Protein homeostasis and aging in neurodegeneration

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

Resveratrol improves health and survival of mice on a high-calorie diet

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882

Rapamycin fed late in life extends lifespan in genetically heterogeneous mice

Harrison, D. E., Strong, R., Sharp, Z. D., Nelson, J. F., Astle, C. M., Flurkey, K., Nadon, N. L., Wilkinson, J. E., Frenkel, K., Carter, C. S., et al. (2009) · Nature · doi:10.1038/nature08221 · Cited by 3,766

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

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 2×

IGF-1 receptor regulates lifespan and resistance to oxidative stress in mice

Holzenberger, M., Dupont, J., Ducos, B., Leneuve, P., Géloën, A., Even, P. C., Cervera, P., & Le Bouc, Y. (2003) · Nature · doi:10.1038/nature01298 · Cited by 2,109

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

Widespread Proteome Remodeling and Aggregation in Aging C. elegans

Walther, D. M., Kasturi, P., Zheng, M., Pinkert, S., Vecchi, G., Ciryam, P., Morimoto, R. I., Dobson, C. M., Vendruscolo, M., Mann, M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.032 · Cited by 569

Aging, Rejuvenation, and Epigenetic Reprogramming: Resetting the Aging Clock

Rando, T. A., & Chang, H. Y. (2012) · Cell · doi:10.1016/j.cell.2012.01.003 · Cited by 520

Extensive innate immune gene activation accompanies brain aging, increasing vulnerability to cognitive decline and neurodegeneration: a microarray study

Cribbs, D. H., Berchtold, N. C., Perreau, V., Coleman, P. D., Rogers, J., Tenner, A. J., & Cotman, C. W. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-179 · Cited by 499

Autophagy: A Key Regulator of Homeostasis and Disease: An Overview of Molecular Mechanisms and Modulators

Gómez-Virgilio, L., Silva-Lucero, M.-D.-C., Flores-Morelos, D.-S., Gallardo-Nieto, J., Lopez-Toledo, G., Abarca-Fernandez, A.-M., Zacapala-Gómez, A.-E., Luna-Muñoz, J., Montiel-Sosa, F., Soto-Rojas, L. O., et al. (2022) · Cells · doi:10.3390/cells11152262 · Cited by 431

Gut-seeded α-synuclein fibrils promote gut dysfunction and brain pathology specifically in aged mice

Challis, C., Hori, A., Sampson, T. R., Yoo, B. B., Challis, R. C., Hamilton, A. M., Mazmanian, S. K., Volpicelli-Daley, L. A., & Gradinaru, V. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0589-7 · Cited by 405

Pharmacological approaches to restore mitochondrial function

Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383

Repairing mitochondrial dysfunction in disease

Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337

Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome

Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337

Astrocytes in the aging brain express characteristics of senescence-associated secretory phenotype: Astrocyte senescence in aging brain

Salminen, A., Ojala, J., Kaarniranta, K., Haapasalo, A., Hiltunen, M., & Soininen, H. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07738.x · Cited by 333

Mammalian/mechanistic target of rapamycin (mTOR) complexes in neurodegeneration

Querfurth, H., & Lee, H.-K. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00428-5 · Cited by 288

Cellular and epigenetic drivers of stem cell ageing

Ermolaeva, M., Neri, F., Ori, A., & Rudolph, K. L. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0020-3 · Cited by 272

ER stress and UPR in Alzheimer’s disease: mechanisms, pathogenesis, treatments

Ajoolabady, A., Lindholm, D., Ren, J., & Pratico, D. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05153-5 · Cited by 261

Firefly luciferase mutants as sensors of proteome stress

Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219

Inhibition of AMP-activated protein kinase signaling alleviates impairments in hippocampal synaptic plasticity induced by amyloid β

Ma, T., Chen, Y., Vingtdeux, V., Zhao, H., Viollet, B., Marambaud, P., & Klann, E. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1694-14.2014 · Cited by 191

Skeletal muscle autophagy and its role in sarcopenia and organismal aging

Jiao, J., & Demontis, F. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.03.009 · Cited by 184

Emerging role of p62/sequestosome-1 in the pathogenesis of Alzheimer's disease

Salminen, A., Kaarniranta, K., Haapasalo, A., Hiltunen, M., Soininen, H., & Alafuzoff, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.11.005 · Cited by 153

The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases

Nixon, R. A. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140443 · Cited by 149

The Essential Role of Soluble Aβ Oligomers in Alzheimer’s Disease

Wang, Z.-X., Tan, L., Liu, J., & Yu, J.-T. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9143-0 · Cited by 110

Proteostasis and lysosomal repair deficits in transdifferentiated neurons of Alzheimer’s disease

Chou, C.-C., Vest, R., Prado, M. A., Wilson-Grady, J., Paulo, J. A., Shibuya, Y., Moran-Losada, P., Lee, T.-T., Luo, J., Gygi, S. P., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01623-y · Cited by 94

Hydralazine induces stress resistance and extends C. elegans lifespan by activating the NRF2/SKN-1 signalling pathway

Dehghan, E., Zhang, Y., Saremi, B., Yadavali, S., Hakimi, A., Dehghani, M., Goodarzi, M., Tu, X., Robertson, S., Lin, R., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02394-3 · Cited by 92

Contribution of proteases to the hallmarks of aging and to age-related neurodegeneration

Rai, M., Curley, M., Coleman, Z., & Demontis, F. (2022) · Aging Cell · doi:10.1111/acel.13603 · Cited by 72

Mitochondrial Dysfunction, Neurogenesis, and Epigenetics: Putative Implications for Amyotrophic Lateral Sclerosis Neurodegeneration and Treatment

Calió, M. L., Henriques, E., Siena, A., Bertoncini, C. R. A., Gil-Mohapel, J., & Rosenstock, T. R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00679 · Cited by 64

The Cullin 4A/B-DDB1-Cereblon E3 Ubiquitin Ligase Complex Mediates the Degradation of CLC-1 Chloride Channels

Chen, Y.-A., Peng, Y.-J., Hu, M.-C., Huang, J.-J., Chien, Y.-C., Wu, J.-T., Chen, T.-Y., & Tang, C.-Y. (2015) · Scientific Reports · doi:10.1038/srep10667 · Cited by 61

mTORC2 (Rictor) in Alzheimer’s Disease and Reversal of Amyloid-β Expression-Induced Insulin Resistance and Toxicity in Rat Primary Cortical Neurons

Lee, H.-K., Kwon, B., Lemere, C. A., de la Monte, S., Itamura, K., Ha, A. Y., & Querfurth, H. W. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161029 · Cited by 57

Heat Shock Factor 2 Protects against Proteotoxicity by Maintaining Cell-Cell Adhesion

Joutsen, J., Da Silva, A. J., Luoto, J. C., Budzynski, M. A., Nylund, A. S., de Thonel, A., Concordet, J.-P., Mezger, V., Sabéran-Djoneidi, D., Henriksson, E., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.037 · Cited by 51

Chaperone-Mediated Autophagy and Its Emerging Role in Hematological Malignancies

Robert, G., Jacquel, A., & Auberger, P. (2019) · Cells · doi:10.3390/cells8101260 · Cited by 45

DEGRONOPEDIA: a web server for proteome-wide inspection of degrons

Szulc, N. A., Stefaniak, F., Piechota, M., Soszyńska, A., Piórkowska, G., Cappannini, A., Bujnicki, J. M., Maniaci, C., & Pokrzywa, W. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae238 · Cited by 35

What lysosomes actually tell us about Parkinson’s disease?

Bourdenx, M., & Dehay, B. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.02.008 · Cited by 26

The absence of specific yeast heat-shock proteins leads to abnormal aggregation and compromised autophagic clearance of mutant Huntingtin proteins

Higgins, R., Kabbaj, M.-H., Hatcher, A., & Wang, Y. (2018) · PLOS ONE · doi:10.1371/journal.pone.0191490 · Cited by 22

Immunity, stem cells, and aging

Devaraj, E., Anbalagan, M., Ileng Kumaran, R., & Bhaskaran, N. (2021) · Stem Cells and Aging · doi:10.1016/b978-0-12-820071-1.00006-2 · Cited by 8