Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease

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

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

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

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

Autophagy as a Regulated Pathway of Cellular Degradation

Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630

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

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

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732

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

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209

Sequestosome 1/p62: a multi-domain protein with multi-faceted functions

Liu, X., Gál, J., & Zhu, H. (2012) · Frontiers in Biology · doi:10.1007/s11515-012-1217-z · Cited by 5

Aminopeptidase‐Resistant Peptides Are Targeted to Lysosomes and Subsequently Degraded

Gillis, J., Benckhuijsen, W. E., van Veen, H. A., Sanz, A. S., Drijfhout, J. W., & Reits, E. A. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01270.x · Cited by 5

Population-Specific Regulation of Chmp2b by Lbx1 during Onset of Synaptogenesis in Lateral Association Interneurons

Xu, J., Nonogaki, M., Madhira, R., Ma, H., Hermanson, O., Kioussi, C., & Gross, M. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048573 · Cited by 8

A Humanized Yeast Phenomic Model of Deoxycytidine Kinase to Predict Genetic Buffering of Nucleoside Analog Cytotoxicity

Santos, S. M., Icyuz, M., Pound, I., William, D., Guo, J., McKinney, B. A., Niederweis, M., Rodgers, J. W., & Hartman, J. L. (2019) · Genes · doi:10.3390/genes10100770 · Cited by 5

Using genetic mouse models to study the biology and pathology of autophagy in the central nervous system.

Yue, Z., Holstein, G., Chait, B., & Wang, Q.-J. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(08)04008-1 · Cited by 6

Infection and intracellular transport of white spot syndrome virus require the ESCRT machinery in shrimp

Lv, L.-X., Gao, J., Wang, H., Zhao, X., & Wang, J. (2024) · Journal of Virology · doi:10.1128/jvi.00433-24 · Cited by 5

Amino acid deprivation in cancer cells with compensatory autophagy induction increases sensitivity to autophagy inhibitors

Fukui, T., Yabumoto, M., Nishida, M., Hirokawa, S., Sato, R., Kurisu, T., Nakai, M., Hassan, M. A., & Kishimoto, K. (2024) · Molecular & Cellular Oncology · doi:10.1080/23723556.2024.2377404 · Cited by 4

Autophagy controls differentiation of Drosophila blood cells by regulating Notch levels in response to nutrient availability

Katz, M. J., Rodríguez, F., Evangelisti, F., Borrat, A., Pérez-Pandolfo, S., Peters, T., Sommario, N., Boccaccio, G. L., Melani, M., & Wappner, P. (2025) · Nature Communications · doi:10.1038/s41467-025-58389-y · Cited by 6

Atrogin-1 knockdown inhibits the autophagy-lysosome system in mammalian and avian myotubes

Saneyasu, T., Ogasawara, K., Fujiwara, Y., Honda, K., & Kamisoyama, H. (2022) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2022.111262 · Cited by 4

Neuronal Autophagy and Prion Proteins

Ragagnin, A., Guillemain, A., Nancy, J., & Bailly, Y. J. R. (2013) · InTech eBooks · doi:10.5772/55646 · Cited by 5

Familiar amyotrophic lateral sclerosis (FALS)-linked SOD1 mutation accelerates neuronal cell death by activating cleavage of caspase-4 under ER stress in an in vitro model of FALS

Koyama, Y., Hiratsuka, T., Matsuzaki, S., Yamagishi, S., Kato, S., Katayama, T., & Tohyama, M. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.08.023 · Cited by 4

Comments on Fornai et al. (PNAS/ Feb 2008)

Figlewicz, D. A. (2008) · Amyotrophic Lateral Sclerosis · doi:10.1080/17482960802066643 · Cited by 4

ESCRTs and associated proteins in lysosomal fusion with endosomes and autophagosomes

Majumder, P., & Chakrabarti, O. (2016) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0099 · Cited by 4

Genetic analysis of the Drosophila ESCRT-III complex protein, VPS24, reveals a novel function in lysosome homeostasis

Florian, J. R., DeMatte, S. J., Sweeder, D. M., Ordway, R. W., & Kawasaki, F. (2021) · PLoS ONE · doi:10.1371/journal.pone.0251184 · Cited by 4

Innovative approaches to metabolic dysfunction-associated steatohepatitis diagnosis and stratification

Matboli, M., Hamady, S., Saad, M., Khaled, R., Khaled, A., Barakat, E., Sayed, S. A., Agwa, S. H. A., & Youssef, I. (2024) · Non-coding RNA Research · doi:10.1016/j.ncrna.2024.10.002 · Cited by 4

Classical swine fever virus hijacks ESCRT-III and VPS4A to promote phagophore closure for accelerating mitophagy

Cheng, Y. F., Li, Y., Bi, X., Chen, J., Zhao, B., Bai, J., Ye, Y., Dai, Q., Zou, L., Chen, J., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2523734 · Cited by 3

The Ku80-p53-SIRT1 axis in DNA damage response contributes to sporadic and familial ALS and FTD

Jun, Y.-W., Lee, S., Almeida, S., Freude, K., Ichida, J. K., & Gao, F. (2025) · Nature Communications · doi:10.1038/s41467-025-67749-7 · Cited by 3

Lithium treatment in amyotrophic lateral sclerosis: do we have enough trials?

de Carvalho, M. A., & Pinto, S. (2011) · Expert Review of Neurotherapeutics · doi:10.1586/ern.11.164 · Cited by 3

Identification of Atypical Peri-Nuclear Multivesicular Bodies in Oxidative and Glycolytic Skeletal Muscle of Aged and Pompe's Disease Mouse Models

Neel, B. A., Zong, H., Backer, J., & Pessin, J. E. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00393 · Cited by 3

Endo‐lysosomal protein concentrations in CSF from patients with frontotemporal dementia caused by CHMP2B mutation

Toft, A. D., Sjödin, S., Simonsen, A. H., Ejlerskov, P., Roos, P., Musaeus, C. S., Henriksen, E. E., Nielsen, T. T., Brinkmalm, A., Blennow, K., et al. (2023) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.12402 · Cited by 3

Autophagy, the “Master” Regulator of Cellular Quality Control: What Happens when Autophagy Fails?

Raquel, A., Catarina, R. A., & Morais, S. (2013) · InTech eBooks · doi:10.5772/55196 · Cited by 4

Time Flies: Autophagy During Ageing in Drosophila

Schultz, S. W., Brech, A., & Ioannis, P. (2013) · InTech eBooks · doi:10.5772/55396 · Cited by 3

THE CELLULAR PROCESS OF AUTOPHAGY AND CONTROL OF AUTOPHAGY IN NEURONS

McKnight, N. C., Mizushima, N., & Yue, Z. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0001 · Cited by 3

WH2 domains and actin variants as multifunctional organizers of the actin cytoskeleton

Gallinger, J. O. (2013) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.16169 · Cited by 3

NFκB and JNK pathways mediate metabolic adaptation upon ESCRT-I deficiency

Cendrowski, J., Wróbel, M., Mazur, M., Jary, B., Maurya, R., Wang, S., Korostyński, M., Dziewulska, A., Rohm, M., Kuropka, P., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05490-y · Cited by 2

The E193K LRRK2 mutation interferes with the autophagosome processing through the impairment of the LRRK2-Dynein-1 complex

Redl, S., von Zweydorf, F., Gloeckner, C. J., Posadas, I., Ceña, V., Hess, M. W., Piccoli, G., & Pérez‐Carrión, M. D. (2025) · Scientific Reports · doi:10.1038/s41598-025-26716-4 · Cited by 2

Ribosome remodeling drives translation adaptation during viral infection and cellular stress

Tsai, H.-Y., Liu, L., Fleming, R. H., Mintseris, J., Ekanayake, D., Guo, J., Gu, X., Gygi, S. P., & Lee, A. S. Y. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.09.008 · Cited by 2

Differential levels of CHMP2B, LLPH, and SLC25A51 proteins in secondary renal amyloidosis

Gupta, N., Sahar, T., Khowal, S., Ganaie, I. A., Mughees, M., Khullar, D., Jain, S. K., & Wajid, S. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1890588 · Cited by 2

Trafficking of K63-polyubiquitin–modified membrane proteins in a macroautophagy-independent pathway is linked to ATG9A

Scavone, F., Lian, S., Eskelinen, E., Cohen, R. E., & Yao, T. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-12-0535 · Cited by 2

The Roles of ESCRT Proteins in Healthy Cells and in Disease

Ilievska, J., Naomi, E., Sarah, J. M., & Paul, R. (2012) · InTech eBooks · doi:10.5772/33537 · Cited by 2

Molecular Machinery and Genetics of the Autophagy Pathway

Herr, D. R., & Finley, K. D. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-385101-7.00002-4 · Cited by 2

Lysosomal Quality Control in Prion Diseases

Majumder, P., & Chakrabarti, O. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0512-8 · Cited by 3

Autophagy and Huntington's disease

Croce, K. R., Jasutkar, H. G., & Yamamoto, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95672-7.00018-2 · Cited by 2

Short Duration Alagebrium Chloride Therapy Prediabetes Does Not Inhibit Progression to Autoimmune Diabetes in an Experimental Model

Borg, D. J., Faridi, P., Giam, K., Reeves, P., Fotheringham, A. K., McCarthy, D. A., Leung, S. S., Ward, M. S., Harcourt, B. E., Ayala, R., et al. (2021) · Metabolites · doi:10.3390/metabo11070426 · Cited by 2

Amyloid fibrils are nanoparticles that target lysosomes.

Jakhria, T. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University) · Cited by 2

Codon-optimized TDP-43-mediated neurodegeneration in a Drosophila model for ALS/FTLDPreprint

Yusuff, T., Chatterjee, S., Chang, Y., Sang, T., & Jackson, G. R. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/696963 · Cited by 2

Intracellular Trafficking

Cheville, N. F. (2009) · Wiley eBooks · doi:10.1002/9780813810379.ch5 · Cited by 2

Autophagy and Huntington’s disease

Mano, T., & Iwata, A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00001-0 · Cited by 1

The Dynamics of the ESCRT Machinery in Open Mitosis from Physiology to Pathology

Torre, M. L., Cannistrà, F., Burla, R., & Saggio, I. (2025) · Cells · doi:10.3390/cells14211681 · Cited by 1

Deubiquitinase MoAMSH inhibits autophagy by targeting MoAtg6 in Magnaporthe oryzae

Liao, J., Shen, Z.-F., Wang, J.-Y., He, M.-F., Lv, H.-M., Zhao, J., Zhang, Y., Zhu, X., Li, L., Wang, Z., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02487-3 · Cited by 1

Mislocalization of FTD3-associated mutant CHMP2B to the nucleus of human neurons due to loss of a nuclear export signal

Jun, Y., Hass, E. P., Lee, S., Fazzio, T. G., & Gao, F. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02222-0 · Cited by 1

Integration of cross-species multi-omics with in vivo experimental validation identifies Parkinson's disease therapeutic targets and novel risk factors within endolysosomal pathway subnetworks

Moore, J., Rao, L., Garcia-Bellido, S., Guo, F., Botas, J., & Botas, J. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107364 · Cited by 1

Cutting edge: ESCRT-mediated phagophore closure in mammals

Takahashi, Y., Opozda, D. M., & Wang, H. (2026) · Biochemical Journal · doi:10.1042/bcj20250148 · Cited by 1

TDP-43: a critical amplifier of Alzheimer’s disease beyond amyloid and tau

Roy, A., Chhetry, S., Deka, H., Roy, R., Bhattacharya, P., Patel, B. K., & Borah, A. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.05.024 · Cited by 1

Role of ESCRT pathway and autophagy in neurodegenerative diseases

Dongre, S., Soni, N., & Bissa, B. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.05.022 · Cited by 1

Regulation of Endocytic Trafficking of Receptors and Transporters by Ubiquitination: Possible Role in Neurodegenerative Disease

Sorkin, A. D. (2009) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-540-87941-1_11 · Cited by 1

Contribution of Multivesicular Bodies to the Prion-Like Propagation of Lesions in Alzheimer’s Disease

Vingtdeux, V., Buée, L., & Sergeant, N. (2011) · InTech eBooks · doi:10.5772/20567 · Cited by 1

Autophagosomes and multivesicular bodies in neuronal development and degeneration

Diana, A. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0048-3 · Cited by 1

AUTOPHAGOSOME MATURATION, ENDOCYTOSIS AND NEURODEGENERATIVE DISEASE

Yamamoto, A., & Simonsen, A. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0002 · Cited by 1

Localization of CHMP2B in postnatal rd1 mouse retina

Assaf, F., Irqeba, A. A., & Ogilvie, J. M. (2018) · BIOS · doi:10.1893/0005-3155-89.2.58 · Cited by 1

Proteostasis function and dysfunction in Huntington's disease

Abramovich, J., Kleczko, K. M., Masto, V. B., & Frydman, J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95672-7.00025-x · Cited by 3

Cytoplasmic expression of trans-active response DNA-binding protein-43 in aged mice display hippocampal sclerosis-like degeneration and neuronal loss with reduced lifespan

Anderson, A. N., Dopler, M. B., Arezoumandan, S., Osei‐KanKam, D., Davis, S. A., Ajroud, K., Lilek, J. N., Bambakadis, E., Shapiro, R., Flanagan, M. E., et al. (2025) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlae137 · Cited by 1

Protein/Peptide Tags

Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.en.2.116 · Cited by 1

Autophagy and Endocytosis

Roy, R., Floyd, B. E., & Bassham, D. C. (2014) · Springer eBooks · doi:10.1007/978-1-4614-7881-2_2-1 · Cited by 1

Autophagy in head and neck cancer therapy

Lee, Y.-S., Eckers, J. C., & Kimple, R. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817868-3.00013-5 · Cited by 1

Diseases of Protein Folding: Huntington’s Disease and Amyotrophic Lateral Sclerosis

Bailus, B. J., & Ellerby, L. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10013-6 · Cited by 1

Clean up or go crazy

Williams, R. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.1793iti4 · Cited by 1

The TMEM106B rs1990621 protective variant is also associated with increased neuronal proportionPreprint

Li, Z., Farias, F. G., Dube, U., Del‐Aguila, J. L., Mihindukulasuriya, K. A., Fernández, M. V., Ibáñez, L., Budde, J., Wang, F., Lake, A. M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/583286 · Cited by 1

Identification and Characterization of autophagic and non-autophagic Interaction Partners of Atg18

Marquardt, L. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8638 · Cited by 1

Autophagy controls differentiation of Drosophila blood cells by regulating Notch levels in response to nutrient availabilityPreprint

Katz, M. J., Rodríguez, F., Evangelisti, F., Pérez-Pandolfo, S., Sommario, N., Borrat, A., Melani, M., & Wappner, P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.25.600418 · Cited by 1

Macrophage WDFY3, a protector against autoimmunityPreprint

Wu, X., Wang, Z., Croce, K. R., Li, F., Cui, J. G., D’Agati, V. D., Soni, R. K., Khalid, S., Saleheen, D., Tabas, I. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.17.608411 · Cited by 1

Linking tumour susceptibility ESCRT proteins and epithelial cell polarity

Fish, L. P. (2011) · The University of Bath Online Publications Store (The University of Bath)

SQSTM1 mutations and Paget's disease of bone

Najat, D. (2010) · Nottingham ePrints (University of Nottingham)

Clearance of intracellular aggregation-prone protein fragments

Gillis, J. (2009) · UvA-DARE (University of Amsterdam)

Analysis of the molecular mechanism of autophagosome formation in yeast and zebrafish models

He, C. (2009) · Deep Blue (University of Michigan)

A Yeast Genomic Screen to Identify Effectors of Kir2.1 Plasma Membrane Residence

Kolb, A. (2013) · D-Scholarship@Pitt (University of Pittsburgh)

Neural repair: basic cellular and molecular processes

Selzer, M. E., Clarke, S., Cohen, L. G., Kwakkel, G., & Miller, R. H. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511995583.020

Mutant Superoxide Dismutase-1-caused pathogenesis in Amyotrophic Lateral Sclerosis

Bergemalm, D. (2010) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

A Get‐Together to Tear It Apart

McLelland, G., & Fon, E. A. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch12

Connections between autophagy and other degradative pathways: investigating the role of Rab11 protein

Erdei, A., & Sass, M. (2014)

P R O T E I N FA M I LY R E V I E W

Shpilka, T., Weidberg, H., Pietrokovski, S., & Elazar, Z. (2011)

For peer review only Presymptomatic cerebral blood flow changes in CHMP2B mutation carriers of familial frontotemporal dementia (FTD- 3), measured with MRI

Mouridsen, K., Rodell, A. B., Østergaard, L., Nielsen, J. E., & Johannsen, P. (2011)

Frontotemporal Dementia Linked to Chromosome 3 in Saccharomyces cerevisiae

Sulkko, N. (2013) · CU Scholar (University of Colorado Boulder)

Dissecting molecular elements of mitophagy and the lysis of intravacuolar vesicles

Montino, M. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5327

The study of Drosophila melanogaster blue cheese (bchs) function in the involvement of autophagy in neurodegenerative disorders

Sim, J. P. L. (2014) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/64797

The genetic basis of amyotrophic lateral sclerosis: recent breakthroughs

Leuven, K. (2015)

Frontotemporal Dementia, Chromosome 3-Linked

Holm, I. E., Nielsen, J. E., Brown, J. M., Johannsen, P., & Isaacs, A. M. (2012) · University of Washington, Seattle eBooks

The role of autophagy in clearance of protein aggregates

Isakson, P. (2011) · NORA - Norwegian Open Research Archives

THE POTENTIAL OF AUTOPHAGY REGULATION IN THE TREATMENT OF NEURODEGENERATIVE DISEASES

Winslow, A. R., Green-Thompson, Z. W., & Rubinsztein, D. C. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0013

AUTOPHAGY IN AMYOTROPHIC LATERAL SCLEROSIS

Gál, J., & Zhu, H. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0009

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

The role of ALS associated genes and c-Jun in neurodegeneration

Acosta‐Saltos, A. (2016) · UCL Discovery (University College London)

Divergent Roles of Atg8 Orthologues in Autophagy

Mathur, A. (2015) · Biochemistry & Pharmacology Open Access · doi:10.4172/2167-0501.1000e177

Exosomes in the Preservation of Cellular Homeostasis

Baixauli, F., & Mittelbrunn, M. (2016) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-33486-8_2

Identification of novel components involved in selective and unselective autophagic pathways

Welter, E. (2012) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3159

AutophA gosomes And mul Ar bodies in neuronA l development And degener Ation

Diana, A. (2012)

Unselective Disposal of Cellular Aggregates

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00004-3

Development and characterization of cell models of tau aggregation

Cavallini, A. (2018) · UCL Discovery (University College London)

Autophagy and multivesicular body formation in blastocysts during the experimental diapause in mice

Lim, H., Shin, H. R., Hyun, J. J., & Song, H. (2020) · Bioscientifica Proceedings · doi:10.1530/biosciprocs.10.011

Surface Transporters and Receptors are downregulated by a two-tier system in response to diverse stimuli in Saccharomyces cerevisiae

Golden, C. K. (2021) · Spectrum Research Repository (Concordia University)

Posttranslational modifications of TDP-43

Rahman, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820066-7.20002-7

Role of chaperone-like activity of high mobility group box 1 : its role in reducing the formation of polyglutamine aggregates

민현진 (2013) · YUHSpace (Yonsei University Medical Library)

PLATFORM COMMUNICATIONS

(2012) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482968.2012.721231b

Faculty Opinions recommendation of Starvation induces rapid degradation of selective autophagy receptors by endosomal microautophagy.

Deretic, V. P. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733643363.793549028

Faculty Opinions recommendation of Starvation induces rapid degradation of selective autophagy receptors by endosomal microautophagy.

Molinari, M., & Loi, M. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733643363.793551952

Structure and molecular function of WD-40 repeat-containing autophagy proteins Atg18, Atg21 and Hsv2

Taylor, M. F. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9302

Diseases of Protein Folding: Huntington's Disease and Amyotrophic Lateral Sclerosis

Bailus, B. J., & Ellerby, L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.10013-6

A Drosophila Arl8 kis GTPáz szerepe a lizoszomális fúziós folyamatokban

Boda, A. (2020) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2020.141

ESCRT disruption provides evidence against signaling functions for synaptic exosomesPreprint

Dresselhaus, E. C., Harris, K. P., Blanchette, C. R., Koles, K., Signore, S. J. D., Pescosolido, M. F., Ermanoska, B., Rozencwaig, M., Soslowsky, R. C., Parisi, M. J., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.22.537920

Aberrant Mineral Deposition in Soft and Hard Tissues

Shapiro, I. M., & Landis, W. J. (2023) · Springer eBooks · doi:10.1007/978-3-031-34304-9_10

ESCRTing autophagic clearance of aggregating proteins

Rusten, T. E., Filimonenko, M., Rodahl, L. M., Stenmark, H., & Simonsen, A. (2008) · Autophagy · doi:10.4161/auto.5396 · Cited by 44

ESCRT functions in autophagy and associated disease

Rusten, T. E., & Simonsen, A. (2008) · Cell Cycle · doi:10.4161/cc.7.9.5784 · Cited by 118

BMB reports

(2014)

ESCRT, autophagy, and frontotemporal dementia

Lee, J., & Gao, F. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.12.827 · Cited by 29

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