. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00041-1 · Cited by 3

Cloning and characterization of heat shock transcription factor 1 and its functional role for Hsp70 production in the sea slug Onchidium reevesii

Tu, Z., Tang, L., Abo‐Raya, M. H., Sun, M., Shen, H., & Wang, Y. (2023) · Gene · doi:10.1016/j.gene.2023.147945 · Cited by 2

Ubiquitin Mediated Posttranslational Modification of Proteins Involved in Various Signaling Diseases

LAVANYA, V. A., Jamal, S., & Ahmed, N. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811913-6.00005-9 · Cited by 2

Plant E3 Ligases as Versatile Tools for Novel Drug Development and Plant Bioengineering

Al‐Saharin, R., Mooney, S., & Hellmann, H. A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160691-00212 · Cited by 2

Fibrilpaint20 directs the ubiquitin–proteasome system to Tau amyloid fibrilsPreprint

Dekker, F. A., Pedrola, J. A., van Weert, E., den Breejen, A., Peters, L., Poza-Rodriguez, A., Mayer, G., Singh, S., Vertegaal, A. C. O., Friedler, A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.27.609886 · Cited by 2

Chaperone-directed ubiquitylation maintains proteostasis at the expense of longevity

Pokrzywa, W., Lorenz, R., & Hoppe, T. (2017) · Worm · doi:10.1080/21624054.2017.1371403 · Cited by 2

Quantification of Methylation and Phosphorylation Stoichiometry

Ayoub, C. A., Moore, K. I., & Kuret, J. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_13 · Cited by 1

Mechanism Underlying Major Neurodegenerative Disorders

Chongtham, A., & Agrawal, N. (2024) · Springer eBooks · doi:10.1007/978-981-97-4288-2_2 · Cited by 1

Bridging autophagy and endolysosomal dysfunction: Role of bridging integrator 1 in Alzheimer’s disease

Duckhorn, J. C., Kim, D. K., & Huang, Y. A. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00243 · Cited by 2

The Roles of Moonlighting Nicotinamide Mononucleotide Adenylyl Transferases in Cell Physiology

Lee, Y., & Lin, S.-J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26189098 · Cited by 2

Prefoldin 5 is a microtubule-associated protein that suppresses Tau aggregation and neurotoxicity

Bisht, A., Pippadpally, S., Majumder, S., Gopi, A. T., Das, A., Sahi, C., Ramaswami, M., & Kumar, V. (2024) · eLife · doi:10.7554/elife.104691.3 · Cited by 4

Dysfunctional Ubiquitin-Proteasome System and Consequences: Disease Mechanism

Milmile, M., Singh, S., Pandey, A., Ahire, N., & Chawla, R. (2026) · Springer eBooks · doi:10.1007/978-981-95-6099-8_2 · Cited by 1

Ubiquitin signatures on aggregating proteins in neurodegeneration

Sahoo, S., Padhy, A. A., Shivani, K., Misra, A., & Mishra, P. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253046 · Cited by 1

Beyond Inhibition: Rebalancing the Hsp90 Chaperone Network as a Therapeutic Strategy for Alzheimer’s Disease

Tang, Z., Xie, H., Xu, Y., Zhou, Z., Lu, F., Wu, Q., Liang, W., Zhong, M., & Li, S. (2026) · Drug Design Development and Therapy · doi:10.2147/dddt.s602287 · Cited by 1

Tau profiling of brain extracellular vesicles reveals PHF6 peptide as core for pathological tau seeding in Alzheimer's disease

Oosterlynck, M., Fichter, L., Leroux, É., Eddarkaoui, S., Bouillet, T., Lefebvre, C., Nguyen, M., Maurage, C., Accart, B., Dupré, E., et al. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-026-01250-1 · Cited by 1

Molecular Chaperones as Potential Therapeutic Targets for Neurological Disorders

Delenclos, M., & McLean, P. J. (2013) · Royal Society of Chemistry eBooks · doi:10.1039/9781849739689-00392 · Cited by 1

The Role of Hsp70 and Its Co-Chaperones in Protein Misfolding, Aggregation and Disease

van der Spuy, J., Cheetham, M. E., & Chapple, J. P. (2007) · Springer eBooks · doi:10.1007/978-0-387-49310-7_11 · Cited by 1

Cells and Fugu Response to Capsid of BFNNV Genotype

Mao, M., Jiang, J., Xu, J. W., et al. (2023) · Viruses · doi:10.3390/v15040988 · Cited by 1

Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

Parolini, F., Kachoie, E. A., Leo, G., Civiero, L., Bubacco, L., Arrigoni, G., Munari, F., Assfalg, M., D’Onofrio, M., & Capaldi, S. (2023) · Angewandte Chemie · doi:10.1002/ange.202310230 · Cited by 1

Neurodegeneration models in Drosophila

Roy, B., & Jackson, G. R. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.012 · Cited by 1

HSF Inhibits the Progression of Age-Related Neurodegenerative Diseases

Kondo, N., Katsuno, M., Riku, Y., & Sobue, G. (2016) · Springer eBooks · doi:10.1007/978-4-431-55852-1_11 · Cited by 1

Nano-Chaperones: Nanoparticles Acting as Artificial Chaperones

Boridy, S., & Maysinger, D. (2013) · Regenerative medicine, artificial cells and nanomedicine · doi:10.1142/9789814472869_0019 · Cited by 1

Current and Future Therapies for Alzheimer Disease

Chakrabarty, P., Das, P., & Golde, T. E. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch34 · Cited by 1

Commentary: p62 plays a protective role in the autophagic degradation of polyglutamine protein oligomers in polyglutamine disease model flies

Nagai, Y. (2017) · Journal of Rare Diseases Research & Treatment · doi:10.29245/2572-9411/2017/3.1106 · Cited by 1

Correction: Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue

Liu‐Yesucevitz, L., Bilgutay, A. N., Zhang, Y., et al. (2011) · PLoS ONE · doi:10.1371/annotation/7d880410-06e3-4fe3-a8f1-e84c89bcf8d0 · Cited by 1

Treadmill exercise promotes E3 ubiquitin ligase to remove amyloid β and P-tau and improve cognitive ability in APP/PS1 Transgenic MicePreprint

Xu, L., Li, M., Wei, A., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1758813/v1 · Cited by 1

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIPPreprint

Nadel, C. M., Wucherer, K., Oehler, A., Thwin, A. C., Basu, K., Callahan, M. D., Southworth, D. R., Mordes, D. A., Craik, C. S., & Gestwicki, J. E. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.16.553575 · Cited by 1

Structures of Fab-stabilized CHIP reveal a conformational switch important in E3 ligase and chaperone functionsPreprint

Unnikrishnan, A., Chung, D. H., Connelly, E. J., Chuo, S., Devi, S., Thwin, A. C., Nadel, C. M., Tse, E., Gestwicki, J. E., Craik, C. S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.15.654159 · Cited by 1

Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease

Chimal-Juárez, E., Patel, H., Jury-Garfe, N., Dabin, L. C., Vidal, R., Kim, J., & Lasagna-Reeves, C. A. (2026) · bioRxiv · doi:10.64898/2026.05.12.724684

Mutant ubiquitin and the proteasome in Alzheimer's disease

de Vrij, F. M. S. (2005) · UvA-DARE (University of Amsterdam)

Therapeutics: Harnessing the Power of Molecular and Pharmacological Chaperones

Gross, D. S., Klein, R. L., & Witt, S. N. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch12

Characterization of the Ubc13-Mms2 Lysine-63-linked ubiquitin conjugating complex

Pastushok, L. (2006) · University Library - University of Saskatchewan (University of Saskatchewan)

Using Drosophila to Reveal Insight into Protein Misfolding Diseases

Bilen, J., & Bonini, N. M. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch10

Regional lysosomal malfunction underlies the selectivity of alpha-synuclein neurodegeneration

Malkus, K. A. (2011) · Scholarly Commons (University of Pennsylvania)

Pin1: A New Enzyme Pivotal for Protecting Against Alzheimer’s Disease

Nakamura, K., Ma, S. L., & Lu, K. P. (2011) · InTech eBooks · doi:10.5772/20852

Targeting the Protein Quality Control (PQC) Machinery

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00002-3

The cytosolic fate of ricin A chain in target cells

Hart, P. J. (2026) · Warwick Research Archive Portal (University of Warwick) · doi:10.82444/warw.33594793

Animal Models of Tauopathy

Duff, K., Krishnamurthy, P., Planel, E., & Hutton, M. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_13

Targeting Protein Quality Control Pathways in Spinal and Bulbar Muscular Atrophy

Wang, A. M. (2012) · Deep Blue (University of Michigan)

Age-associated increases in FKBP51 facilitate tau neurotoxicity

Blair, L. J. (2014) · Digital Commons - University of South Florida (University of South Florida)

A role for the ubiquitin domain protein HERP in ER-associated protein degradation

Schulze, A. (2007) · edoc Publication server (Humboldt University of Berlin) · doi:10.18452/15575

Non‐amyloid Approaches To Alzheimer's Disease

Veng, L., Savage, M. J., Barrow, J. C., & Zerbinatti, C. (2010) · Wiley eBooks · doi:10.1002/0471266949.bmc253

Structural Basis for Ternary Complex Formation between Tau, Hsp90, and FKBP51

Barrett, A. S., Wu, H., Kashtanov, S., & Daughdrill, G. W. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.2162

Past, Present, and Future: The Behavioral Sciences.

Darley, J. G. (1971) · Contemporary Psychology · doi:10.1037/014015

Molecular Mechanisms of Tau Protein Aggregation Inhibition

Akoury, E. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4145

Sistemas neuromodulatórios: implicações fisiopatológicas

Carrettiero, D. C. (2008) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.41.2008.tde-16062008-174159

The Chaperone-assisted E3 Ligase C Terminus of Hsc70-interacting Protein (CHIP) Targets PTEN for

Ahmed, S. F., Deb, S., Paul, I., Chatterjee, A., Mandal, T., Chatterjee, U., & Ghosh, M. K. (2012)

BlockingA 42 AccumulationDelaystheOnsetand ProgressionofTauPathologyviatheCTerminusofHeat ShockProtein70-InteractingProtein:AMechanisticLink betweenAandTauPathology

LaFerla, F. M. (2008)

Role of C-terminus of HSC70 interacting protein in determining neuronal fate in acute injury

Stankowski, J. N. (2011)

Dissecting the Biochemical Pathways Mediated by Genes Implicated in Parkinson’s Disease: Induction of DJ-1 Expression in A30P α-Synuclein Mice

Frasier, M. A., Frausto, S. F., Lewicki, D., Golbe, L. I., & Wolozin, B. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-72076-0_11

Pick’s Disease

Anderson-Mooney, A. J., & Abisambra, J. F. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-407824-6.00012-4

Alternatives Fehlspleißen von Tau Exon 10, Htra2-ß und Clk2 in post mortem Hirngewebe von Alzheimer-Patienten

Möller, H.-J. (2005)

Visions & Reflections (Minireview) Synphilin-1 isoforms in Parkinsons disease: regulation by phosphorylation and ubiquitylation

Szargel, R., Rott, R., & Engelender, S. (2008)

The ubiquitin proteasome system in Huntington disease : impairment of the proteolytic machinery aggravates huntingtin aggregation and toxicity

de Pril, R. (2011)

Proteasomal Degradation of Soluble, Misfolded Proteins

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00003-1

Targeting the Protein Quality Control (PQC) Machinery

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00002-x

DeletionoftheUbiquitinLigaseCHIPLeadstothe Accumulation,ButNottheAggregation,ofBothEndogenous Phospho-andCaspase-3-CleavedTauSpecies

Dickey, C., & Clark, K. P. (2006)

Protein Aggregation and Neurodegeneration: Tauopathies and Synucleinopathies

Goedert, M. (2017) · Neurodegeneration · doi:10.1002/9781118661895.ch2

THE ROLE OF HSF1 PROTEIN REGULATION ON NEURODEGENERATION

Kim, E. (2017) · doi:10.21007/etd.cghs.2017.0432

Lysosomal interplay between ubiquitination and phosphorylation regulates chaperone-mediated autophagy

Rakshit, M. (2017) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/72725

Role of Molecular Chaperone Network in Understanding In Vitro Proteotoxicity

Srivastava, T., Sharma, S., & Priya, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804667-8.00008-0 · Cited by 1

Keeping it Together. Axonal Transport to the Synapse and the Effects of Molecular Chaperones in Health and Disease

Sinadinos, C., & Mudher, A. K. (2010) · Springer eBooks · doi:10.1007/978-1-4419-7061-9_5

The N-terminal sequence of murine PRMT5 variant 2 is required for Hsp70 interaction and CHIP ligase-mediated degradation

Lu, W., Kim, J., Tabara, S., Kwon, C., Mizukami, H., Kimura, K., & Fukamizu, A. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.077

The cochaperone and ubiquitin ligase CHIP in protein quality control

Dai, Q. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/3tfn-ca45

Thiol-Based Redox Signaling: Impacts on Molecular Chaperones and Cellular Proteostasis

Ford, A. E., & Morano, K. A. (2019) · Heat shock proteins · doi:10.1007/978-3-030-03952-3_1

Chaperone-Mediated Autophagy

Wong, E. S. P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00078-6

THE ROLE OF MICROTUBULE-ASSOCIATED PROTEIN TAU IN NEURONAL EXCITABILITY AND EPILEPTOGENESIS

Cloyd, R. (2021) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2021.271

On some topological concepts via the lattice of closed sets

Mukherjee, M., & Sengupta, A. (2004) · Revista de la Academia Canaria de Ciencias: = Folia Canariensis Academiae Scientiarum

Biomedicine & Diseases: Review RNA and protein-dependent mechanisms in tauopathies: consequences for therapeutic strategies

Gallo, J., Noble, W. J., & Martin, T. R. (2007)

Exploring the human Hsp70-Hop-Hsp90 system for Tau recognition

Moll, A. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9131

Rodent models of Alzheimer’s disease

Kasza, Á. (2018) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.9743

Heat Shock Proteins for Neurological Gene Therapy

Howarth, J. L., Kelly, S., & Uney, J. B. (2006) · CRC Press eBooks · doi:10.3109/9781420016390-5

Extracellular Tau Oligomers Induce Disruption of Endogenous Tau Distribution, Invasion of Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E. C. (2017) · doi:10.18130/v3p643

CHIP ubiquitin ligase is involved in the nucleolar stress managementPreprint

Piechota, M. J., Biriczová, L., Kowalski, K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.17.492288

CHIP mediates CAD ubiquitination and degradation to suppress the proliferation and colony formation of glioblastoma cellsPreprint

Li, G., Xiao, K., Li, Y., Gao, J., He, S., & Li, T. (2022) · Research Square · doi:10.21203/rs.3.rs-2182862/v1

Reducing neurodegeneration and oxidative damage in Alzheimer's disease: Role of the Nrf2 pathway activation by natural compounds

Villavicencio-Tejo, F., & Quintanilla, R. A. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-90052-2.00003-2

The Mechanistic Approach Involved in the Progression of Neurodegenerative Disorders

Rather, M. A., Khan, A., Alsharani, S., Jahan, S., Siddiqui, A. J., Mehan, S., & Alexiou, A. T. (2023) · Springer eBooks · doi:10.1007/978-981-99-3848-3_2

Additional file 1 of P2X7 receptor inhibition ameliorates ubiquitin–proteasome system dysfunction associated with Alzheimer’s disease

Bianchi, C., Alvarez‐Castelao, B., Sebastián‐Serrano, Á., Lauro, C. D., Soria-Tobar, L., Nicke, A., Engel, T., & Dı́az-Hernández, M. (2023) · Figshare · doi:10.6084/m9.figshare.23354460

Identification of HSP70 genes in Diaphorina citri Kuwayama Reveals Their Involvement in Immunity and Development

Li, R., Du, Y., Zhou, Y., et al. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01232-4

Prefoldin 5 is a microtubule-associated protein that suppresses Tau-aggregation and neurotoxicityPreprint

Bisht, A., Pippadpally, S., Majumder, S., Gopi, A. T., Das, A., Sahi, C., Ramaswami, M., & Kumar, V. (2024) · eLife · doi:10.7554/elife.104691.1

Molecular and Cellular Mechanisms of Primary Tauopathies

Gong, S., & Gan, L. (2025) · Oxford University Press eBooks · doi:10.1093/med/9780197640654.003.0056

Cocktail gene therapy (CGT) for neurodegenerative diseases: Targeting protein clearance systems

Zhang, H., & Teplow, D. B. (2025) · Medical Hypotheses · doi:10.1016/j.mehy.2025.111814

Prefoldin 5 is a microtubule-associated protein that suppresses Tau-aggregation and neurotoxicityPreprint

Bisht, A., Pippadpally, S., Majumder, S., Gopi, A. T., Das, A., Sahi, C., Ramaswami, M., & Kumar, V. (2025) · eLife · doi:10.7554/elife.104691.2

Molecular chaperones mediated proteostasis depletion: A cause of neurodegeneration?

Kinger, S., Choudhary, A., Kumar, P., Jagtap, Y. A., Sharma, V., Dhiman, R., Prasad, A., Verma, R., Chinnathambi, S., & Mishra, A. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.033

Therapeutic targets in diabetic peripheral neuropathy: heat shock proteins

Yin, C., Lv, J., Huang, S., Lang, C., Zhao, Y., Wang, G., Kan, J.-M., & Wang, X. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1729488

From Creator to Terminator: Co-Chaperones That Link Molecular Chaperones to the Ubiquitin/Proteasome System

Höhfeld, J., Böhse, K., Genau, M., et al. (2007) · Springer eBooks · doi:10.1007/978-0-387-49310-7_10

Additional file 2 of P2X7 receptor inhibition ameliorates ubiquitin–proteasome system dysfunction associated with Alzheimer’s disease

Bianchi, C., Alvarez‐Castelao, B., Sebastián‐Serrano, Á., Lauro, C. D., Soria-Tobar, L., Nicke, A., Engel, T., & Dı́az-Hernández, M. (2023) · Figshare · doi:10.6084/m9.figshare.23354463

Additional file 1 of Treadmill exercise promotes E3 ubiquitin ligase to remove amyloid β and P-tau and improve cognitive ability in APP/PS1 transgenic mice

Xu, L., Li, M., Wei, A., Yang, M., Li, C., Liu, R., Zheng, Y., Chen, Y., Wang, Z., Wang, K., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21275870

Synergistic MAPT mutations as a platform to uncover modifiers of tau pathogenesisPreprint

Bryan, M. R., Almeida, M. F., Pellegrino, K., Opland, C. K., Paulakonis, J. E., McGillion-Moore, J., Trzeciakiewicz, H., King, D. P., Tian, X., Tseng, J., et al. (2025) · eLife · doi:10.7554/elife.109145 · Cited by 1

Synergistic MAPT mutations as a platform to uncover modifiers of tau pathogenesisPreprint

Bryan, M. R., Almeida, M. F., Pellegrino, K., Opland, C. K., Paulakonis, J. E., McGillion-Moore, J., Trzeciakiewicz, H., King, D. P., Tian, X., Tseng, J., et al. (2025) · eLife · doi:10.7554/elife.109145.1

P3–294: The impact of chip on neurodegenerative diseases

Petrucelli, L., Dickey, C. A., Dickson, D. W., Hutton, M., Patterson, C., & Caldwell, G. A. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1563

In vivo evidence of CHIP up‐regulation attenuating tau aggregation

Sahara, N., Murayama, M., Mizoroki, T., Urushitani, M., Imai, Y., Takahashi, R., Murata, S., Tanaka, K., & Takashima, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03272.x · Cited by 208

P3-228 Chip and HSP70 regulate tau ubiquitination, degradation and aggregation

Petrucelli, L., Taylor, J. P., Kehoe, K. J., Lewis, J. M., McGowan, E. M., Snyder, H. M., Wolozin, B. L., Dawson, T. M., DILLMANN, W. H., Voellmy, R. W., et al. (2004) · Neurobiology of Aging · doi:10.1016/s0197-4580(04)81378-2 · Cited by 6

P3–314: Molecular chaperone related tau protein metabolism in human brain

Sahara, N., Togo, T., Maeda, S., Mizoroki, T., Murayama, M., Hirayasu, Y., & Takashima, A. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1584

Hsp multichaperone complex buffers pathologically modified TauPreprint

Moll, A., Ramirez, L. M., Ninov, M., Schwarz, J., Urlaub, H., & Zweckstetter, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.18.484853 · Cited by 1