The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Autophagy gone awry in neurodegenerative diseases
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Autophagic flux dysfunction contributes to AD, PD, HD, and ALS.
“Autophagic flux, encompassing autophagosome formation, maturation, lysosomal fusion, and degradation, is essential for neuronal homeostasis, and its dysfunction contributes to AD, PD, HD, and ALS (Williams et al. 2006), (Rubinsztein et al. 2007), (Wong and Cuervo 2010).”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Wong and Cuervo 2010
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
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
Self-citationParkin 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
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
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609
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
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
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 · cited 1×
“Cross-talk between these pathways is of particular interest in neurodegeneration because primary blockage of CMA has been identified in Parkinson's disease models and certain tauopathie”
Self-citationα-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.
Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234
Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z. (2009) · Nature Cell Biology · doi:10.1038/ncb1854 · Cited by 1,005
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
Self-citationBeclin–phosphatidylinositol 3‐kinase complex functions at the trans‐Golgi network
Kihara, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve061 · Cited by 813
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756
Self-citationHDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin.
Iwata, A., Riley, B. E., Johnston, J. A., & Kopito, R. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508786200 · Cited by 719
Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702115 · Cited by 626
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
Komatsu, M., Wang, Q. J., Holstein, G. R., Friedrich, V. L., Iwata, J.-I., Kominami, E., Chait, B. T., Tanaka, K., & Yue, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701311104 · Cited by 614
Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
Shibata, M., Lu, T., Furuya, T., Degterev, A., Mizushima, N., Yoshimori, T., MacDonald, M., Yankner, B., & Yuan, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600364200 · Cited by 458
Neurodegenerative lysosomal disorders: A continuum from development to late age
Nixon, R. A., Yang, D.-S., & Lee, J.-H. (2008) · Autophagy · doi:10.4161/auto.6259 · Cited by 362
Induction of Autophagy in Axonal Dystrophy and Degeneration
Wang, Q. J., Ding, Y., Kohtz, S., Mizushima, N., Cristea, I. M., Rout, M. P., Chait, B. T., Zhong, Y., Heintz, N., & Yue, Z. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2261-06.2006 · Cited by 308
Chaperone-mediated autophagy: selectivity pays off
Cuervo, A. M. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.10.003 · Cited by 260 · cited 1×
“In the third common type of autophagy, CMA, cargo is not sequestered but is instead selectively recognized by a complex of cytosolic chaperones that mediates its delivery to a receptor at the lysosomal membran”
Self-citationKanazawa, T., Taneike, I., Akaishi, R., Yoshizawa, F., Furuya, N., Fujimura, S., & Kadowaki, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306337200 · Cited by 208
Flagged first, then by citations
Research works printed but not linked: 77
- Klionsky, D.J. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8, 931–937 (2007). · DOI
- Rubinsztein, D.C., Gestwicki, J.E., Murphy, L.O. & Klionsky, D.J. Potential therapeutic applications of autophagy. Nat. Rev. Drug Discov. 6, 304–312 (2007). · DOI · Paper page
- Winslow, A.R. & Rubinsztein, D.C. Autophagy in neurodegeneration and development. Biochim. Biophys. Acta 1782, 723–729 (2008). · DOI
- Komatsu, M. et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441, 880–884 (2006). · DOI · Paper page
- Pickford, F. et al. The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J. Clin. Invest. 118, 2190–2199 (2008).
- Fimia, G.M. et al. Ambra1 regulates autophagy and development of the nervous system. Nature 447, 1121–1125 (2007). · DOI
- Kegel, K.B. et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J. Neurosci. 20, 7268–7278 (2000). · DOI · Paper page
- Nixon, R.A. et al. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J. Neuropathol. Exp. Neurol. 64, 113–122 (2005). · DOI · Paper page
- Yang, Y., Fukui, K., Koike, T. & Zheng, X. Induction of autophagy in neurite degeneration of mouse superior cervical ganglion neurons. Eur. J. Neurosci. 26, 2979–2988 (2007). · DOI
- Mortimore, G.E., Poso, A.R. & Lardeux, B.R. Mechanism and regulation of protein degradation in liver. Diabetes Metab. Rev. 5, 49–70 (1989). · DOI
- Dice, J.F. Chaperone-mediated autophagy. Autophagy 3, 295–299 (2007). · DOI
- Meijer, A.J. & Codogno, P. Autophagy: regulation and role in disease. Crit. Rev. Clin. Lab. Sci. 46, 210–240 (2009). · DOI
- Boland, B. et al. Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J. Neurosci. 28, 6926–6937 (2008). · DOI · Paper page
- Ravikumar, B., Duden, R. & Rubinsztein, D. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11, 1107–1117 (2002). · DOI
- Stefanis, L., Larsen, K., Rideout, H., Sulzer, D. & Greene, L. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J. Neurosci. 21, 9549–9560 (2001). · DOI
- Morimoto, N. et al. Increased autophagy in transgenic mice with a G93A mutant SOD1 gene. Brain Res. 1167, 112–117 (2007). · DOI · Paper page
- Li, L., Zhang, X. & Le, W. Altered macroautophagy in the spinal cord of SOD1 mutant mice. Autophagy 4, 290–293 (2008). · DOI
- Iwata, A. et al. Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proc. Natl. Acad. Sci. USA 102, 13135–13140 (2005). · DOI
- Samara, C., Syntichaki, P. & Tavernarakis, N. Autophagy is required for necrotic cell death in Caenorhabditis elegans. Cell Death Differ. 15, 105–112 (2008). · DOI
- Uchiyama, Y., Koike, M., Shibata, M. & Sasaki, M. Autophagic neuron death. Methods Enzymol. 453, 33–51 (2009). · DOI
- Cherra, S.J. & Chu, C.T. Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurol. 3, 309–323 (2008). · DOI
- Rubinsztein, D.C. et al. In search of an “autophagomometer”. Autophagy 5, 585–589 (2009). · DOI · Paper page
- Axe, E.L. et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol. 182, 685–701 (2008). · DOI · Paper page
- Ohsumi, Y. & Mizushima, N. Two ubiquitin-like conjugation systems essential for autophagy. Semin. Cell Dev. Biol. 15, 231–236 (2004). · DOI
- Simonsen, A. et al. Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila. Autophagy 4, 176–184 (2008). · DOI · Paper page
- Erlich, S., Shohami, E. & Pinkas-Kramarski, R. Neurodegeneration induces upregulation of Beclin 1. Autophagy 2, 49–51 (2006). · DOI
- Pattingre, S. et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 122, 927–939 (2005). · DOI · Paper page
- Pattingre, S. et al. Role of JNK1-dependent Bcl-2 phosphorylation in ceramide-induced macroautophagy. J. Biol. Chem. 284, 2719–2728 (2009). · DOI
- Rosenbluth, J.M. & Pietenpol, J.A. mTOR regulates autophagy-associated genes downstream of p73. Autophagy 5, 114–116 (2009). · DOI
- Kraft, C., Reggiori, F. & Peter, M. Selective types of autophagy in yeast. Biochim. Biophys. Acta 1793, 1404–1412 (2009). · DOI
- Kirkin, V., McEwan, D.G., Novak, I. & Dikic, I. A role for ubiquitin in selective autophagy. Mol. Cell 34, 259–269 (2009). · DOI
- Sarkar, S., Ravikumar, B. & Rubinsztein, D.C. Autophagic clearance of aggregate-prone proteins associated with neurodegeneration. Methods Enzymol. 453, 83–110 (2009). · DOI · Paper page
- Bjorkoy, G. et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603–614 (2005). · DOI · Paper page
- Tan, J.M., Wong, E.S., Dawson, V.L., Dawson, T.M. & Lim, K.L. Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy. Autophagy 4, 251–253 (2007). · DOI
- Komatsu, M. et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149–1163 (2007). · DOI · Paper page
- Zheng, Y.T. et al. The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway. J. Immunol. 183, 5909–5916 (2009). · DOI
- Kim, P.K., Hailey, D.W., Mullen, R.T. & Lippincott-Schwartz, J. Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes. Proc. Natl. Acad. Sci. USA 105, 20567–20574 (2008). · DOI
- Kirkin, V. et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol. Cell 33, 505–516 (2009). · DOI · Paper page
- Thurston, T.L.M., Ryzhakov, G., Bloor, S., von Muhlinen, N. & Randow, F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10, 1215–1221 (2009). · DOI
- Wong, E.S. et al. Autophagy-mediated clearance of aggresomes is not a universal phenomenon. Hum. Mol. Genet. 17, 2570–2582 (2008). · DOI
- Jeong, H. et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 137, 60–72 (2009). · DOI
- Mookerjee, S. et al. Posttranslational modification of ataxin-7 at lysine 257 prevents autophagy-mediated turnover of an N-terminal caspase-7 cleavage fragment. J. Neurosci. 29, 15134–15144 (2009). · DOI
- Webb, J.L., Ravikumar, B. & Rubinsztein, D.C. Microtubule disruption inhibits autophagosome-lysosome fusion: implications for studying the roles of aggresomes in polyglutamine diseases. Int. J. Biochem. Cell Biol. 36, 2541–2550 (2004). · DOI
- Kochl, R., Hu, X.W., Chan, E.Y. & Tooze, S.A. Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Traffic 7, 129–145 (2006). · DOI
- Kimura, S., Noda, T. & Yoshimori, T. Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct. Funct. 33, 109–122 (2008). · DOI · Paper page
- Pacheco, C.D., Elrick, M.J. & Lieberman, A.P. Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis. Hum. Mol. Genet. 18, 956–965 (2009). · DOI
- Settembre, C. et al. A block of autophagy in lysosomal storage disorders. Hum. Mol. Genet. 17, 119–129 (2008). · DOI
- Vergarajauregui, S., Connelly, P.S., Daniels, M.P. & Puertollano, R. Autophagic dysfunction in mucolipidosis type IV patients. Hum. Mol. Genet. 17, 2723–2737 (2008). · DOI
- Bi, X. & Liao, G. Autophagic-lysosomal dysfunction and neurodegeneration in Niemann-Pick Type C mice: lipid starvation or indigestion? Autophagy 3, 646–648 (2007). · DOI
- Lee, J.-H. et al. Presenilin 1 (PS1) is required for v-ATPase targeting and autolysosome acidification. Cell (in the press).
- Yu, W.H. et al. Macroautophagy—a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease. J. Cell Biol. 171, 87–98 (2005). · DOI · Paper page
- Kaasik, A., Rikk, T., Piirsoo, A., Zharkovsky, T. & Zharkovsky, A. Up-regulation of lysosomal cathepsin L and autophagy during neuronal death induced by reduced serum and potassium. Eur. J. Neurosci. 22, 1023–1031 (2005). · DOI
- Massey, A.C., Kaushik, S., Sovak, G., Kiffin, R. & Cuervo, A.M. Consequences of the selective blockage of chaperone-mediated autophagy. Proc. Natl. Acad. Sci. USA 103, 5805–5810 (2006). · DOI · Paper page
- Kaushik, S., Massey, A., Mizushima, N. & Cuervo, A.M. Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol. Biol. Cell 19, 2179–2192 (2008). · DOI
- Martinez-Vicente, M. et al. Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. J. Clin. Invest. 118, 777–788 (2008).
- Lee, J.A. & Gao, F.B. Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia. J. Neurosci. 29, 8506–8511 (2009). · DOI
- Urwin, H., Ghazi-Noori, S., Collinge, J. & Isaacs, A. The role of CHMP2B in frontotemporal dementia. Biochem. Soc. Trans. 37, 208–212 (2009). · DOI
- Rusten, T.E. et al. ESCRTs and Fab1 regulate distinct steps of autophagy. Curr. Biol. 17, 1817–1825 (2007). · DOI
- Eskelinen, E.L. et al. Role of LAMP-2 in lysosome biogenesis and autophagy. Mol. Biol. Cell 13, 3355–3368 (2002). · DOI · Paper page
- Massey, A.C., Follenzi, A., Kiffin, R., Zhang, C. & Cuervo, A.M. Early cellular changes after blockage of chaperone-mediated autophagy. Autophagy 4, 442–456 (2008). · DOI
- Kovacs, G.G. & Herbert, B. Prion diseases: from protein to cell pathology. Am. J. Pathol. 172, 555–565 (2008). · DOI
- Frost, B. & Diamond, M.I. Prion-like mechanisms in neurodegenerative diseases. Nat. Rev. Neurosci. 11, 155–159 (2009). · DOI · Paper page
- Heiseke, A., Aguib, Y. & Schatzl, H.M. Autophagy, prion infection and their mutual interactions. Curr. Issues Mol. Biol. 12, 87–98 (2009).
- Nedelsky, N.B., Todd, P.K. & Taylor, J.P. Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection. Biochim. Biophys. Acta 1782, 691–699 (2008). · DOI · Paper page
- Ding, Q. et al. Characterization of chronic low-level proteasome inhibition on neural homeostasis. J. Neurochem. 86, 489–497 (2003). · DOI
- Pan, T. et al. Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement. Neurobiol. Dis. 32, 16–25 (2008). · DOI
- Kirkin, V., Lamark, T., Johansen, T. & Dikic, I. NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets. Autophagy 5, 732–733 (2009). · DOI
- Zhang, X.D. et al. p53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum. Autophagy 5, 339–350 (2009). · DOI
- Korolchuk, V.I., Mansilla, A., Menzies, F.M. & Rubinsztein, D.C. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol. Cell 33, 517–527 (2009). · DOI · Paper page
- Ichimura, Y., Kominami, E., Tanaka, K. & Komatsu, M. Selective turnover of p62/A170/SQSTM1 by autophagy. Autophagy 4, 1063–1066 (2008). · DOI
- Dagda, R.K. et al. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem. 284, 13843–13855 (2009). · DOI · Paper page
- Chu, C.T., Zhu, J. & Dagda, R. Beclin 1-independent pathway of damage-induced mitophagy and autophagic stress: implications for neurodegeneration and cell death. Autophagy 3, 663–666 (2007). · DOI
- Sardiello, M. et al. A gene network regulating lysosomal biogenesis and function. Science 325, 473–477 (2009). · DOI · Paper page
- Sarkar, S. et al. A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum. Mol. Genet. 17, 170–178 (2008). · DOI
- Yamamoto, A., Cremona, M. & Rothman, J. Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J. Cell Biol. 172, 719–731 (2006). · DOI
- Scarlatti, F., Maffei, R., Beau, I., Codogno, P. & Ghidoni, R. Role of non-canonical Beclin 1-independent autophagy in cell death induced by resveratrol in human breast cancer cells. Cell Death Differ. 15, 1318–1329 (2008). · DOI · Paper page
- Nishida, Y. et al. Discovery of Atg5/Atg7-independent alternative macroautophagy. Nature 461, 654–658 (2009). · DOI · Paper page
Cited by
Sorted by citations
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
The Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
Autophagy in Human Health and Disease
Choi, A. M. K., Ryter, S. W., & Levine, B. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1205406 · Cited by 2,583
Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811
Obesity is associated with hypothalamic injury in rodents and humans.
Thaler, J. P., Yi, C.-X., Schur, E. A., Guyenet, S. J., Hwang, B. H., Dietrich, M. O., Zhao, X., Sarruf, D. A., Izgur, V., Maravilla, K. R., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci59660 · Cited by 1,857
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
Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β
Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., & Deretic, V. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.398 · Cited by 967
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
AMP-Activated Protein Kinase (AMPK) Controls the Aging Process via an Integrated Signaling Network
Salminen, A., & Kaarniranta, K. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2011.12.005 · Cited by 860
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
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Regulation of lipid stores and metabolism by lipophagy
Liu, K., & Czaja, M. J. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.63 · Cited by 542
Deficient autophagy in microglia impairs synaptic pruning and causes social behavioral defects
Kim, H.-J., Cho, M.-H., Shim, W. H., Kim, J. K., Jeon, E.-Y., Kim, D.-H., & Yoon, S.-Y. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.103 · Cited by 475
Mitter, S. K., Song, C., Qi, X., Mao, H., Rao, H., Akin, D., Lewin, A., Grant, M., Dunn, W., Ding, J., et al. (2014) · Autophagy · doi:10.4161/auto.36184 · Cited by 449
Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414
Noncanonical autophagy promotes the visual cycle
Kim, J.-Y., Zhao, H., Martinez, J., Doggett, T. A., Kolesnikov, A. V., Tang, P. H., Ablonczy, Z., Chan, C.-C., Zhou, Z., Green, D. R., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.012 · Cited by 347
HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?
Simões-Pires, C., Zwick, V., Nurisso, A., Schenker, E., Carrupt, P.-A., & Cuendet, M. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-7 · Cited by 341
Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy
Tanik, S. A., Schultheiss, C. E., Volpicelli-Daley, L. A., Brunden, K. R., & Lee, V. M. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457408 · Cited by 326
Molecular mechanism of diabetic neuropathy and its pharmacotherapeutic targets
Dewanjee, S., Das, S., Das, A. K., Bhattacharjee, N., Dihingia, A., Dua, T. K., Kalita, J., & Manna, P. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.06.034 · Cited by 300
Proteostasis and the Aging Proteome in Health and Disease
Morimoto, R. I., & Cuervo, A. M. (2014) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu049 · Cited by 277
Self-citationDeconstruction for Reconstruction: The Role of Proteolysis in Neural Plasticity and Disease
Bingol, B., & Sheng, M. (2011) · Neuron · doi:10.1016/j.neuron.2010.11.006 · Cited by 275
Liu, D., Pitta, M., Jiang, H., Lee, J.-H., Zhang, G., Chen, X., Kawamoto, E. M., & Mattson, M. P. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.020 · Cited by 238
A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy
Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238
Huett, A., Heath, R. J., Begun, J., Sassi, S. O., Baxt, L. A., Vyas, J. M., Goldberg, M. B., & Xavier, R. J. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.10.019 · Cited by 239
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
Self-citationParkinson’s disease as a result of aging
Rodriguez, M., Rodriguez‐Sabate, C., Morales, I., Sanchez, A., & Sabate, M. (2015) · Aging Cell · doi:10.1111/acel.12312 · Cited by 214
Tashiro, Y., Urushitani, M., Inoue, H., Koike, M., Uchiyama, Y., Komatsu, M., Tanaka, K., Yamazaki, M., Abe, M., Misawa, H., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.417600 · Cited by 194
TDP‐43 loss of function increases TFEB activity and blocks autophagosome–lysosome fusion
Xia, Q., Wang, H., Hao, Z., Fu, C., Hu, Q., Gao, F., Ren, H., Chen, D., Han, J., Ying, Z., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201591998 · Cited by 195
The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease
Ihara, Y., Morishima-Kawashima, M., & Nixon, R. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006361 · Cited by 190
ATP13A2 regulates mitochondrial bioenergetics through macroautophagy
Gusdon, A. M., Zhu, J., Van Houten, B., & Chu, C. T. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.015 · Cited by 167
Cyclic GMP-AMP synthase promotes the inflammatory and autophagy responses in Huntington disease
Sharma, M., Rajendrarao, S., Shahani, N., Ramírez-Jarquín, U. N., & Subramaniam, S. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002144117 · Cited by 155
Annunziata, I., Patterson, A., Helton, D., Hu, H., Moshiach, S., Gomero, E., Nixon, R., & d’Azzo, A. (2013) · Nature Communications · doi:10.1038/ncomms3734 · Cited by 146
Lysosomal adaptation: how the lysosome responds to external cues
Settembre, C., & Ballabio, A. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016907 · Cited by 126
Are there roles for brain cell senescence in aging and neurodegenerative disorders?
Tan, F. C. C., Hutchison, E. R., Eitan, E., & Mattson, M. P. (2014) · Biogerontology · doi:10.1007/s10522-014-9532-1 · Cited by 116
Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113
Sensory neuropathy with bone destruction due to a mutation in the membrane-shaping atlastin GTPase 3
Kornak, U., Mademan, I., Schinke, M., Voigt, M., Krawitz, P., Hecht, J., Barvencik, F., Schinke, T., Gießelmann, S., Beil, F. T., et al. (2014) · Brain · doi:10.1093/brain/awt357 · Cited by 109
Integrating the DNA damage and protein stress responses during cancer development and treatment
Gorgoulis, V. G., Pefani, D., Pateras, I. S., & Trougakos, I. P. (2018) · The Journal of Pathology · doi:10.1002/path.5097 · Cited by 108
Nascimento-Ferreira, I., Nóbrega, C., Vasconcelos-Ferreira, A., Onofre, I., Albuquerque, D., Aveleira, C., Hirai, H., Déglon, N., & Pereira de Almeida, L. (2013) · Brain · doi:10.1093/brain/awt144 · Cited by 96
Proximal Tubule Autophagy Differs in Type 1 and 2 Diabetes
Sakai, S., Yamamoto, T., Takabatake, Y., Takahashi, A., Namba-Hamano, T., Minami, S., Fujimura, R., Yonishi, H., Matsuda, J., Hesaka, A., et al. (2019) · Journal of the American Society of Nephrology · doi:10.1681/asn.2018100983 · Cited by 96
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
Pathomechanisms in the neuronal ceroid lipofuscinoses
Nelvagal, H. R., Lange, J., Takahashi, K., Tarczyluk-Wells, M. A., & Cooper, J. D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165570 · Cited by 80
Saera-Vila, A., Kish, P. E., Louie, K. W., Grzegorski, S. J., Klionsky, D. J., & Kahana, A. (2016) · Autophagy · doi:10.1080/15548627.2016.1207015 · Cited by 69
Nalbandian, A., Llewellyn, K. J., Kitazawa, M., Yin, H. Z., Badadani, M., Khanlou, N., Edwards, R., Nguyen, C., Mukherjee, J., Mozaffar, T., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046308 · Cited by 68
Oxidative stress, DNA damage, and c-Abl signaling: At the crossroad in neurodegenerative diseases?
Gonfloni, S., Maiani, E., Di Bartolomeo, C., Diederich, M., & Cesareni, G. (2012) · International Journal of Cell Biology · doi:10.1155/2012/683097 · Cited by 63
Valera, E., Spencer, B., Mott, J., Trejo, M., Adame, A., Mante, M., Rockenstein, E., Troncoso, J. C., Beach, T. G., Masliah, E., et al. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00329 · Cited by 55
Dhingra, A., Bell, B. A., Peachey, N. S., Daniele, L. L., Reyes-Reveles, J., Sharp, R. C., Jun, B., Bazan, N. G., Sparrow, J. R., Kim, H. J., et al. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00351 · Cited by 41
Autophagy supports color vision
Zhou, Z., Vinberg, F., Schottler, F., Doggett, T. A., Kefalov, V. J., & Ferguson, T. A. (2015) · Autophagy · doi:10.1080/15548627.2015.1084456 · Cited by 40
Autophagy proteins regulate cell engulfment mechanisms that participate in cancer
Kim, S. E., & Overholtzer, M. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.05.004 · Cited by 35
Regulatory role of exercise-induced autophagy for sarcopenia
Liang, J., Zeng, Z., Zhang, Y., & Chen, N. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2019.110789 · Cited by 33
A neurogenic perspective of Sarcopenia: time course study of sciatic nerves from aging mice
Krishnan, V. S., White, Z., McMahon, C. D., Hodgetts, S. I., Fitzgerald, M., Shavlakadze, T., Harvey, A. R., & Grounds, M. D. (2016) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlw019 · Cited by 32
Ramachandra Rao, S., Pfeffer, B. A., Más Gómez, N., Skelton, L. A., Keiko, U., Sparrow, J. R., Rowsam, A. M., Mitchell, C. H., & Fliesler, S. J. (2018) · Autophagy · doi:10.1080/15548627.2018.1490851 · Cited by 28
TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models
Roy, B., Contu, V. R., Jeziorek, M., Friedman, W. J., & Wong, C.-O. (2026) · doi:10.64898/2026.10.21.760809
Metadata
- Authors
- Wong, E., & Cuervo, A. M.
- Venue
- Nature Neuroscience
- Published
- 2010-06-25
- Volume
- 13
- Issue
- 7
- Pages
- 805-811
- ISSN
- 1097-6256
- 1546-1726
- PMC
- PMC4038747
- Cited by
- 815
- References
- 23
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review