Protein misfolding in neurodegenerative diseases: Implications and strategies

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works

The amyloid state and its association with protein misfolding diseases.

Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382 · see citing works

Immune attack: the role of inflammation in Alzheimer disease

Heppner, F. L., Ransohoff, R. M., & Becher, B. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3880 · Cited by 2,134 · see citing works

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764 · see citing works

Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS

Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235 · see citing works

Converging concepts of protein folding in vitro and in vivo

Hartl, F. U., & Hayer-Hartl, M. K. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1591 · Cited by 1,186 · see citing works

ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models

Cramer, P. E., Cirrito, J. R., Wesson, D. W., Lee, C. Y. D., Karlo, J. C., Zinn, A. E., Casali, B. T., Restivo, J. L., Goebel, W. D., James, M. J., et al. (2012) · Science · doi:10.1126/science.1217697 · Cited by 1,050 · see citing works

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works

Misfolded proteins partition between two distinct quality control compartments

Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932 · see citing works

Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies

Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898 · see citing works

Neuronal activity enhances tau propagation and tau pathology in vivo

Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820 · see citing works

Spreading of pathology in neurodegenerative diseases: a focus on human studies

Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790 · see citing works

Prion-like transmission of protein aggregates in neurodegenerative diseases

Brundin, P., Melki, R., & Kopito, R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2873 · Cited by 778 · see citing works

The Evolution of Preclinical Alzheimer’s Disease: Implications for Prevention Trials

Sperling, R., Mormino, E., & Johnson, K. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.038 · Cited by 725 · see citing works

HSF1 Drives a Transcriptional Program Distinct from Heat Shock to Support Highly Malignant Human Cancers

Mendillo, M. L., Santagata, S., Koeva, M., Bell, G. W., Hu, R., Tamimi, R. M., Fraenkel, E., Ince, T. A., Whitesell, L. J., & Lindquist, S. L. (2012) · Cell · doi:10.1016/j.cell.2012.06.031 · Cited by 696 · see citing works

Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

Olzscha, H., Schermann, S. M., Woerner, A. C., Pinkert, S., Hecht, M. H., Tartaglia, G. G., Vendruscolo, M., Hayer-Hartl, M. K., Hartl, F. U., & Vabulas, R. M. (2011) · Cell · doi:10.1016/j.cell.2010.11.050 · Cited by 692 · see citing works

Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680 · see citing works

Amyloid fibril formation by an SH3 domain

Guijarro, J. I., Sunde, M., Jones, J. A., Campbell, I. D., & Dobson, C. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.8.4224 · Cited by 669 · see citing works

Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like Tauopathy

Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works

Proteostasis impairment in protein-misfolding and -aggregation diseases

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 656 · see citing works

Progressive disruption of cellular protein folding in models of polyglutamine diseases

Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006) · Science · doi:10.1126/science.1124514 · Cited by 643 · see citing works

α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease

Di Maio, R., Barrett, P. J., Hoffman, E. K., Barrett, C. W., Zharikov, A., Borah, A., Hu, X., McCoy, J., Chu, C. T., Burton, E. A., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf3634 · Cited by 619 · see citing works

Oxidative stress: A major pathogenesis and potential therapeutic target of antioxidative agents in Parkinson’s disease and Alzheimer’s disease

Jiang, T., Sun, Q., & Chen, S. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.07.005 · Cited by 594 · see citing works

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease

Brehme, M., Voisine, C., Rolland, T., Wachi, S., Soper, J. H., Zhu, Y., Orton, K., Villella, A., Garza, D., Vidal, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.042 · Cited by 584 · see citing works

Imaging synaptic density in the living human brain

Finnema, S. J., Nabulsi, N. B., Eid, T., Detyniecki, K., Lin, S.-F., Chen, M.-K., Dhaher, R., Matuskey, D., Baum, E., Holden, D., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf6667 · Cited by 575 · see citing works

Clearance of Amyloid-β Peptide Across the Blood-Brain Barrier: Implication for Therapies in Alzheimers Disease

Deane, R., Bell, R. D., Sagare, A. P., & Zloković, B. V. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601867 · Cited by 549 · see citing works

Aging as an event of proteostasis collapse

Taylor, R. C., & Dillin, A. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004440 · Cited by 538 · see citing works

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Cellular Strategies of Protein Quality ControlPreprint

Chen, B., Retzlaff, M., Roos, T. R., & Frydman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004374 · Cited by 499 · see citing works

Elusive roles for reactive astrocytes in neurodegenerative diseases

Ben Haim, L., Carrillo-de Sauvage, M.-A., Ceyzériat, K., & Escartin, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00278 · Cited by 453 · see citing works

GSK-3β, a pivotal kinase in Alzheimer disease

Llorens-Marítin, M., Jurado, J., Hernández, F., & Ávila, J. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00046 · Cited by 451 · see citing works

Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling

Myeku, N., Clelland, C. L., Emrani, S., Kukushkin, N. V., Yu, W. H., Goldberg, A. L., & Duff, K. E. (2016) · Nature Medicine · doi:10.1038/nm.4011 · Cited by 446 · see citing works

Control of autophagy as a therapy for neurodegenerative disease

Harris, H., & Rubinsztein, D. C. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.200 · Cited by 445 · see citing works

Extracellular vesicles in neurodegenerative disease — pathogenesis to biomarkers

Thompson, A. G., Gray, E., Heman-Ackah, S. M., Mäger, I., Talbot, K., Andaloussi, S. E., Wood, M. J., & Turner, M. R. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.68 · Cited by 431 · cited 1× · see citing works

Structure of an Intermediate State in Protein Folding and Aggregation

Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine‐Afsar, A., Sharpe, S. J., Vendruscolo, M., & Kay, L. E. (2012) · Science · doi:10.1126/science.1214203 · Cited by 399 · see citing works

The BACE1 inhibitor verubecestat (MK-8931) reduces CNS β-amyloid in animal models and in Alzheimer’s disease patients

Kennedy, M., Stamford, A., Chen, X., Cox, K., Cumming, J., Dockendorf, M., Egan, M. F., Ereshefsky, L., Hodgson, R., Hyde, L., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad9704 · Cited by 391 · see citing works

Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

Woerner, A. C., Frottin, F., Hornburg, D., Feng, L., Meissner, F., Patra, M., Tatzelt, J., Mann, M., Winklhofer, K. F., Hartl, F. U., et al. (2015) · Science · doi:10.1126/science.aad2033 · Cited by 386 · see citing works

Integrated genomics and proteomics define huntingtin CAG length-dependent networks in mice

Langfelder, P., Cantle, J. P., Chatzopoulou, D., Wang, N., Gao, F., Al-Ramahi, I., Lu, X.-H., Ramos, E. M., El-Zein, K., Zhao, Y., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4256 · Cited by 385 · see citing works

Distinct RolesIn Vivofor the Ubiquitin–Proteasome System and the Autophagy–Lysosomal Pathway in the Degradation of α-Synuclein

Ebrahimi‐Fakhari, D., Cantuti‐Castelvetri, I., Fan, Z., Rockenstein, E. M., Masliah, E., Hyman, B. T., McLean, P. J., & Unni, V. K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.1560-11.2011 · Cited by 378 · see citing works

Alpha-Synuclein Oligomers—Neurotoxic Molecules in Parkinson's Disease and Other Lewy Body Disorders

Ingelsson, M. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00408 · Cited by 374 · see citing works

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

Höhn, A., Weber, D., Jung, T., Ott, C., Hugo, M., Kochlik, B., Kehm, R., König, J., Grune, T., & Castro, J. P. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.001 · Cited by 368 · see citing works

Il10 Deficiency Rebalances Innate Immunity to Mitigate Alzheimer-Like Pathology

Guillot-Sestier, M.-V., Doty, K. R., Gate, D., Rodriguez, J., Leung, B. P., Rezai-Zadeh, K., & Town, T. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.068 · Cited by 363 · see citing works

IL-10 Alters Immunoproteostasis in APP Mice, Increasing Plaque Burden and Worsening Cognitive Behavior

Chakrabarty, P., Li, A., Ceballos-Diaz, C., Eddy, J. A., Funk, C. C., Moore, B., DiNunno, N., Rosario, A. M., Cruz, P. E., Verbeeck, C., et al. (2015) · Neuron · doi:10.1016/j.neuron.2014.11.020 · Cited by 354 · see citing works

The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution

Dantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 336 · see citing works

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

Escusa-Toret, S., Vonk, W. I. M., & Frydman, J. (2013) · Nature Cell Biology · doi:10.1038/ncb2838 · Cited by 321 · see citing works

DNAJC13 mutations in Parkinson disease

Vilariño‐Güell, C., Rajput, A. H., Milnerwood, A. J., Shah, B., Szu‐Tu, C., Trinh, J., Yu, I. S., Encarnacion, M. J., Munsie, L. N., Tapia, L., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt570 · Cited by 313 · see citing works

Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases

Neef, D. W., Jaeger, A. M., & Thiele, D. J. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3453 · Cited by 307 · see citing works

Missorting of Tau in Neurons Causes Degeneration of Synapses That Can Be Rescued by the Kinase MARK2/Par-1

Thies, E., & Mandelkow, E.-M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4674-06.2007 · Cited by 293 · see citing works

Post-translational modifications of Hsp90 and their contributions to chaperone regulation

Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288 · see citing works

Immunotherapeutic Approaches for Alzheimer’s Disease

Wisniewski, T., & Goñi, F. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.064 · Cited by 284 · see citing works

Tau PET imaging: present and future directions

Saint‐Aubert, L., Lemoine, L., Chiotis, K., Leuzy, A., Rodriguez‐Vieitez, E., & Nordberg, A. K. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0162-3 · Cited by 283 · see citing works

A critique of the drug discovery and phase 3 clinical programs targeting the amyloid hypothesis for Alzheimer disease

Karran, E. H., & Hardy, J. (2014) · Annals of Neurology · doi:10.1002/ana.24188 · Cited by 275 · see citing works

Interface between tauopathies and synucleinopathies: A tale of two proteins

Galpern, W. R., & Lang, A. E. (2006) · Annals of Neurology · doi:10.1002/ana.20819 · Cited by 263 · see citing works

Immune aging, dysmetabolism, and inflammation in neurological diseases

Deleidi, M., Jäggle, M., & Rubino, G. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00172 · Cited by 260 · see citing works

Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells

Albanèse, V., Yam, A. Y.-W., Baughman, J. M., Parnot, C., & Frydman, J. (2006) · Cell · doi:10.1016/j.cell.2005.11.039 · Cited by 254 · see citing works

Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events

Jackrel, M. E., DeSantis, M. E., Martinez, B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.11.047 · Cited by 246 · see citing works

Targeting Hsp90/Hsp70-Based Protein Quality Control for Treatment of Adult Onset Neurodegenerative Diseases

Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124332 · Cited by 241 · see citing works

Soluble forms of tau are toxic in Alzheimer's disease

Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232 · see citing works

Challenges and opportunities for non-antibody scaffold drugs

Vazquez-Lombardi, R., Phan, T. G., Zimmermann, C., Lowe, D., Jermutus, L., & Christ, D. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.09.004 · Cited by 226 · see citing works

Antibody-based PET imaging of amyloid beta in mouse models of Alzheimer’s disease

Sehlin, D., Fang, X. T., Cato, L., Antoni, G., Lannfelt, L., & Syvänen, S. (2016) · Nature Communications · doi:10.1038/ncomms10759 · Cited by 223 · see citing works

Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells

Lee, J., Takahama, S., Zhang, G., Tomarev, S. I., & Ye, Y. (2016) · Nature Cell Biology · doi:10.1038/ncb3372 · Cited by 217 · see citing works

DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative‐associated proteins

Fontaine, S. N., Zheng, D., Sabbagh, J. J., Martin, M. D., Chaput, D., Darling, A. L., Trotter, J. H., Stothert, A. R., Nordhues, B. A., Lussier, A. L., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593489 · Cited by 206 · see citing works

Human glia can both induce and rescue aspects of disease phenotype in Huntington disease

Benraiss, A., Wang, S., Herrlinger, S., Li, X., Chandler-Militello, D., Mauceri, J., Burm, H. B., Toner, M., Osipovitch, M., Jim Xu, Q., et al. (2016) · Nature Communications · doi:10.1038/ncomms11758 · Cited by 199 · see citing works

Destabilizing Protein Polymorphisms in the Genetic Background Direct Phenotypic Expression of Mutant SOD1 Toxicity

Gidalevitz, T., Krupinski, T., Garcia, S. M. D. A., & Morimoto, R. I. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000399 · Cited by 191 · see citing works

Operational Plasticity Enables Hsp104 to Disaggregate Diverse Amyloid and Nonamyloid Clients

DeSantis, M. E., Leung, E. H., Sweeny, E. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.09.038 · Cited by 184 · see citing works

A Sensitive Aβ Oligomer Assay Discriminates Alzheimer's and Aged Control Cerebrospinal Fluid

Savage, M. J., Kalinina, J., Wolfe, A. L., Tugusheva, K., Korn, R., Cash-Mason, T., Maxwell, J. W., Hatcher, N. G., Haugabook, S. J., Wu, G., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1675-13.2014 · Cited by 183 · see citing works

An evolutionarily conserved pathway controls proteasome homeostasis

Rousseau, A., & Bertolotti, A. (2016) · Nature · doi:10.1038/nature18943 · Cited by 182 · see citing works

Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease

Labbadia, J. P., Cunliffe, H. E., Weiss, A., Katsyuba, E., Sathasivam, K., Seredenina, T. S., Woodman, B., Moussaoui, S. M., Frentzel, S., Luthi‐Carter, R., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57413 · Cited by 173 · see citing works

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington’s disease

Hipp, M. S., Patel, C. N., Bersuker, K., Riley, B. E., Kaiser, S. E., Shaler, T. A., Brandeis, M., & Kopito, R. R. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201110093 · Cited by 169 · see citing works

Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain

Pearce, M. M. P., Spartz, E. J., Hong, W., Luo, L., & Kopito, R. R. (2015) · Nature Communications · doi:10.1038/ncomms7768 · Cited by 159 · see citing works

Defining the Specificity of Cotranslationally Acting Chaperones by Systematic Analysis of mRNAs Associated with Ribosome-Nascent Chain Complexes

del Álamo, M., Hogan, D. J., Pechmann, S., Albanèse, V., Brown, P. O., & Frydman, J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001100 · Cited by 158 · see citing works

Sorting out the trash: the spatial nature of eukaryotic protein quality control

Sontag, E. M., Vonk, W. I. M., & Frydman, J. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.12.006 · Cited by 146 · see citing works

Disruption of Protein Quality Control in Parkinson's DiseasePreprint

Cook, C. N., Stetler, C. T., & Petrucelli, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009423 · Cited by 145 · see citing works

Generation and characterization of novel conformation-specific monoclonal antibodies for α-synuclein pathology

Vaikath, N. N., Majbour, N. K., Paleologou, K. E., Ardah, M. T., van Dam, E., van de Berg, W. D. J., Forrest, S. L., Parkkinen, L., Gai, W., Hattori, N., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.04.009 · Cited by 142 · see citing works

Seeded strain‐like transmission of β‐amyloid morphotypes in APP transgenic mice

Heilbronner, G., Eisele, Y. S., Langer, F., Kaeser, S. A., Novotny, R., Nagarathinam, A., Åslund, A., Hammarström, P., Nilsson, K. P. R., & Jucker, M. (2013) · EMBO Reports · doi:10.1038/embor.2013.137 · Cited by 139 · see citing works

Accelerating drug discovery for Alzheimer's disease: best practices for preclinical animal studies

Shineman, D. W., Basi, G. S., Bizon, J. L., Colton, C. A., Greenberg, B., Hollister, B. A., Lincecum, J. M., Leblanc, G. G., Lee, L. H., Luo, F. R., et al. (2011) · Alzheimer s Research & Therapy · doi:10.1186/alzrt90 · Cited by 136 · see citing works

Reversal of apoE4-driven brain pathology and behavioral deficits by bexarotene

Boehm-Cagan, A., & Michaelson, D. M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.5198-13.2014 · Cited by 134 · see citing works

Animal models of Alzheimer disease: historical pitfalls and a path forward

Cavanaugh, S. E. (2014) · ALTEX · doi:10.14573/altex.1310071 · Cited by 132 · see citing works

The Parkinson’s-associated protein DJ-1 regulates the 20S proteasome

Moscovitz, O., Ben‐Nissan, G., Fainer, I., Pollack, D., Mizrachi, L., & Sharon, M. (2015) · Nature Communications · doi:10.1038/ncomms7609 · Cited by 126 · see citing works

SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS

Pujol‐Pina, R., Vilaprinyó-Pascual, S., Mazzucato, R., Arcella, A., Vilaseca, M., Orozco, M., & Carulla, N. (2015) · Scientific Reports · doi:10.1038/srep14809 · Cited by 114 · see citing works

Intraneuronal protein aggregation as a trigger for inflammation and neurodegeneration in the aging brain

Currais, A. J. M., Fischer, W. H., Maher, P. A., & Schubert, D. A. (2016) · The FASEB Journal · doi:10.1096/fj.201601184 · Cited by 114 · see citing works

Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

Woods, L. A., Platt, G. W., Hellewell, A. L., Hewitt, E. W., Homans, S. W., Ashcroft, A. E., & Radford, S. E. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.635 · Cited by 110 · see citing works

Aβ-amyloid and Tau Imaging in Dementia

Villemagne, V. L., Doré, V., Bourgeat, P., Burnham, S. C., Laws, S., Salvado, O., Masters, C. L., & Rowe, C. C. (2017) · Seminars in Nuclear Medicine · doi:10.1053/j.semnuclmed.2016.09.006 · Cited by 110 · see citing works

Autophagy in neurodegenerative diseases: From pathogenic dysfunction to therapeutic modulation

Martínez‐Vicente, M. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.03.005 · Cited by 109 · see citing works

Molecular chaperones and neuronal proteostasis

Smith, H., Li, W., & Cheetham, M. E. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.03.003 · Cited by 107 · see citing works

The Chemical Biology of Molecular Chaperones—Implications for Modulation of Proteostasis

Brandvold, K. R., & Morimoto, R. I. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.05.010 · Cited by 105 · see citing works

A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis

Albanèse, V., Reißmann, S., & Frydman, J. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001054 · Cited by 100 · see citing works

Targeting Human Central Nervous System Protein Kinases: An Isoform Selective p38αMAPK Inhibitor That Attenuates Disease Progression in Alzheimer’s Disease Mouse Models

Roy, S. M., Grum-Tokars, V. L., Schavocky, J. P., Saeed, F., Staniszewski, A., Teich, A. F., Arancio, O., Bachstetter, A. D., Webster, S. J., Van Eldik, L. J., et al. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00002 · Cited by 99 · see citing works

Alpha-synuclein and beta-amyloid – different targets, same players: calcium, free radicals and mitochondria in the mechanism of neurodegeneration

Angelova, P. R., & Abramov, A. Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.103 · Cited by 98 · see citing works

Chaperones in Neurodegeneration

Lindberg, I., Shorter, J., Wiseman, R. L., Chiti, F., Dickey, C. A., & McLean, P. J. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2600-15.2015 · Cited by 97 · see citing works

Molecular basis for mid-region amyloid-β capture by leading Alzheimer's disease immunotherapies

Crespi, G. A. N., Hermans, S. J., Parker, M. W., & Miles, L. A. (2015) · Scientific Reports · doi:10.1038/srep09649 · Cited by 96 · see citing works

NEDD4-mediated HSF1 degradation underlies α-synucleinopathy

Kim, E., Wang, B., Sastry, N. G., Masliah, E., Nelson, P. T., Cai, H., & Liao, F. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv445 · Cited by 96 · see citing works

Ion Mobility Spectrometry Reveals the Mechanism of Amyloid Formation of Aβ(25–35) and Its Modulation by Inhibitors at the Molecular Level: Epigallocatechin Gallate andScyllo-inositol

Bleiholder, C., Do, T. D., Wu, C. F., Economou, N. J., Bernstein, S. L., Buratto, S. K., Shea, J., & Bowers, M. T. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406197f · Cited by 93 · see citing works

Natural Compounds May Open New Routes to Treatment of Amyloid Diseases

Bieschke, J. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0192-7 · Cited by 84 · see citing works

Amyloidogenic sequences in native protein structures

Tzotzos, S. J., & Doig, A. J. (2009) · Protein Science · doi:10.1002/pro.314 · Cited by 83 · see citing works

mTOR independent regulation of macroautophagy by Leucine Rich Repeat Kinase 2 via Beclin-1

Manzoni, C., Mamais, A., Roosen, D. A., Dihanich, S., Soutar, M. P. M., Plun‐Favreau, H., Bandopadhyay, R., Hardy, J., Tooze, S. A., Cookson, M., et al. (2016) · Scientific Reports · doi:10.1038/srep35106 · Cited by 83 · see citing works

Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT

Hayashida, N., Fujimoto, M., Tan, K., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.225 · Cited by 82 · see citing works

Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors

Jaeger, A. M., Pemble, C. W., IV, Sistonen, L., & Thiele, D. J. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3150 · Cited by 79 · see citing works

Neuronal response in Alzheimer’s and Parkinson’s disease: the effect of toxic proteins on intracellular pathways

Majd, S., Power, J. H. T., & Grantham, H. J. M. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0211-1 · Cited by 76 · see citing works

Abeta targets of the biosimilar antibodies of Bapineuzumab, Crenezumab, Solanezumab in comparison to an antibody against N-truncated Abeta in sporadic Alzheimer disease cases and mouse models

Bouter, Y., López‐Noguerola, J. S., Tucholla, P., Crespi, G. A. N., Parker, M. W., Wiltfang, J., Miles, L. A., & Bayer, T. A. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1489-x · Cited by 74 · see citing works

The unpredictability of prolonged activation of stress response pathways

Lamech, L. T., & Haynes, C. M. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201503107 · Cited by 72 · see citing works

HSF1 Protects Neurons through a Novel Trimerization- and HSP-Independent Mechanism

Verma, P., Pfister, J. A., Mallick, S., & D’Mello, S. R. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3039-13.2014 · Cited by 70 · see citing works

Facilitated Tau Degradation by USP14 Aptamers via Enhanced Proteasome Activity

Lee, J. H., Shin, S. K., Jiang, Y., Choi, W. H., Hong, C., Kim, D., & Lee, M. J. (2015) · Scientific Reports · doi:10.1038/srep10757 · Cited by 69 · see citing works

Antibodies and protein misfolding: From structural research tools to therapeutic strategies

Genst, E. D., Messer, A. C., & Dobson, C. M. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.08.016 · Cited by 69 · see citing works

A CNS-permeable Hsp90 inhibitor rescues synaptic dysfunction and memory loss in APP-overexpressing Alzheimer’s mouse model via an HSF1-mediated mechanism

Wang, B., Liu, Y., Huang, L., Chen, J., Li, J. J., Wang, R., Kim, E., Chen, Y., Justicia, C., Sakata, K., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.104 · Cited by 69 · see citing works

Network dysfunction in<i>α</i>‐synuclein transgenic mice and human Lewy body dementia

Morris, M., Sanchez, P. E., Verret, L., Beagle, A. J., Guo, W., Dubal, D., Ranasinghe, K. G., Koyama, A., Ho, K., Yu, G., et al. (2015) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.257 · Cited by 61 · see citing works

Do current therapeutic anti-Aβ antibodies for Alzheimer’s disease engage the target?

Watt, A. D., Crespi, G. A. N., Down, R. A., Ascher, D. B., Gunn, A. P., Perez, K. A., McLean, C., Villemagne, V. L., Parker, M. W., Barnham, K. J., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1290-2 · Cited by 60 · see citing works

Heat shock factor-1 influences pathological lesion distribution of polyglutamine-induced neurodegeneration

Kondo, N., Katsuno, M., Adachi, H., et al. (2013) · Nature Communications · doi:10.1038/ncomms2417 · Cited by 57 · see citing works

A Cellular Model To Monitor Proteasome Dysfunction by α-Synuclein

Nonaka, T., & Hasegawa, M. (2009) · Biochemistry · doi:10.1021/bi900619j · Cited by 55 · see citing works

Targeting chaperones, heat shock factor-1, and unfolded protein response: Promising therapeutic approaches for neurodegenerative disorders

Bose, S., & Cho, J. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.09.004 · Cited by 55 · see citing works

Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity

Mack, K. L., & Shorter, J. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00008 · Cited by 54 · see citing works

Heat Shock Response Activation Exacerbates Inclusion Body Formation in a Cellular Model of Huntington Disease

Bersuker, K., Hipp, M. S., Calamini, B., Morimoto, R. I., & Kopito, R. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.481945 · Cited by 51 · see citing works

Conophylline Protects Cells in Cellular Models of Neurodegenerative Diseases by Inducing Mammalian Target of Rapamycin (mTOR)-independent Autophagy

Sasazawa, Y., Sato, N., Umezawa, K., & Simizu, S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.606293 · Cited by 46 · see citing works

Comparing the efficacy and neuroinflammatory potential of three anti-abeta antibodies

Fuller, J. P., Stavenhagen, J. B., Christensen, S., Kartberg, F., Glennie, M. J., & Teeling, J. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1484-2 · Cited by 44 · see citing works

Stabilization of α-Synuclein Fibril Clusters Prevents Fragmentation and Reduces Seeding Activity and Toxicity

Lam, H. T., Graber, M. C., Gentry, K. A., et al. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01168 · Cited by 44 · see citing works

Functional Significance of Point Mutations in Stress Chaperone Mortalin and Their Relevance to Parkinson Disease

Wadhwa, R., Ryu, J., Ahn, H. M., Saxena, N., Chaudhary, A., Yun, C., & Kaul, S. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.627463 · Cited by 43 · see citing works

Heat shock protein 104 inhibited the fibrillization of prion peptide 106–126 and disassembled prion peptide 106–126 fibrils in vitro

Liu, Y., Han, Y., Song, J., et al. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.01.022 · Cited by 38 · see citing works

Analysis of Chaperone mRNA Expression in the Adult Mouse Brain by Meta Analysis of the Allen Brain Atlas

Tebbenkamp, A. T. N., & Borchelt, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013675 · Cited by 36 · see citing works

Ubiquitin-Proteasome System in Neurodegenerative Disorders

Croft, G. R. B. (2015) · Journal of Drug Metabolism & Toxicology · doi:10.4172/2157-7609.1000187 · Cited by 34 · see citing works

Amphoterin Includes a Sequence Motif Which Is Homologous to the Alzheimer's β-Amyloid Peptide (Aβ), Forms Amyloid Fibrils in Vitro, and Binds Avidly to Aβ

Kallijärvi, J., Haltia, M., & BAUMANN, M. H. (2001) · Biochemistry · doi:10.1021/bi002095n · Cited by 33 · see citing works

The ubiquitin proteasome system as a potential therapeutic target for treatment of neurodegenerative diseases.

Opattová, A., Cente, M., Novak, M., & Filipčík, P. (2015) · PubMed · doi:10.4149/gpb_2015024 · Cited by 32 · see citing works

Linking HSP90 target occupancy to HSP70 induction and efficacy in mouse brain

Thirstrup, K., Sotty, F., Montezinho, L., Badolo, L., Thougaard, A., Kristjánsson, M., Jensen, T. N., Watson, S. P., & Nielsen, S. M. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.12.028 · Cited by 28 · see citing works

Regulating extracellular proteostasis capacity through the unfolded protein response

Genereux, J. C., & Wiseman, R. L. (2015) · Prion · doi:10.1080/19336896.2015.1011887 · Cited by 27 · see citing works

Neurodegeneration and the Heat Shock Protein 70 Machinery: Implications for Therapeutic Development

Fontaine, S. N., Martin, M. D., & Dickey, C. A. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160413140741 · Cited by 24 · see citing works

Inhibition of Both Hsp70 Activity and Tau Aggregation in Vitro Best Predicts Tau Lowering Activity of Small Molecules

Martin, M. D., Baker, J. D., Suntharalingam, A., Nordhues, B. A., Shelton, L. B., Zheng, D., Sabbagh, J. J., Haystead, T., Gestwicki, J. E., & Dickey, C. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00223 · Cited by 22 · see citing works

Non-Amyloid PET Imaging Biomarkers for Neurodegeneration: Focus on Tau, Alpha-Synuclein and Neuroinflammation

Catafau, A. M., & Bullich, S. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160620111408 · Cited by 21 · see citing works

Differential roles of NF-Y transcription factor in ER chaperone expression and neuronal maintenance in the CNS

Yamanaka, T., Tosaki, A., Miyazaki, H., Kurosawa, M., Koike, M., Uchiyama, Y., Maity, S. N., Misawa, H., Takahashi, R., Shimogori, T., et al. (2016) · Scientific Reports · doi:10.1038/srep34575 · Cited by 17 · see citing works

In Vivo Profiling Reveals a Competent Heat Shock Response in Adult Neurons: Implications for Neurodegenerative Disorders

Carnemolla, A., Lazell, H., Moussaoui, S. M., & Bates, G. P. (2015) · PLoS ONE · doi:10.1371/journal.pone.0131985 · Cited by 13 · see citing works

Rewiring macrophages for anti-tumour immunity

Lee, Y., & Biswas, S. K. (2016) · Nature Cell Biology · doi:10.1038/ncb3384 · Cited by 11 · see citing works

Imaging Neurodegeneration: Steps Toward Brain Network-Based Pathophysiology and Its Potential for Multi-modal Imaging Diagnostics

Sorg, C., Göttler, J., & Zimmer, C. (2015) · Clinical Neuroradiology · doi:10.1007/s00062-015-0438-3 · Cited by 6 · see citing works

Tau-targeting therapies for Alzheimer disease

Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · see citing works

Recent advances in carrier mediated nose-to-brain delivery of pharmaceutics

Bourganis, V., Kammona, O., Alexopoulos, A., & Kiparissides, C. (2018) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2018.05.009 · Cited by 357 · see citing works

Recent Advancements of Nanomedicine in Neurodegenerative Disorders Theranostics

Mukherjee, S., Madamsetty, V. S., Bhattacharya, D., Roy Chowdhury, S., Paul, M. K., & Mukherjee, A. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202003054 · Cited by 152 · see citing works

Multitarget Therapeutic Strategies for Alzheimer’s Disease: Review on Emerging Target Combinations

Maramai, S., Benchekroun, M., Gabr, M. T., & Yahiaoui, S. (2020) · BioMed Research International · doi:10.1155/2020/5120230 · Cited by 121 · see citing works

Beneficial Effects of Spirulina Consumption on Brain Health

Trotta, T., Porro, C., Cianciulli, A., & Panaro, M. A. (2022) · Nutrients · doi:10.3390/nu14030676 · Cited by 98 · see citing works

Extensive accumulation of misfolded protein aggregates during natural aging and senescence

Cuanalo-Contreras, K., Schulz, J., Mukherjee, A., Park, K.-W., Armijo, E., & Soto, C. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1090109 · Cited by 92 · see citing works

HDAC6 Inhibition Promotes Transcription Factor EB Activation and Is Protective in Experimental Kidney Disease

Brijmohan, A. S., Batchu, S. N., Majumder, S., Alghamdi, T. A., Thieme, K., McGaugh, S., Liu, Y., Advani, S. L., Bowskill, B. B., Kabir, M. G., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00034 · Cited by 71 · see citing works

Mass spectrometry: A platform for biomarker discovery and validation for Alzheimer's and Parkinson's diseases

Cilento, E. M., Jin, L., Stewart, T., Shi, M., Sheng, L., & Zhang, J. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14635 · Cited by 60 · see citing works

Altered neural cell junctions and ion-channels leading to disrupted neuron communication in Parkinson’s disease

Choudhury, S. P., Bano, S., Sen, S., Suchal, K., Kumar, S., Nikolajeff, F., Dey, S. K., & Sharma, V. (2022) · npj Parkinson's Disease · doi:10.1038/s41531-022-00324-9 · Cited by 52 · see citing works

Loss of <i>Fis1</i> impairs proteostasis during skeletal muscle aging in <i>Drosophila</i>

Lee, T., Chen, P., Su, M. P., Li, J., Chang, Y., Liu, R., Juan, H., Yang, J., Chan, S., Tsai, Y., et al. (2021) · Aging Cell · doi:10.1111/acel.13379 · Cited by 27 · see citing works

DNA damage as a marker of brain damage in individuals with history of concussions

Schwab, N., Tator, C., & Hazrati, L.-N. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0199-8 · Cited by 26 · see citing works

Navigating Neurodegeneration: Integrating Biomarkers, Neuroinflammation, and Imaging in Parkinson’s, Alzheimer’s, and Motor Neuron Disorders

Tanaka, M., Battaglia, S., & Liloia, D. (2025) · Biomedicines · doi:10.3390/biomedicines13051045 · Cited by 24 · see citing works

Concept and application of circulating proteasomes

Choi, W. H., Kim, S., Park, S., & Lee, M. J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00692-x · Cited by 27 · see citing works

The Effects of Aging on Proteasome Activity, Assembly, and Abundance in C. elegans

Joyce, D. (2012) · eScholarship (California Digital Library)

The effects of aging on proteasome activity, assembly, and abundance in C. elegans - eScholarship

Joyce, D. (2012)

Person‐specific differences in ubiquitin‐proteasome mediated proteostasis in human neurons

Hsieh, Y.-C., Augur, Z. M., Arbery, M. R., Ashour, N., Barrett, K., Pearse, R., Tio, E., Duong, D., Felsky, D., Jager, P. D., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13680 · Cited by 19 · see citing works

A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers

Thibaudeau, T. A., Anderson, R. T., & Smith, D. M. (2018) · Nature Communications · doi:10.1038/s41467-018-03509-0 · Cited by 362 · see citing works