Compromised autophagy and neurodegenerative diseases

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.

Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605 · see citing works

Autophagy fights disease through cellular self-digestion

Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452 · see citing works

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · see citing works

α-Synuclein Locus Triplication Causes Parkinson's Disease

Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383 · see citing works

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · see citing works

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 · see citing works

Loss of autophagy in the central nervous system causes neurodegeneration in mice

Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · see citing works

TFEB Links Autophagy to Lysosomal Biogenesis

Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365 · see citing works

Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease

Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326 · see citing works

p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death

Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276 · see citing works

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works

A Gene Network Regulating Lysosomal Biogenesis and Function

Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543 · see citing works

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 · see citing works

Dissection of the Autophagosome Maturation Process by a Novel Reporter Protein, Tandem Fluorescent-Tagged LC3

Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278 · see citing works

Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy

Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · see citing works

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969 · see citing works

Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin

Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788 · see citing works

Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae

Tsukada, M., & Ohsumi, Y. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80398-e · Cited by 1,756 · see citing works

Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin

Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705 · see citing works

Inhibition of Macroautophagy Triggers Apoptosis

Boya, P., González‐Polo, R. A., Casares, N., Perfettini, J., Dessen, P., Larochette, N., Métivier, D., Meley, D., Souquère, S., Yoshimori, T., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1025-1040.2005 · Cited by 1,629 · see citing works

The roles of intracellular protein-degradation pathways in neurodegeneration

Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625 · see citing works

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works

ULK1 induces autophagy by phosphorylating Beclin-1 and activating VPS34 lipid kinase

Russell, R. C., Tian, Y., Yuan, H., Park, H. W., Chang, Y.-Y., Kim, J., Kim, H., Neufeld, T. P., Dillin, A. G., & Guan, K. (2013) · Nature Cell Biology · doi:10.1038/ncb2757 · Cited by 1,586 · see citing works

Termination of autophagy and reformation of lysosomes regulated by mTOR

Yu, L., McPhee, C. K., Zheng, L., Mardones, G. A., Rong, Y., Peng, J., Mi, N., Zhao, Y., Liu, Z., Wan, F., et al. (2010) · Nature · doi:10.1038/nature09076 · Cited by 1,544 · see citing works

Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks

Alers, S., Löffler, A. S., Wesselborg, S., & Stork, B. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06159-11 · Cited by 1,483 · see citing works

Lysosomal membrane permeabilization in cell death

Boya, P., & Kroemer, G. (2008) · Oncogene · doi:10.1038/onc.2008.310 · Cited by 1,425 · see citing works

Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation

Hailey, D. W., Rambold, A. S., Satpute‐Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott‐Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,419 · see citing works

α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models

Cooper, A. A., Gitler, A. D., Cashikar, A. G., Haynes, C. M., Hill, K. J., Bhullar, B., Liu, K., Xu, K., Strathearn, K. E., Liu, F., et al. (2006) · Science · doi:10.1126/science.1129462 · Cited by 1,377 · see citing works

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works

Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies

Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341 · see citing works

Nix is a selective autophagy receptor for mitochondrial clearance

Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · see citing works

Mutations of optineurin in amyotrophic lateral sclerosis

Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265 · see citing works

Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations

Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212 · see citing works

Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase

Ramirez, A., Heimbach, A., Gründemann, J., Stiller, B., Hampshire, D., Cid, L. P., Goebel, I., Mubaidin, A. F., Wriekat, A.-L., Roeper, J., et al. (2006) · Nature Genetics · doi:10.1038/ng1884 · Cited by 1,208 · see citing works

Cargo recognition and trafficking in selective autophagy

Stolz, A., Ernst, A., & Dikic, I. (2014) · Nature Cell Biology · doi:10.1038/ncb2979 · Cited by 1,207 · see citing works

A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates

Kirkin, V., Lamark, T., Sou, Y., Bjørkøy, G., Nunn, J. A. L., Bruun, J., Shvets, E., McEwan, D. G., Clausen, T. H., Wild, P. S., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.020 · Cited by 1,156 · see citing works

Trehalose, a Novel mTOR-independent Autophagy Enhancer, Accelerates the Clearance of Mutant Huntingtin and α-Synuclein

Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142 · see citing works

Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells

Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2837 · Cited by 1,083 · see citing works

A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation

Hayashi, M., Fujita, N., Noda, T., Yamaguchi, A., Yoshimori, T., & Yamamoto, A. (2009) · Nature Cell Biology · doi:10.1038/ncb1991 · Cited by 1,050 · see citing works

Inhibition of mTOR by Rapamycin Abolishes Cognitive Deficits and Reduces Amyloid-β Levels in a Mouse Model of Alzheimer's Disease

Spilman, P., Podlutskaya, N., Hart, M. J., Debnath, J., Gorostiza, O., Bredesen, D., Richardson, A., Strong, R., & Galvan, V. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009979 · Cited by 1,033 · see citing works

Interactions between Autophagy Receptors and Ubiquitin-like Proteins Form the Molecular Basis for Selective Autophagy

Rogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992 · see citing works

Lithium induces autophagy by inhibiting inositol monophosphatase

Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985 · see citing works

Plasma membrane contributes to the formation of pre-autophagosomal structures

Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., & Rubinsztein, D. C. (2010) · Nature Cell Biology · doi:10.1038/ncb2078 · Cited by 902 · see citing works

WIPI2 Links LC3 Conjugation with PI3P, Autophagosome Formation, and Pathogen Clearance by Recruiting Atg12–5-16L1

Dooley, H. C., Razi, M., Polson, H. E. J., Girardin, S. E., Wilson, M. I., & Tooze, S. A. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.021 · Cited by 886 · see citing works

A Mutation in VPS35, Encoding a Subunit of the Retromer Complex, Causes Late-Onset Parkinson Disease

Zimprich, A. A., Benet‐Pagès, A., Struhal, W., Graf, E., Eck, S. H., Offman, M. N., Haubenberger, D., Spielberger, S., Schulte, E. C., Lichtner, P., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.008 · Cited by 885 · see citing works

Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease

Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885 · see citing works

The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria

Thurston, T. L. M., Ryzhakov, G., Bloor, S., von Muhlinen, N., & Randow, F. (2009) · Nature Immunology · doi:10.1038/ni.1800 · Cited by 872 · see citing works

The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy

Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855 · see citing works

Exosomal cell-to-cell transmission of alpha synuclein oligomers

Danzer, K. M., Kranich, L. R., Ruf, W. P., Cagsal‐Getkin, O., Winslow, A. R., Zhu, L., Vanderburg, C. R., & McLean, P. J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-42 · Cited by 852 · see citing works

Chaperone-mediated autophagy: roles in disease and aging

Cuervo, A. M., & Wong, E. S. P. (2013) · Cell Research · doi:10.1038/cr.2013.153 · Cited by 850 · see citing works

Beclin1 Controls the Levels of p53 by Regulating the Deubiquitination Activity of USP10 and USP13

Liu, J., Xia, H., Kim, M., Xu, L., Li, Y., Zhang, L., Cai, Y. C., Norberg, H. V., Zhang, T., Furuya, T., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.037 · Cited by 828 · see citing works

α-Synuclein impairs macroautophagy: implications for Parkinson’s disease

Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works

Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia

Skibinski, G., Parkinson, N. J., Brown, J. M., Chakrabarti, L., Lloyd, S. L., Hummerich, H., Nielsen, J. E., Hodges, J. R., Spillantini, M. G., Thusgaard, T., et al. (2005) · Nature Genetics · doi:10.1038/ng1609 · Cited by 822 · see citing works

Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation

Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812 · see citing works

Novel targets for Huntington's disease in an mTOR-independent autophagy pathway

Williams, A., Sarkar, S., Cuddon, P., Ttofi, E. K., Saiki, S., Siddiqi, F. H., Jahreiss, L., Fleming, A., Pask, D., Goldsmith, P., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.79 · Cited by 800 · see citing works

p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

Narendra, D. P., Kane, L. A., Hauser, D. N., Fearnley, I. M., & Youle, R. J. (2010) · Autophagy · doi:10.4161/auto.6.8.13426 · Cited by 789 · see citing works

TFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity

Decressac, M., Mattsson, B., Weikop, P., Lundblad, M., Jakobsson, J., & Björklund, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305623110 · Cited by 753 · see citing works

The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis

Yang, Y., Hentati, A., Deng, H.-X., Dabbagh, O., Sasaki, T., Hirano, M., Hung, W.-Y., Ouahchi, K., Yan, J., Azim, A. C., et al. (2001) · Nature Genetics · doi:10.1038/ng1001-160 · Cited by 743 · see citing works

<i>C9orf72</i> repeat expansions cause neurodegeneration in <i>Drosophila</i> through arginine-rich proteins

Mizielinska, S., Grönke, S., Niccoli, T., Ridler, C. E., Clayton, E. L., Devoy, A., Moens, T., Norona, F. E., Woollacott, I. O. C., Pietrzyk, J., et al. (2014) · Science · doi:10.1126/science.1256800 · Cited by 740 · see citing works

Defective Mitophagy in XPA via PARP-1 Hyperactivation and NAD+/SIRT1 Reduction

Fang, E. F., Scheibye-Knudsen, M., Brace, L. E., Kassahun, H., SenGupta, T., Nilsen, H., Mitchell, J. R., Croteau, D. L., & Bohr, V. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.026 · Cited by 711 · see citing works

Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment

Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711 · see citing works

Transcriptional Activation of Lysosomal Exocytosis Promotes Cellular Clearance

Medina, D. L., Fraldi, A., Bouchè, V., Annunziata, F., Mansueto, G., Spampanato, C., Puri, C., Pignata, A., Martina, J. A., Sardiello, M., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.07.016 · Cited by 708 · see citing works

3D tomography reveals connections between the phagophore and endoplasmic reticulum

Ylä‐Anttila, P., Vihinen, H., Jokitalo, E., & Eskelinen, E. (2009) · Autophagy · doi:10.4161/auto.5.8.10274 · Cited by 670 · see citing works

Autophagy Inhibition Compromises Degradation of Ubiquitin-Proteasome Pathway Substrates

Korolchuk, V. I., Mansilla, A., Menzies, F. M., & Rubinsztein, D. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.021 · Cited by 657 · see citing works

&lt;emph type="ital"&gt;SQSTM1&lt;/emph&gt; Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

Fecto, F. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.250 · Cited by 650 · see citing works

p62 Is a Common Component of Cytoplasmic Inclusions in Protein Aggregation Diseases

Zatloukal, K., Stumptner, C., Fuchsbichler, A., Heid, H., Schnoelzer, M., Kenner, L., Kleinert, R., Prinz, M., Aguzzi, A., & Denk, H. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64369-6 · Cited by 624 · see citing works

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works

Interplay of LRRK2 with chaperone-mediated autophagy

Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588 · see citing works

Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy

Orsi, A., Razi, M., Dooley, H. C., Robinson, D. J., Weston, A., Collinson, L., & Tooze, S. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0746 · Cited by 570 · see citing works

TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways

Fader, C. M., Sánchez, D. G., Mestre, M. B., & Colombo, M. I. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.09.011 · Cited by 544 · see citing works

Web-based genome-wide association study identifies two novel loci and a substantial genetic component for Parkinson’s disease

Do, C. B., Tung, J. Y., Dorfman, E., Kiefer, A. K., Drabant, E. M., Francke, U., Mountain, J. L., Goldman, S. M., Tanner, C. M., Langston, J. W., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002141 · Cited by 515 · see citing works

Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin

Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502 · see citing works

ESCRT-III Dysfunction Causes Autophagosome Accumulation and Neurodegeneration

Lee, J., Beigneux, A. P., Ahmad, S. T., Young, S. G., & Gao, F. (2007) · Current Biology · doi:10.1016/j.cub.2007.07.029 · Cited by 490 · see citing works

C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking

Farg, M. A., Sundaramoorthy, V., Sultana, J. M., Yang, S., Atkinson, R. A. K., Levina, V., Halloran, M. A., Gleeson, P. A., Blair, I. P., Soo, K. Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu068 · Cited by 478 · see citing works

Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson’s disease

Murphy, K. E., Gysbers, A. M., Abbott, S. K., Tayebi, N., Kim, W. S., Sidransky, E., Cooper, A., Garner, B., & Halliday, G. M. (2014) · Brain · doi:10.1093/brain/awt367 · Cited by 475 · see citing works

De novo mutations in the autophagy gene WDR45 cause static encephalopathy of childhood with neurodegeneration in adulthood

Saitsu, H., Nishimura, T., Muramatsu, K., Kodera, H., Kumada, S., Sugai, K., Kasai-Yoshida, E., Sawaura, N., Nishida, H., Hoshino, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2562 · Cited by 474 · see citing works

Mutation in VPS35 associated with Parkinson’s disease impairs WASH complex association and inhibits autophagy

Zavodszky, E., Seaman, M. N. J., Moreau, K., Jimenez-Sanchez, M., Breusegem, S. Y., Harbour, M. E., & Rubinsztein, D. C. (2014) · Nature Communications · doi:10.1038/ncomms4828 · Cited by 466 · see citing works

The return of the nucleus: transcriptional and epigenetic control of autophagy

Füllgrabe, J., Klionsky, D. J., & Joseph, B. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3716 · Cited by 463 · see citing works

Aβ Secretion and Plaque Formation Depend on Autophagy

Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., & Saido, T. C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.042 · Cited by 459 · see citing works

Dynein mutations impair autophagic clearance of aggregate-prone proteins

Ravikumar, B., Acevedo‐Arozena, A., Imarisio, S., Berger, Z., Vacher, C., O’Kane, C. J., Brown, S. D. M., & Rubinsztein, D. C. (2005) · Nature Genetics · doi:10.1038/ng1591 · Cited by 458 · see citing works

The retromer complex – endosomal protein recycling and beyond

Seaman, M. N. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.103440 · Cited by 455 · see citing works

Mutations in the Small GTP-ase Late Endosomal Protein RAB7 Cause Charcot-Marie-Tooth Type 2B Neuropathy

Verhoeven, K., Jonghe, P. D., Coen, K., Verpoorten, N., Auer‐Grumbach, M., Kwon, J. M., FitzPatrick, D. R., Schmedding, E., Vriendt, E. D., Jacobs, A., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/367847 · Cited by 454 · 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

The Selective Macroautophagic Degradation of Aggregated Proteins Requires the PI3P-Binding Protein Alfy

Filimonenko, M., Isakson, P., Finley, K. D., Anderson, M. R., Jeong, H., Melia, T. J., Bartlett, B. J., Myers, K. M., Birkeland, H. C. G., Lamark, T., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.007 · Cited by 432 · see citing works

A mutation in sigma‐1 receptor causes juvenile amyotrophic lateral sclerosis

Al-Saif, A. M., Al-Mohanna, F. A., & Bohlega, S. (2011) · Annals of Neurology · doi:10.1002/ana.22534 · Cited by 430 · see citing works

Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer’s disease ameliorates amyloid pathologies and memory deficits

Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429 · see citing works

Huntingtin functions as a scaffold for selective macroautophagy

Rui, Y.-N., Xu, Z., Patel, B., Chen, Z., Chen, D., Tito, A., David, G., Sun, Y., Stimming, E. F., Bellen, H. J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3101 · Cited by 423 · see citing works

Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes

Puri, C., Renna, M., Bento, C. F., Moreau, K., & Rubinsztein, D. C. (2013) · Cell · doi:10.1016/j.cell.2013.08.044 · Cited by 423 · see citing works

Meta-analysis Confirms CR1, CLU, and PICALM as Alzheimer Disease Risk Loci and Reveals Interactions With APOE Genotypes

Jun, G. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.201 · Cited by 422 · see citing works

Huntington's disease: from pathology and genetics to potential therapies

Imarisio, S., Carmichael, J., Korolchuk, V., Chen, C.-W., Saiki, S., Rose, C., Krishna, G., Davies, J. E., Ttofi, E., Underwood, B. R., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071619 · Cited by 409 · see citing works

Rapamycin pre-treatment protects against apoptosis

Ravikumar, B., Berger, Z., Vacher, C., O’Kane, C. J., & Rubinsztein, D. C. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl036 · Cited by 400 · see citing works

Autophagy in lysosomal storage disorders

Lieberman, A. P., Puertollano, R., Raben, N., Slaugenhaupt, S., Walkley, S. U., & Ballabio, A. (2012) · Autophagy · doi:10.4161/auto.19469 · Cited by 399 · see citing works

The Regulation of Autophagosome Dynamics by Huntingtin and HAP1 Is Disrupted by Expression of Mutant Huntingtin, Leading to Defective Cargo Degradation

Wong, Y. C., & Holzbaur, E. L. F. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1870-13.2014 · Cited by 395 · see citing works

Parkin and PINK1: much more than mitophagy

Scarffe, L. A., Stevens, D. A., Dawson, V. L., & Dawson, T. M. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.03.004 · Cited by 392 · see citing works

Autophagosome Precursor Maturation Requires Homotypic Fusion

Moreau, K., Ravikumar, B., Renna, M., Puri, C., & Rubinsztein, D. C. (2011) · Cell · doi:10.1016/j.cell.2011.06.023 · Cited by 382 · see citing works

Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration

Dehay, B., Ramı́rez, A., Martínez‐Vicente, M., Perier, C., Canron, M., Doudnikoff, É., Vital, A., Vila, M., Klein, C., & Bézard, E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112368109 · Cited by 381 · see citing works

Microglial Beclin 1 Regulates Retromer Trafficking and Phagocytosis and Is Impaired in Alzheimer’s Disease

Lucin, K. M., O’Brien, C. E., Bieri, G., Czirr, E., Mosher, K. I., Abbey, R. J., Mastroeni, D. F., Rogers, J., Spencer, B., Masliah, E., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.046 · Cited by 374 · see citing works

Selective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB

Polito, V. A., Li, H., Martini‐Stoica, H., Wang, B., Li, Y., Xu, Y., Swartzlander, D. B., Palmieri, M., di Ronza, A., Lee, V. M. ‐., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201303671 · Cited by 351 · see citing works

Autophagic Clearance of PolyQ Proteins Mediated by Ubiquitin-Atg8 Adaptors of the Conserved CUET Protein Family

Lu, K., Psakhye, I., & Jentsch, S. (2014) · Cell · doi:10.1016/j.cell.2014.05.048 · Cited by 343 · see citing works

Early Steps in Autophagy Depend on Direct Phosphorylation of Atg9 by the Atg1 Kinase

Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C. A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijańska, M., Stoffel-Studer, I., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.011 · Cited by 343 · see citing works

Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy

Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343 · see citing works

Rhes, a Striatal Specific Protein, Mediates Mutant-Huntingtin Cytotoxicity

Subramaniam, S., Sixt, K. M., Barrow, R. K., & Snyder, S. H. (2009) · Science · doi:10.1126/science.1172871 · Cited by 340 · see citing works

Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons

Castillo, K., Nassif, M., Valenzuela, V., Rojas, F., Matus, S., Mercado, G., Court, F. A., van Zundert, B., & Hetz, C. A. (2013) · Autophagy · doi:10.4161/auto.25188 · Cited by 338 · see citing works

At the end of the autophagic road: an emerging understanding of lysosomal functions in autophagy

Shen, H., & Mizushima, N. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.001 · Cited by 334 · see citing works

Autophagy and neurodegeneration

Frake, R. A., Ricketts, T., Menzies, F. M., & Rubinsztein, D. C. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73944 · Cited by 332 · see citing works

Mitochondria and Quality Control Defects in a Mouse Model of Gaucher Disease—Links to Parkinson’s Disease

Osellame, L. D., Rahim, A. A., Hargreaves, I. P., Gegg, M. E., Richard-Loendt, A., Brandner, S., Waddington, S. N., Schapira, A. H. V., & Duchen, M. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.014 · Cited by 329 · see citing works

Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52

Jo, C., Gundemir, S., Pritchard, S., Jin, Y. N., Rahman, I., & Johnson, G. V. W. (2014) · Nature Communications · doi:10.1038/ncomms4496 · Cited by 323 · see citing works

p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy

Clausen, T. H., Lamark, T., Isakson, P., Finley, K. D., Larsen, K. B., Brech, A., Øvervatn, A., Stenmark, H., Bjørkøy, G., Simonsen, A., et al. (2010) · Autophagy · doi:10.4161/auto.6.3.11226 · Cited by 321 · see citing works

The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs

Levine, T. P., Daniels, R. D., Gatta, A. T., Wong, L. H., & Hayes, M. J. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts725 · 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

Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation

Rodríguez-Navarro, J. A., Rodríguez, L., Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., Cuervo, A. M., García de Yébenes, J., & Mena, M. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.014 · Cited by 298 · see citing works

Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease

Ravikumar, B., Imarisio, S., Sarkar, S., O’Kane, C. J., & Rubinsztein, D. C. (2008) · Journal of Cell Science · doi:10.1242/jcs.025726 · Cited by 298 · see citing works

Impaired Autophagy in the Lipid-Storage Disorder Niemann-Pick Type C1 Disease

Sarkar, S., Carroll, B., Buganim, Y., Maetzel, D., Ng, A. H. M., Cassady, J. P., Cohen, M. A., Chakraborty, S., Wang, H., Spooner, E., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.042 · Cited by 290 · see citing works

Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes

Simonsen, A., Birkeland, H. C. G., Gillooly, D. J., Mizushima, N., Kuma, A., Yoshimori, T., Slagsvold, T., Brech, A., & Stenmark, H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01287 · Cited by 282 · see citing works

PICALM modulates autophagy activity and tau accumulation

Moreau, K., Fleming, A., Imarisio, S., Lopez Ramirez, A., Mercer, J. L., Jimenez-Sanchez, M., Bento, C. F., Puri, C., Zavodszky, E., Siddiqi, F., et al. (2014) · Nature Communications · doi:10.1038/ncomms5998 · Cited by 281 · see citing works

Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3

Menzies, F. M., Hübener‐Schmid, J., Renna, M., von Bonin, M., Rieß, O., & Rubinsztein, D. C. (2009) · Brain · doi:10.1093/brain/awp292 · Cited by 260 · see citing works

PI(5)P Regulates Autophagosome Biogenesis

Vicinanza, M., Korolchuk, V. I., Ashkenazi, A., Puri, C., Menzies, F. M., Clarke, J. H., & Rubinsztein, D. C. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.007 · Cited by 256 · see citing works

MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis

Zhang, X., Chen, S., Song, L., Tang, Y., Shen, Y., Li, J. X., & Le, W. (2014) · Autophagy · doi:10.4161/auto.27710 · Cited by 256 · see citing works

Inflammation-Induced Alteration of Astrocyte Mitochondrial Dynamics Requires Autophagy for Mitochondrial Network Maintenance

Motori, E., Puyal, J., Toni, N., Ghanem, A., Angeloni, C., Malaguti, M., Cantelli-Forti, G., Berninger, B., Conzelmann, K.-K., Götz, M., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.005 · Cited by 249 · see citing works

Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy

Schwarten, M., Mohrluder, J., Ma, P., Stoldt, M., Thielmann, Y., Stangler, T., Hersch, N., Hoffmann, B., Merkel, R., & Willbold, D. (2009) · Autophagy · doi:10.4161/auto.5.5.8494 · Cited by 247 · see citing works

Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology

Teyssou, E., Takeda, T., Lebon, V., Boillée, S., Doukouré, B., Bataillon, G., Sazdovitch, V., Cazeneuve, C., Meininger, V., LeGuern, E., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1090-0 · Cited by 241 · see citing works

Tubulin Polymerization-promoting Protein (TPPP/p25α) Promotes Unconventional Secretion of α-Synuclein through Exophagy by Impairing Autophagosome-Lysosome Fusion

Ejlerskov, P., Rasmussen, I., Nielsen, T. T., Bergström, A., Tohyama, Y., Jensen, P. H., & Vilhardt, F. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401174 · Cited by 236 · see citing works

Inhibition of Glycogen Synthase Kinase-3 Ameliorates β-Amyloid Pathology and Restores Lysosomal Acidification and Mammalian Target of Rapamycin Activity in the Alzheimer Disease Mouse Model

Avrahami, L., Farfara, D., Shaham-Kol, M., Vassar, R. J., Frenkel, D., & Eldar-Finkelman, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409250 · Cited by 232 · see citing works

AMPK-dependent phosphorylation of ULK1 regulates ATG9 localization

Mack, H. I. D., Zheng, B., Asara, J. M., & Thomas, S. Μ. (2012) · Autophagy · doi:10.4161/auto.20586 · Cited by 221 · see citing works

Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation

Deretic, V. P., Jiang, S., & Dupont, N. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.04.008 · Cited by 218 · see citing works

Autophagy promotes survival of retinal ganglion cells after optic nerve axotomy in mice

Rodríguez-Muela, N., Germain, F., Mariño, G., Fitze, P. S., & Boya, P. (2012) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2011.88 · Cited by 216 · see citing works

Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation

Chang, J., Lee, S., & Blackstone, C. D. (2014) · Journal of Clinical Investigation · doi:10.1172/jci77598 · Cited by 216 · see citing works

Cell-Autonomous Death of Cerebellar Purkinje Neurons with Autophagy in Niemann-Pick Type C Disease

Ko, D. C., Milenković, L., Beier, S., Manuel, H., Buchanan, J., & Scott, M. P. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010007 · Cited by 214 · see citing works

Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells

Coen, K., Flannagan, R. S., Baron, S., Carraro-Lacroix, L. R., Wang, D., Vermeire, W., Michiels, C., Munck, S., Baert, V., Sugita, S., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201201076 · Cited by 208 · see citing works

The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy

Yen, W.-L., Shintani, T., Nair, U., Cao, Y., Richardson, B. C., Li, Z., Hughson, F. M., Baba, M., & Klionsky, D. J. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200904075 · Cited by 206 · see citing works

Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington's disease

Rose, C., Menzies, F. M., Renna, M., Acevedo‐Arozena, A., Corrochano, S., Sadiq, O., Brown, S. D. M., & Rubinsztein, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq093 · Cited by 200 · see citing works

Autophagic failure promotes the exocytosis and intercellular transfer of α-synuclein

Lee, H.-J., Cho, E.-D., Lee, K., Kim, J., Cho, S., & Lee, S. (2013) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.45 · Cited by 199 · see citing works

Sigma nonopioid intracellular receptor 1 mutations cause frontotemporal lobar degeneration–motor neuron disease

Luty, A. A., Kwok, J. B., Dobson‐Stone, C., Loy, C. T., Coupland, K., Karlström, H., Sobów, T., Tchorzewska, J., Maruszak, A., Barcikowska, M., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22274 · Cited by 196 · see citing works

Genetic and Chemical Correction of Cholesterol Accumulation and Impaired Autophagy in Hepatic and Neural Cells Derived from Niemann-Pick Type C Patient-Specific iPS Cells

Maetzel, D., Sarkar, S., Wang, H., Abi-Mosleh, L., Xu, P., Cheng, A. W., Gao, Q., Mitalipova, M., & Jaenisch, R. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.03.014 · Cited by 195 · see citing works

Mitophagy Selectively Degrades Individual Damaged Mitochondria After Photoirradiation

Kim, I., & Lemasters, J. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3768 · Cited by 193 · see citing works

Exit from the Golgi Is Required for the Expansion of the Autophagosomal Phagophore in YeastSaccharomyces cerevisiae

van der Vaart, A., Griffith, J. M., & Reggiori, F. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-04-0345 · Cited by 185 · see citing works

Alsin Is a Rab5 and Rac1 Guanine Nucleotide Exchange Factor

Topp, J. D., Gray, N. W., Gerard, R. D., & Horazdovsky, B. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313504200 · Cited by 184 · see citing works

Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration

Tsvetkov, A. S., Arrasate, M., Barmada, S., Ando, D. M., Sharma, P., Shaby, B. A., & Finkbeiner, S. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1308 · Cited by 178 · see citing works

High sphingomyelin levels induce lysosomal damage and autophagy dysfunction in Niemann Pick disease type A

Gabandé‐Rodríguez, E., Boya, P., Labrador-Cantarero, V., Dotti, C. G., & Ledesma, M. D. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.4 · Cited by 176 · see citing works

The sigma-1 receptor is enriched in postsynaptic sites of C-terminals in mouse motoneurons. An anatomical and behavioral study

Mavlyutov, T. A., Epstein, M. L., Andersen, K. A., Ziskind‐Conhaim, L., & Ruoho, A. E. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.022 · Cited by 171 · see citing works

Temsirolimus promotes autophagic clearance of amyloid-β and provides protective effects in cellular and animal models of Alzheimer's disease

Jiang, T., Yu, J., Zhu, X., Tan, M., Wang, H.-F., Cao, L., Zhang, Q.-Q., Shi, J., Gao, L., Qin, H., et al. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.02.008 · Cited by 171 · see citing works

Sigma-1R Agonist Improves Motor Function and Motoneuron Survival in ALS Mice

Mancuso, R., Oliván, S., Rando, A., Casas, C., Osta, R., & Navarro, X. (2012) · Neurotherapeutics · doi:10.1007/s13311-012-0140-y · Cited by 165 · see citing works

Polyglutamine-expanded androgen receptor interferes with TFEB to elicit autophagy defects in SBMA

Cortés, C. J., Miranda, H. C., Frankowski, H., Batlevi, Y., Young, J. E., Le, A. T., Ivanov, N., Sopher, B. L., Carromeu, C., Muotri, A. R., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3787 · Cited by 164 · see citing works

Rapamycin Activates Autophagy and Improves Myelination in Explant Cultures from Neuropathic Mice

Rangaraju, S., Verrier, J. D., Madorsky, I., Nicks, J., Dunn, W. A., & Notterpek, L. M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1356-10.2010 · Cited by 152 · see citing works

The autophagic roles of Rab small GTPases and their upstream regulators

Szatmári, Z., & Sass, M. (2014) · Autophagy · doi:10.4161/auto.29395 · Cited by 152 · see citing works

Connections between SNAREs and autophagy

Moreau, K., Renna, M., & Rubinsztein, D. C. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.11.004 · Cited by 151 · see citing works

Altered localization, abnormal modification and loss of function of Sigma receptor-1 in amyotrophic lateral sclerosis

Prause, J. U., Goswami, A., Katona, I., Roos, A., Schnizler, M. K., Bushuven, E., Dreier, A., Buchkremer, S., Johann, S., Beyer, C., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt008 · Cited by 151 · see citing works

Autophagy Enhancer Carbamazepine Alleviates Memory Deficits and Cerebral Amyloid-β Pathology in a Mouse Model of Alzheimer's Disease

Li, L., Zhang, S., Zhang, X., Li, T., Tang, Y., Liu, H., Yang, W., & Le, W. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310040008 · Cited by 149 · see citing works

Impaired proteolysis underlies autophagic dysfunction in Niemann–Pick type C disease

Elrick, M. J., Yu, T., Chung, C., & Lieberman, A. P. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds324 · Cited by 148 · see citing works

Acid sphingomyelinase modulates the autophagic process by controlling lysosomal biogenesis in Alzheimer’s disease

Lee, J. K., Jin, H. K., Park, M. H., Kim, B.-R., Lee, P. H., Nakauchi, H., Carter, J., He, X., Schuchman, E. H., & Bae, J. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20132451 · Cited by 147 · see citing works

p53 inhibits autophagy by interacting with the human ortholog of yeast Atg17, RB1CC1/FIP200

Morselli, E., Shen, S., Ruckenstuhl, C., Bauer, M. A., Mariño, G., Galluzzi, L., Criollo, A., Michaud, M., Maiuri, M., Chano, T., et al. (2011) · Cell Cycle · doi:10.4161/cc.10.16.16868 · Cited by 145 · see citing works

Presenilin Is Necessary for Efficient Proteolysis through the Autophagy–Lysosome System in a γ-Secretase-Independent Manner

Neely, K. M., Green, K. N., & LaFerla, F. M. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5156-10.2010 · Cited by 141 · see citing works

Clathrin adaptor CALM/PICALM is associated with neurofibrillary tangles and is cleaved in Alzheimer’s brains

Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136 · see citing works

Genome-wide RNAi screen identifies the Parkinson disease GWAS risk locus <i>SREBF1</i> as a regulator of mitophagy

Ivatt, R. M., Sanchez-Martinez, A., Godena, V. K., Brown, S., Ziviani, E., & Whitworth, A. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321207111 · Cited by 130 · see citing works

Measurement of autophagy flux in the nervous system in vivo

Castillo, K., Valenzuela, V, Matus, S., Nassif, M., Oñate, M., Fuentealba, Y., Encina, G., Irrazabal, T., Parsons, G., Court, F. A., et al. (2013) · Cell Death &amp; Disease · doi:10.1038/cddis.2013.421 · Cited by 127 · see citing works

Rhes, a Striatal-selective Protein Implicated in Huntington Disease, Binds Beclin-1 and Activates Autophagy

Mealer, R. G., Murray, A. J., Shahani, N., Subramaniam, S., & Snyder, S. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.536912 · Cited by 124 · see citing works

Astrocyte dysfunction triggers neurodegeneration in a lysosomal storage disorder

Malta, C. D., Fryer, J. D., Settembre, C., & Ballabio, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209577109 · Cited by 123 · see citing works

A Role for Presenilins in Autophagy Revisited: Normal Acidification of Lysosomes in Cells Lacking PSEN1 and PSEN2

Zhang, X., Garbett, K., Veeraraghavalu, K., Wilburn, B., Gilmore, R., Mirnics, K., & Sisodia, S. S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0556-12.2012 · Cited by 122 · see citing works

Calpain inhibition mediates autophagy-dependent protection against polyglutamine toxicity

Menzies, F. M., Garcı́a-Arencibia, M., Imarisio, S., O’Sullivan, N. C., Ricketts, T., Kent, B. A., Rao, M. V., Lam, W., Green-Thompson, Z. W., Nixon, R. A., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.151 · Cited by 117 · see citing works

Disruption and therapeutic rescue of autophagy in a human neuronal model of Niemann Pick type C1

Ordonez, M. P., Roberts, E. A., Kidwell, C. U., Yuan, S. H., Plaisted, W. C., & Goldstein, L. S. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds090 · Cited by 117 · see citing works

The pathogenesis of Niemann–Pick type C disease: a role for autophagy?

Pacheco, C. D., & Lieberman, A. P. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s146239940800080x · Cited by 109 · see citing works

Age at onset in Huntington’s disease is modified by the autophagy pathway: implication of the V471A polymorphism in Atg7

Metzger, S., Saukko, M., Che, H. V., Tong, L., Puder, Y., Rieß, O., & Nguyen, H. P. (2010) · Human Genetics · doi:10.1007/s00439-010-0873-9 · Cited by 107 · see citing works

Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons

Wilson, C., Murphy, D. D., Giasson, B. I., Zhang, B., Trojanowski, J. Q., & Lee, V. M. ‐. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403061 · Cited by 106 · see citing works

Loss of function of the ALS protein SigR1 leads to ER pathology associated with defective autophagy and lipid raft disturbances

Vollrath, J. T., Sechi, A. S., Dreser, A., Katona, I., Wiemuth, D., Vervoorts, J., Dohmen, M., Chandrasekar, A., Prause, J. U., Brauers, E., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.243 · Cited by 100 · see citing works

p62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate

Watanabe, Y., & Tanaka, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.081232 · Cited by 99 · see citing works

Mitophagy and Parkinson's disease: Be eaten to stay healthy

de Vries, R. L. A., & Przedborski, S. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.07.008 · Cited by 94 · see citing works

Long-term oral lithium treatment attenuates motor disturbance in tauopathy model mice: Implications of autophagy promotion

Shimada, K., Motoi, Y., Ishiguro, K., Kambe, T., Matsumoto, S., Itaya, M., Kunichika, M., Mori, H., Shinohara, A., Chiba, M., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.050 · Cited by 87 · see citing works

Defective autophagy in spastizin mutated patients with hereditary spastic paraparesis type 15

Vantaggiato, C., Crimella, C., Airoldi, G., Polishchuk, R., Bonato, S., Brighina, E., Scarlato, M., Musumeci, O., Toscano, A., Martinuzzi, A., et al. (2013) · Brain · doi:10.1093/brain/awt227 · Cited by 86 · see citing works

Identification of a novel candidate gene for non-syndromic autosomal recessive intellectual disability: the WASH complex member SWIP

Ropers, F. G., Derivery, E., Hu, H., Garshasbi, M., Karbasiyan, M., Herold, M. J., Nürnberg, G., Ullmann, R., Gautreau, A. M., Sperling, K., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr158 · Cited by 82 · see citing works

Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode

Becker, D., Richter, J., Tocilescu, M. A., Przedborski, S., & Voos, W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365700 · Cited by 77 · see citing works

Correction: Uncoupling of Longevity and Telomere Length in C. elegans

Raı́ces, M., Maruyama, H., Dillin, A., et al. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010081 · Cited by 77 · see citing works

Autophagy Promotes Oligodendrocyte Survival and Function following Dysmyelination in a Long-Lived Myelin Mutant

Smith, C. M., Mayer, J. A., & Duncan, I. D. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.0233-13.2013 · Cited by 69 · see citing works

Chaperone mediated autophagy to the rescue: A new-fangled target for the treatment of neurodegenerative diseases

Xilouri, M., & Stefanis, L. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.01.003 · Cited by 67 · see citing works

Depletion of p62 reduces nuclear inclusions and paradoxically ameliorates disease phenotypes in Huntington's model mice

Kurosawa, M., Matsumoto, G., Kino, Y., Okuno, M., Kurosawa-Yamada, M., Washizu, C., Taniguchi, H., Nakaso, K., Yanagawa, T., Warabi, E., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu522 · Cited by 63 · see citing works

BPAN

Haack, T. B., Hogarth, P., Gregory, A., Prokisch, H., & Hayflick, S. J. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00005-3 · Cited by 60 · see citing works

p62 Plays a Protective Role in the Autophagic Degradation of Polyglutamine Protein Oligomers in Polyglutamine Disease Model Flies

Saitoh, Y., Fujikake, N., Okamoto, Y., Popiel, H. A., Hatanaka, Y., Ueyama, M., Suzuki, M., Gaumer, S., Murata, M., Wada, K., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.590281 · Cited by 59 · see citing works

p62/SQSTM1 Differentially Removes the Toxic Mutant Androgen Receptor via Autophagy and Inclusion Formation in a Spinal and Bulbar Muscular Atrophy Mouse Model

Doi, H., Adachi, H., Katsuno, M., Minamiyama, M., Matsumoto, S., Kondo, N., Miyazaki, Y., Iida, M., Tohnai, G., Qiang, Q., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3021-12.2013 · Cited by 58 · see citing works

The V471A Polymorphism in Autophagy-Related Gene ATG7 Modifies Age at Onset Specifically in Italian Huntington Disease Patients

Metzger, S., Walter, C., Rieß, O., Roos, R. A. C., Nielsen, J. E., Craufurd, D., REGISTRY Investigators of the European Huntington’s Disease Network, & Nguyen, H. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068951 · Cited by 55 · see citing works

Overexpression of Human E46K Mutant α-Synuclein Impairs Macroautophagy via Inactivation of JNK1-Bcl-2 Pathway

Yan, J., Yuan, Y., Gao, Y., Huang, J., Ma, K., Gao, Y., Zhang, W., Guo, X., & Chen, N. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8738-1 · Cited by 53 · see citing works

Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation

Otomo, A., Kunita, R., Suzuki-Utsunomiya, K., Ikeda, J., & Hadano, S. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.045 · Cited by 50 · see citing works

The hereditary spastic paraplegia protein strumpellin: Characterisation in neurons and of the effect of disease mutations on WASH complex assembly and function

Freeman, C., Seaman, M. N. J., & Reid, E. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.10.011 · Cited by 48 · see citing works

Chaperone-mediated autophagy: roles in neurodegeneration

Wang, G., & Mao, Z. (2014) · Translational Neurodegeneration · doi:10.1186/2047-9158-3-20 · Cited by 42 · see citing works

The autophagic defect in Niemann–Pick disease type C neurons differs from somatic cells and reduces neuronal viability

Meske, V., Erz, J., Priesnitz, T., & Ohm, T. G. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.12.018 · Cited by 41 · see citing works

Prion-Like Propagation of Protein Aggregation and Related Therapeutic Strategies

Kaufman, S. K., & Diamond, M. I. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0196-3 · Cited by 38 · see citing works

Optineurin immunoreactivity in neuronal nuclear inclusions of polyglutamine diseases (Huntington’s, DRPLA, SCA2, SCA3) and intranuclear inclusion body disease

Mori, F., Tanji, K., Toyoshima, Y., Yoshida, M., Kakita, A., Takahashi, H., & Wakabayashi, K. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0956-x · Cited by 37 · see citing works

A Tumor-Associated Mutation of FYVE-CENT Prevents Its Interaction with Beclin 1 and Interferes with Cytokinesis

Sagona, A. P., Nezis, I. P., Bache, K. G., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017086 · Cited by 35 · see citing works

The Association Between ß-Glucocerebrosidase Mutations and Parkinsonism

Swan, M. C., & Saunders‐Pullman, R. (2013) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-013-0368-x · Cited by 35 · see citing works

Alzheimer neurodegeneration, autophagy, and Abeta secretion: The ins and outs (comment on DOI 10.1002/bies.201400002)

Nixon, R. A. (2014) · BioEssays · doi:10.1002/bies.201400064 · Cited by 14 · see citing works

Cellular machinery to fuse antimicrobial autophagosome with lysosome

Furuta, N., & Amano, A. (2010) · Communicative & Integrative Biology · doi:10.4161/cib.3.4.12030 · Cited by 8 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death &amp; Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Hallmarks of neurodegenerative diseases

Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works

Mitophagy inhibits amyloid-β and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease

Fang, E. F., Hou, Y., Palikaras, K., Adriaanse, B. A., Kerr, J. S., Yang, B., Lautrup, S., Hasan-Olive, M. M., Caponio, D., Dan, X., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0332-9 · Cited by 1,740 · see citing works

Molecular definitions of autophagy and related processes

Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646 · see citing works

Autophagy in healthy aging and disease

Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313 · see citing works

Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities

Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134 · see citing works

Ageing, neurodegeneration and brain rejuvenation

Wyss-Coray, T. (2016) · Nature · doi:10.1038/nature20411 · Cited by 1,147 · see citing works

Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms

Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870 · see citing works

Autophagy and mitophagy in cardiovascular disease

Bravo-San Pedro, J. M., Kroemer, G., & Galluzzi, L. (2017) · Circulation Research · doi:10.1161/circresaha.117.311082 · Cited by 843 · see citing works

Pharmacological modulation of autophagy: therapeutic potential and persisting obstacles

Galluzzi, L., Bravo-San Pedro, J. M., Levine, B., Green, D. R., & Kroemer, G. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.22 · Cited by 842 · see citing works

NAD+ in Brain Aging and Neurodegenerative Disorders

Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790 · see citing works

NAD + Replenishment Improves Lifespan and Healthspan in Ataxia Telangiectasia Models via Mitophagy and DNA Repair

Fang, E. F., Kassahun, H., Croteau, D. L., Scheibye-Knudsen, M., Marosi, K., Lu, H., Shamanna, R. A., Kalyanasundaram, S., Bollineni, R. C., Wilson, M. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.004 · Cited by 575 · see citing works

Disorders of lysosomal acidification—The emerging role of v-ATPase in aging and neurodegenerative disease

Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548 · see citing works

NAD(+) in aging: molecular mechanisms and translational implications

Fang, E. F., Lautrup, S., Hou, Y., Demarest, T. G., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.001 · Cited by 501 · see citing works

The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective

Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.002 · Cited by 436 · see citing works

Autophagy and the cell biology of age-related disease

Leidal, A. M., Levine, B., & Debnath, J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0235-8 · Cited by 424 · see citing works

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 · see citing works

Nuclear DNA damage signalling to mitochondria in ageing

Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works

Presenilin 1 Maintains Lysosomal Ca2+ Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification

Lee, J.-H., McBrayer, M. K., Wolfe, D. M., Haslett, L. J., Kumar, A., Sato, Y., Lie, P. P. Y., Mohan, P., Coffey, E. E., Kompella, U., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.050 · Cited by 358 · see citing works

Mitophagy in neurodegeneration and aging

Fivenson, E. M., Lautrup, S., Sun, N., Scheibye-Knudsen, M., Stevnsner, T., Nilsen, H., Bohr, V. A., & Fang, E. F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.02.007 · Cited by 364 · see citing works

Activating autophagy to potentiate immunogenic chemotherapy and radiation therapy

Galluzzi, L., Bravo-San Pedro, J. M., Demaria, S., Formenti, S. C., & Kroemer, G. (2017) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2016.183 · Cited by 314 · see citing works

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 · see citing works

Autophagy in acute brain injury

Galluzzi, L., Bravo-San Pedro, J. M., Blomgren, K., & Kroemer, G. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.51 · Cited by 234 · see citing works

Interplay of pathogenic forms of human tau with different autophagic pathways

Caballero, B., Wang, Y., Diaz, A., Tasset, I., Juste, Y. R., Stiller, B., Mandelkow, E., Mandelkow, E., & Cuervo, A. M. (2018) · Aging Cell · doi:10.1111/acel.12692 · Cited by 213 · see citing works

Therapeutic targeting of autophagy in neurodegenerative and infectious diseases

Rubinsztein, D. C., Bento, C. F., & Deretic, V. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150956 · Cited by 202 · see citing works

Autophagy and ALS: mechanistic insights and therapeutic implications

Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works

DNA Damage Response and Autophagy: A Meaningful Partnership

Eliopoulos, A. G., Havaki, S., & Gorgoulis, V. G. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00204 · Cited by 169 · see citing works

Prolonged tau clearance and stress vulnerability rescue by pharmacological activation of autophagy in tauopathy neurons

Silva, M. C., Nandi, G. A., Tentarelli, S., Gurrell, I. K., Jamier, T., Lucente, D., Dickerson, B. C., Brown, D. G., Brandon, N. J., & Haggarty, S. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16984-1 · Cited by 157 · see citing works

Progranulin deficiency causes impairment of autophagy and TDP-43 accumulation

Chang, M. C., Srinivasan, K., Friedman, B. A., Suto, E., Modrusan, Z., Lee, W. P., Kaminker, J. S., Hansen, D. V., & Sheng, M. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20160999 · Cited by 141 · see citing works

The mechanism and efficacy of GLP-1 receptor agonists in the treatment of Alzheimer’s disease

Du, H., Meng, X., Yao, Y., & Xu, J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.1033479 · Cited by 125 · see citing works

Three-dimensional hyaluronic acid hydrogel-based models for in vitro human iPSC-derived NPC culture and differentiation

Wu, S., Xu, R., Duan, B., & Jiang, P. (2017) · Journal of Materials Chemistry B · doi:10.1039/c7tb00721c · Cited by 111 · see citing works

&lt;p&gt;Chlorogenic Acid Alleviates Aβ&lt;sub&gt;25-35&lt;/sub&gt;-Induced Autophagy and Cognitive Impairment via the mTOR/TFEB Signaling Pathway&lt;/p&gt;

Gao, L., Li, X., Meng, S., Ma, T., Wan, L., & Xu, S. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s235969 · Cited by 115 · see citing works

Temporal inhibition of autophagy reveals segmental reversal of ageing with increased cancer risk

Cassidy, L. D., Young, A. R. J., Young, C. N. J., Soilleux, E. J., Fielder, E., Weigand, B. M., Lagnado, A., Brais, R., Ktistakis, N. T., Wiggins, K. A., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14187-x · Cited by 108 · see citing works

A catalog of single nucleotide changes distinguishing modern humans from archaic hominins

Kuhlwilm, M., & Boeckx, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-44877-x · Cited by 108 · see citing works

PICALM and Alzheimer’s Disease: An Update and Perspectives

Ando, K., Nagaraj, S., Küçükali, F., de Fisenne, M.-A., Kosa, A.-C., Doeraene, E., Lopez Gutierrez, L., Brion, J.-P., & Leroy, K. (2022) · Cells · doi:10.3390/cells11243994 · Cited by 104 · see citing works

Enhancing autophagy in Alzheimer's disease through drug repositioning

Eshraghi, M., Ahmadi, M., Afshar, S., Lorzadeh, S., Adlimoghaddam, A., Rezvani Jalal, N., West, R., Dastghaib, S., Igder, S., Torshizi, S. R. N., et al. (2022) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2022.108171 · Cited by 89 · see citing works

Activation of AMPK/mTORC1-mediated autophagy by metformin reverses Clk1 deficiency-sensitized dopaminergic neuronal death

Yan, Q., Han, C., Wang, G., Waddington, J. L., Zheng, L., & Zhen, X. (2017) · Molecular Pharmacology · doi:10.1124/mol.117.109512 · Cited by 77 · see citing works

Protective role of quercetin against copper(II)-induced oxidative stress: A spectroscopic, theoretical and DNA damage study

Jomova, K., Lawson, M., Drostinova, L., Lauro, P., Poprac, P., Brezova, V., Michalik, M., Lukes, V., & Valko, M. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.10.042 · Cited by 83 · see citing works

Novel insights into the antioxidant role of tauroursodeoxycholic acid in experimental models of Parkinson's disease

Rosa, A. I., Fonseca, I., Nunes, M. J., Moreira, S., Rodrigues, E., Carvalho, A. N., Rodrigues, C. M. P., Gama, M. J., & Castro-Caldas, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.004 · Cited by 82 · see citing works

NRBF2 is involved in the autophagic degradation process of APP-CTFs in Alzheimer disease models

Yang, C., Cai, C.-Z., Song, J.-X., Tan, J.-Q., Durairajan, S. S. K., Iyaswamy, A., Wu, M.-Y., Chen, L.-L., Yue, Z., Li, M., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1379633 · Cited by 83 · see citing works

The neurological effects of ghrelin in brain diseases: Beyond metabolic functions

Jiao, Q., Du, X., Li, Y., Gong, B., Shi, L., Tang, T., & Jiang, H. (2017) · Neuroscience &amp; Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.12.010 · Cited by 62 · see citing works

Recent progress in the role of autophagy in neurological diseases

Meng, T., Lin, S., Zhuang, H., Huang, H., He, Z., Hu, Y., Gong, Q., & Feng, D. (2019) · Cell Stress · doi:10.15698/cst2019.05.186 · Cited by 58 · see citing works

Novel Insights into the Anti-Aging Role of Mitophagy

(2018) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2018.05.005 · Cited by 56 · see citing works

Polyubiquitinylation Profile in Down Syndrome Brain Before and After the Development of Alzheimer Neuropathology

Tramutola, A., Di Domenico, F., Barone, E., Arena, A., Giorgi, A., di Francesco, L., Schininà, M. E., Coccia, R., Head, E., Butterfield, D. A., et al. (2017) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2016.6686 · Cited by 49 · see citing works

The Molecular Clock and Neurodegenerative Disease: A Stressful Time

Carter, B., Justin, H. S., Gulick, D., & Gamsby, J. J. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.644747 · Cited by 42 · see citing works

A novel <i>Atg5</i>-shRNA mouse model enables temporal control of Autophagy <i>in vivo</i>

Cassidy, L. D., Young, A. R., Pérez-Mancera, P. A., Nimmervoll, B., Jaulim, A., Chen, H.-C., McIntyre, D. J. O., Brais, R., Ricketts, T., Pacey, S., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1458172 · Cited by 40 · see citing works

Cellular and molecular modifier pathways in tauopathies: the big picture from screening invertebrate models

Hannan, S. B., Dräger, N. M., Rasse, T. M., Voigt, A., & Jahn, T. R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13532 · Cited by 38 · see citing works

Role and Potential Mechanisms of Nicotinamide Mononucleotide in Aging

Rahman, S. U., Qadeer, A., & Wu, Z. (2024) · Aging and disease · doi:10.14336/ad.2023.0519-1 · Cited by 34 · see citing works

Deregulation of autophagy under hyperglycemic conditions is dependent on increased lysine 63 ubiquitination: a candidate mechanism in the progression of diabetic nephropathy

Pontrelli, P., Oranger, A., Barozzino, M., Divella, C., Conserva, F., Fiore, M. G., Rossi, R., Papale, M., Castellano, G., Simone, S., et al. (2018) · Journal of Molecular Medicine · doi:10.1007/s00109-018-1656-3 · Cited by 26 · see citing works

Autophagy in cancer biology and therapy

Noor, N., Gammoh, Simon, 。., et al. (2014) · Acta Scientiarum Naturalium Universitatis Sunyatseni

Is Selective Autophagy Distinct from Starvation-Induced Autophagy?

Guillebaud, G., & Germain, M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802937-4.00005-3

Death and survival of neuronal and astrocytic cells in ischemic brain injury： a role of autophagy

Min, Xü, Huiling, et al. (2011) · 中国药理学报：英文版 · Cited by 1 · see citing works

There is more to autophagy than induction

Klionsky, D. J., & Nemchenko, A. (2011) · Autophagy · doi:10.4161/auto.7.8.16609 · Cited by 4 · see citing works

Roles of autophagy in lymphocytes： reflections and directions

Ian, I., McLeod, You-wen, et al. (2010) · 中国免疫学杂志：英文版 · Cited by 1 · see citing works