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

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works

Protein folding in the cell

Gething, M.-J. H., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,137 · see citing works

Molecular chaperones in cellular protein folding

Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,584 · see citing works

Protein Oxidation in Aging, Disease, and Oxidative Stress

Berlett, B. S., & Stadtman, E. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20313 · Cited by 3,339 · see citing works

Aggresomes: A Cellular Response to Misfolded Proteins

Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148 · see citing works

Aging, energy, and oxidative stress in neurodegenerative diseases

Beal, M. F. (1995) · Annals of Neurology · doi:10.1002/ana.410380304 · Cited by 1,434 · see citing works

INTERMEDIATE FILAMENTS: Structure, Dynamics, Function and Disease

Fuchs, E. V., & Weber, K. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.002021 · Cited by 1,427 · see citing works

Oxidative Stress in Neurodegenerative Diseases

Simonian, N. A., & Coyle, J. T. (1996) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.36.040196.000503 · Cited by 1,377 · see citing works

In situ neutralization in Boc‐chemistry solid phase peptide synthesis

Schnölzer, M., Alewood, P. F., Jones, A., Alewood, D., & Kent, S. B. H. (1992) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1992.tb00291.x · Cited by 1,052 · see citing works

Degradation of oxidized proteins in mammalian cells

Grune, T., Reinheckel, T., & Davies, K. J. A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.7.9212076 · Cited by 835 · see citing works

Conformational disease

Carrell, R. W., & Lomas, D. A. (1997) · The Lancet · doi:10.1016/s0140-6736(97)02073-4 · Cited by 806 · see citing works

Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

Ehrnsperger, M., Gräber, S., Gaestel, M., & Büchner, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.221 · Cited by 755 · see citing works

A human beta-actin expression vector system directs high-level accumulation of antisense transcripts.

Gunning, P. W., Leavitt, J. C., Muscat, G. E. O., Ng, S. Y., & Kedes, L. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.14.4831 · Cited by 739 · see citing works

Parkinson's Disease Is Associated with Oxidative Damage to Cytoplasmic DNA and RNA in Substantia Nigra Neurons

Zhang, J., Perry, G. L., Smith, M. A., Robertson, D., Olson, S. J., Graham, D. G., & Montine, T. J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65396-5 · Cited by 636 · see citing works

Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease

Lowe, J., Blanchard, A., Morrell, K., Lennox, G., Reynolds, L., Billett, M., Landon, M., & Mayer, R. J. (1988) · The Journal of Pathology · doi:10.1002/path.1711550105 · Cited by 539 · see citing works

Molecular chaperones in cellular protein folding

Martin, J., & Hartl, F. U. (1994) · BioEssays · doi:10.1002/bies.950160916 · Cited by 498 · see citing works

Coupling of adenovirus to transferrin-polylysine/DNA complexes greatly enhances receptor-mediated gene delivery and expression of transfected genes.

Wagner, E., Zatloukal, K., Cotten, M. L., Kirlappos, H., Mechtler, K., Curiel, D., & Birnstiel, M. L. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.6099 · Cited by 481 · see citing works

Roles of Nuclear Factor κB in Neuronal Survival and Plasticity

Mattson, M. P., Culmsee, C., Yu, Z., & Camandola, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.740443.x · Cited by 449 · see citing works

The interaction of p62 with RIP links the atypical PKCs to NF‐κB activation

Sanz, L., Sánchez‐Gómez, P., Lallena, M., Díaz-Meco, M. T., & Moscat, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.3044 · Cited by 410 · see citing works

Non-alcoholic steatohepatitis (NASH): a disease of emerging identity and importance

James, O., & Day, C. P. (1998) · Journal of Hepatology · doi:10.1016/s0168-8278(98)80073-1 · Cited by 370 · see citing works

Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice.Preprint

Baribault, H., Penner, J., Iozzo, R. V., & Wilson-Heiner, M. (1994) · Genes & Development · doi:10.1101/gad.8.24.2964 · Cited by 304 · see citing works

p62, a Phosphotyrosine-independent Ligand of the SH2 Domain of p56 , Belongs to a New Class of Ubiquitin-binding Proteins

Vadlamudi, R. K., Joung, I., Strominger, J. L., & Shin, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20235 · Cited by 299 · see citing works

Localization of Atypical Protein Kinase C Isoforms into Lysosome-Targeted Endosomes through Interaction with p62

Sánchez‐Gómez, P., de Cárcer, G., Sandoval, I. V., Moscat, J., & Díaz-Meco, M. T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.3069 · Cited by 229 · see citing works

Interaction of protein kinase C ζ with ZIP, a novel protein kinase C-binding protein

Puls, A., Schmidt, S., Grawe, F., & Stabel, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6191 · Cited by 213 · see citing works

Mallory bodies revisited

Denk, H., Stumptner, C., & Zatloukal, K. (2000) · Journal of Hepatology · doi:10.1016/s0168-8278(00)80233-0 · Cited by 208 · see citing works

Lessons from Keratin 18 Knockout Mice: Formation of Novel Keratin Filaments, Secondary Loss of Keratin 7 and Accumulation of Liver-specific Keratin 8-Positive Aggregates

Magin, T. M., Schröder, R., Leitgeb, S., Wanninger, F., Zatloukal, K., Gründ, C., & Melton, D. W. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.6.1441 · Cited by 205 · see citing works

Insulin-like Growth Factor-1-mediated Neuroprotection against Oxidative Stress Is Associated with Activation of Nuclear Factor κB

Heck, S., Lezoualc’h, F., Engert, S., & Behl, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9828 · Cited by 200 · see citing works

Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein.

Nukina, N., Kosik, K. S., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3415 · Cited by 198 · see citing works

Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain.

Joung, I., Strominger, J. L., & Shin, J. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5991 · Cited by 194 · see citing works

Keratins Turn over by Ubiquitination in a Phosphorylation-Modulated Fashion

Ku, N., & Omary, M. B. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.547 · Cited by 159 · see citing works

P62 and the sequestosome, a novel mechanism for protein metabolism

Shin, J. (1998) · Archives of Pharmacal Research · doi:10.1007/bf02976748 · Cited by 146 · see citing works

Cytokeratin 8 Protects from Hepatotoxicity, and Its Ratio to Cytokeratin 18 Determines the Ability of Hepatocytes to Form Mallory Bodies

Zatloukal, K., Stumptner, C., Lehner, M., et al. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64997-8 · Cited by 142 · see citing works

Ubiquitin-Binding Protein p62 Expression Is Induced during Apoptosis and Proteasomal Inhibition in Neuronal Cells

Kuusisto, E., Suuronen, T., & Salminen, A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4107 · Cited by 131 · see citing works

Effects of Chronic Ethanol Administration on Rat Liver Proteasome Activities: Relationship With Oxidative Stress

Fataccioli, V., Andraud, E., Gentil, M., French, S. W., & Rouach, H. (1999) · Hepatology · doi:10.1002/hep.510290106 · Cited by 128 · see citing works

Oxidative stress-inducible proteins in macrophages

Ishii, T., Itoh, K., Sato, H., & Bannai, S. (1999) · Free Radical Research · doi:10.1080/10715769900300921 · Cited by 116 · see citing works

Ultrastructural, biochemical, and immunologic characterization of Mallory bodies in livers of griseofulvin-treated mice. Fimbriated rods of filaments containing prekeratin-like polypeptides.

Franke, W. W., Denk, H., Schmid, E., et al. (1979) · PubMed · Cited by 113 · see citing works

Intermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus.

Bader, B., Magin, T. M., Freudenmann, M., et al. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.5.1293 · Cited by 112 · see citing works

Ubiquitin is present on the cytokeratin intermediate filaments and Mallory bodies of hepatocytes.

Ohta, M., Marceau, N., Perry, G. L., Manetto, V., Gambetti, P., AUTILIO‐GAMBETTI, L., Metuzals, J., Kawahara, H., Cadrin, M., & French, S. W. (1988) · PubMed · Cited by 100 · see citing works

Hepatocyte Cytokeratins Are Hyperphosphorylated at Multiple Sites in Human Alcoholic Hepatitis and in a Mallory Body Mouse Model

Stumptner, C., Omary, M. B., Fickert, P., Denk, H., & Zatloukal, K. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64708-6 · Cited by 92 · see citing works

Effect of Structure on the Signal Strength of Oligosaccharides in Matrix-assisted Laser Desorption/Ionization Mass Spectrometry on Time-of-flight and Magnetic Sector Instruments

Naven, T. J. P., & Harvey, D. J. (1996) · Rapid Communications in Mass Spectrometry · doi:10.1002/(sici)1097-0231(199608)10:11 · Cited by 90 · see citing works

Murine Peritoneal Macrophages Induce a Novel 60-kDa Protein with Structural Similarity to a Tyrosine Kinase p56lck-Associated Protein in Response to Oxidative Stress

Ishii, T., Yanagawa, T., Kawane, T., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1377 · Cited by 86 · see citing works

Analysis of Intracytoplasmic Hyaline Bodies in a Hepatocellular Carcinoma

Stumptner, C., Heid, H., Fuchsbichler, A., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65426-0 · Cited by 83 · see citing works

Low Micromolar Levels of Hydrogen Peroxide and Proteasome Inhibitors Induce the 60-kDa A170 Stress Protein in Murine Peritoneal Macrophages

Ishii, T., Yanagawa, T., Yuki, K., Kawane, T., Yoshida, H., & Bannai, S. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6221 · Cited by 67 · see citing works

Role of ubiquitin in proteasomal degradation of mutant α1-antitrypsin Z in the endoplasmic reticulum

Teckman, J. H., Gilmore, R., & Perlmutter, D. H. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.278.1.g39 · Cited by 64 · see citing works

Molecular events involved in transcriptional activation of heat shock genes become progressively refractory to heat stimulation during aging of human diploid fibroblasts

Liu, A. Y. ‐., Choi, H., Lee, Y., et al. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041490327 · Cited by 53 · see citing works

High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies.

Zatloukal, K., Fésüs, L., Denk, H., Tarcsa, E., Spurej, G., & Böck, G. (1992) · PubMed · Cited by 52 · see citing works

Immunological and biochemical characterization of the keratin‐related component of Mallory bodies: A pathological pattern of hepatocytic cytokeratins

Denk, H., Krepler, R., Lackinger, E., et al. (1982) · Liver International · doi:10.1111/j.1600-0676.1982.tb00194.x · Cited by 50 · see citing works

p62 Functions as a p38 MAP Kinase Regulator

SUDO, T., Maruyama, M., & Osada, H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2333 · Cited by 42 · see citing works

Common epitopes of human and murine Mallory bodies and Lewy bodies as revealed by a neurofilament antibody.

Kh, P., Zatloukal, K., Spurej, G., et al. (1992) · PubMed · Cited by 26 · see citing works

Cytoskeletal alterations leading to Mallory body formation in livers of mice fed 3,5-diethoxycarbonyl-1,4-dihydrocollidine

Tsunoo, C., Harwood, T. R., Arak, S., et al. (1987) · Journal of Hepatology · doi:10.1016/s0168-8278(87)80065-x · Cited by 23 · see citing works

Cloning, Expression Profile, and Genomic Organization of the Mouse STAP/A170 Gene

Okazaki, M., Ito, S., Kawakita, K., Takeshita, S., Kawai, S., Makishima, F., Oda, H., & Kakinuma, A. (1999) · Genomics · doi:10.1006/geno.1999.5902 · Cited by 18 · 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

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

Compromised autophagy and neurodegenerative diseases

Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851 · see citing works

Structural Basis for Sorting Mechanism of p62 in Selective Autophagy

Ichimura, Y., Kumanomidou, T., Sou, Y.-S., Mizushima, T., Ezaki, J., Ueno, T., Kominami, E., Yamane, T., Tanaka, K., & Komatsu, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802182200 · Cited by 803 · see citing works

Stress-activated cap’n’collar transcription factors in aging and human disease

Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776 · see citing works

<emph type="ital">SQSTM1</emph> 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

Selective autophagy: ubiquitin-mediated recognition and beyond

Kraft, C., Peter, M., & Hofmann, K. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-836 · Cited by 639 · see citing works

Autophagy in the liver: functions in health and disease

Ueno, T., & Komatsu, M. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.185 · Cited by 500 · see citing works

ALS phenotypes with mutations in <i>CHMP2B</i> (charged multivesicular body protein 2B)

Parkinson, N., Ince, P. G., Smith, M. O., Highley, R., Skibinski, G., Andersen, P. M., Morrison, K. E., Pall, H. S., Hardiman, O., Collinge, J., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000231510.89311.8b · Cited by 395 · see citing works

Ref(2)P, the <i>Drosophila melanogaster</i> homologue of mammalian p62, is required for the formation of protein aggregates in adult brain

Nezis, I. P., Simonsen, A., Sagona, A. P., Finley, K., Gaumer, S., Contamine, D., Rusten, T. E., Stenmark, H., & Brech, A. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200711108 · Cited by 370 · see citing works

Autophagy and the ubiquitin-proteasome system: Collaborators in neuroprotection

Nedelsky, N. B., Todd, P. K., & Taylor, J. P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.002 · Cited by 351 · 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

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 · see citing works

Autophagy and heterophagy dysregulation leads to retinal pigment epithelium dysfunction and development of age-related macular degeneration

Kaarniranta, K., Sinha, D., Blasiak, J., Kauppinen, A., Veréb, Z., Salminen, A., Boulton, M. E., & Petrovski, G. (2013) · Autophagy · doi:10.4161/auto.24546 · Cited by 326 · see citing works

<i>SQSTM1</i> mutations in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Rubino, E., Rainero, I., Chiò, A., Rogaeva, E., Galimberti, D., Fenoglio, P., Grinberg, Y., Isaia, G., Calvo, A., Gentile, S., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e31826e25df · Cited by 286 · see citing works

Genetic inactivation of p62 leads to accumulation of hyperphosphorylated tau and neurodegeneration

Ramesh Babu, J., Lamar Seibenhener, M., Peng, J., Strom, A., Kemppainen, R., Cox, N., Zhu, H., Wooten, M. C., Diaz‐Meco, M. T., Moscat, J., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05340.x · Cited by 258 · see citing works

Age-related macular degeneration (AMD): Alzheimer's disease in the eye?

Kaarniranta, K., Salminen, A., Haapasalo, A., Soininen, H., & Hiltunen, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101908 · Cited by 248 · see citing works

p62, Ref(2)P and ubiquitinated proteins are conserved markers of neuronal aging, aggregate formation and progressive autophagic defects

Bartlett, B. J., Isakson, P., Lewerenz, J., Sanchez, H., Kotzebue, R. W., Cumming, R. C., Harris, G. L., Nezis, I. P., Schubert, D. R., Simonsen, A., et al. (2011) · Autophagy · doi:10.4161/auto.7.6.14943 · Cited by 215 · see citing works

Mechanisms of Selective Autophagy in Normal Physiology and Cancer

Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196 · see citing works

Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin‐independent mechanism

Gal, J., Ström, A., Kwinter, D. M., Kilty, R., Zhang, J., Shi, P., Fu, W., Wooten, M. W., & Zhu, H. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06388.x · Cited by 187 · 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

Immunoreactivities of p62, an ubiqutin-binding protein, in the spinal anterior horn cells of patients with amyotrophic lateral sclerosis

Mizuno, Y., Amari, M., Takatama, M., Aizawa, H., Mihara, B., & Okamoto, K. (2006) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2006.05.060 · Cited by 158 · see citing works

SQSTM1 mutations – Bridging Paget disease of bone and ALS/FTLD

Rea, S. L., Majcher, V., Searle, M. S., & Layfield, R. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.01.020 · Cited by 152 · see citing works

Role of p62/SQSTM1 in liver physiology and pathogenesis

Manley, S., Williams, J. A., & Ding, W.-X. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213489446 · Cited by 135 · see citing works

An MND/ALS phenotype associated with <i>C9orf72</i> repeat expansion: Abundant p62‐positive, TDP‐43‐negative inclusions in cerebral cortex, hippocampus and cerebellum but without associated cognitive decline

Troakes, C., Maekawa, S., Wijesekera, L., Rogelj, B., Siklós, L., Bell, C., Smith, B., Newhouse, S., Vance, C., Johnson, L., et al. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2011.01286.x · Cited by 124 · see citing works

New Insights Into the Role of Sequestosome 1/p62 Mutant Proteins in the Pathogenesis of Paget's Disease of Bone

Rea, S. L., Walsh, J. P., Layfield, R., Ratajczak, T., & Xu, J. (2013) · Endocrine Reviews · doi:10.1210/er.2012-1034 · Cited by 123 · see citing works

Oxidative damage to the promoter region of SQSTM1/p62 is common to neurodegenerative disease

Du, Y., Wooten, M. C., & Wooten, M. W. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.015 · Cited by 96 · see citing works

Neuronal and glial inclusions in frontotemporal dementia with or without motor neuron disease are immunopositive for p62

Arai, T., Nonaka, T., Hasegawa, M., Akiyama, H., Yoshida, M., Hashizume, Y., Tsuchiya, K., Oda, T., & Ikeda, K. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00216-7 · Cited by 92 · see citing works

Keap1 is localized in neuronal and glial cytoplasmic inclusions in various neurodegenerative diseases

Tanji, K., Maruyama, A., Odagiri, S., Mori, F., Itoh, K., Kakita, A., Takahashi, H., & Wakabayashi, K. (2013) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e31827b5713 · Cited by 80 · see citing works

SQSTM1 and Paget?s Disease of Bone

Layfield, R., & Hocking, L. J. (2004) · Calcified Tissue International · doi:10.1007/s00223-004-0041-0 · Cited by 76 · see citing works

Selective Autophagy Receptors in Neuronal Health and Disease

Conway, O., Akpinar, H. A., Rogov, V. V., & Kirkin, V. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.013 · Cited by 75 · see citing works

Type I interferon enhances necroptosis of <i>Salmonella</i> Typhimurium–infected macrophages by impairing antioxidative stress responses

Hos, N. J., Ganesan, R., Gutiérrez, S., Hos, D., Klimek, J., Abdullah, Z., Krönke, M., & Robinson, N. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201701107 · Cited by 64 · see citing works

Brain-neuron targeted nanoparticles for peptide synergy therapy at dual-target of Alzheimer’s disease

Guo, Q., Li, Y., Xu, S., Wang, P., Qian, K., Yang, P., Sheng, D., Wang, L., Cheng, Y., Meng, R., et al. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.01.074 · Cited by 40 · see citing works

Intranuclear inclusions of meningioma associated with abnormal cytoskeletal protein expression

Yoshida, T., Hirato, J., Sasaki, A., et al. (1999) · Brain Tumor Pathology · doi:10.1007/bf02478908 · Cited by 13 · see citing works

An Electron Microscope Study of Intranuclear Inclusions in Mouse Liver and Hepatoma

Leduc, E. H., & Wilson, J. W. (1959) · The Journal of Cell Biology · doi:10.1083/jcb.6.3.427 · Cited by 115 · see citing works

The Ultrastructure of Cytoplasmic Inclusions in Circulating Lymphocytes in Canine Distemper

Watson, A. D. J., & Rg, W. (1974) · Research in Veterinary Science · doi:10.1016/s0034-5288(18)33680-4 · Cited by 5 · see citing works

Nuclear and cytoplasmic inclusions in normal human epidermis

Karásek, J., Hrdlička, A., & Smetana, K. (1974) · Archives of Dermatological Research · doi:10.1007/bf00558194 · Cited by 3 · see citing works

Structure of inclusion bodies of cabbage black ring virus.

Brčák, J., & Králík, O. (1977) · PubMed · Cited by 1 · see citing works