Transcriptional induction of the heat shock protein B8 mediates the clearance of misfolded proteins responsible for motor neuron diseases
Open accessAbstract
Neurodegenerative diseases (NDs) are often associated with the presence of misfolded protein inclusions. The chaperone HSPB8 is upregulated in mice, the human brain and muscle structures affected during NDs progression. HSPB8 exerts a potent pro-degradative activity on several misfolded proteins responsible for familial NDs forms. Here, we demonstrated that HSPB8 also counteracts accumulation of aberrantly localized misfolded forms of TDP-43 and its 25 KDa fragment involved in most sporadic cases of Amyotrophic Lateral Sclerosis (sALS) and of Fronto Lateral Temporal Dementia (FLTD). HSPB8 acts with BAG3 and the HSP70/HSC70-CHIP complex enhancing the autophagic removal of misfolded proteins. We performed a high-through put screening (HTS) to find small molecules capable of inducing HSPB8 in neurons for therapeutic purposes. We identified two compounds, colchicine and doxorubicin, that robustly up-regulated HSPB8 expression. Both colchicine and doxorubicin increased the expression of the master regulator of autophagy TFEB, the autophagy linker p62/SQSTM1 and the autophagosome component LC3. In line, both drugs counteracted the accumulation of TDP-43 and TDP-25 misfolded species responsible for motoneuronal death in sALS. Thus, analogs of colchicine and doxorubicin able to induce HSPB8 and with better safety and tolerability may result beneficial in NDs models.
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
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?
HSPB8 overexpression enhances autophagic clearance of TARDBP via elevations in TFEB, SQSTM1, and LC3.
“HSPB8 overexpression also enhances autophagic clearance of TARDBP via elevations in TFEB, SQSTM1, and LC3 [355,356].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [356]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 · see citing works
Doxorubicin: an update on anticancer molecular action, toxicity and novel drug delivery systems
Tacar, O., Sriamornsak, P., & Dass, C. R. (2012) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2012.01567.x · Cited by 2,469 · see citing works
DNA Topoisomerases and Their Poisoning by Anticancer and Antibacterial Drugs
Pommier, Y. G., Leo, E., Zhang, H., & Marchand, C. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.04.012 · Cited by 1,842 · see citing works
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,760 · see citing works
Chatterjee, K., Zhang, J., Honbo, N. Y., & Karliner, J. S. (2009) · Cardiology · doi:10.1159/000265166 · Cited by 1,074 · see citing works
The Ubiquitin Proteasome System in Neurodegenerative Diseases
Ciechanover, A. J., & Brundin, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00606-8 · Cited by 984 · see citing works
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 · see citing works
Neuroblastoma × spinal cord (NSC) hybrid cell lines resemble developing motor neurons
Cashman, N. R., Durham, H. D., Blusztajn, J. K., Oda, K., Tabira, T., Shaw, I. T., Dahrouge, S., & Antel, J. P. (1992) · Developmental Dynamics · doi:10.1002/aja.1001940306 · Cited by 724 · see citing works
Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
Zhang, Y., Xu, Y.-F., Cook, C. N., Gendron, T. F., Roettges, P. S., Link, C. D., Lin, W.-L., Tong, J., Castanedes‐Casey, M., Ash, P. E. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900688106 · Cited by 604 · see citing works
Chaperone-Assisted Selective Autophagy Is Essential for Muscle Maintenance
Arndt, V., Dick, N., Tawo, R., Dreiseidler, M., Wenzel, D., Hesse, M., Fürst, D. O., Säftig, P., Saint, R. B., Fleischmann, B. K., et al. (2010) · Current Biology · doi:10.1016/j.cub.2009.11.022 · Cited by 572 · see citing works
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522 · see citing works
Skeletal Muscle Is a Primary Target of SOD1G93A-Mediated Toxicity
Dobrowolny, G., Aucello, M., Rizzuto, E., Beccafico, S., Mammucari, C., Bonconpagni, S., Belia, S., Wannenes, F., Nicoletti, C., Del Prete, Z., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.002 · Cited by 513 · see citing works
Interference by doxorubicin with DNA unwinding in MCF-7 breast tumor cells.
Fornari, F. A., Randolph, J. K., Yalowich, J. C., Ritke, M. K., & Gewirtz, D. A. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10149-1 · Cited by 436 · see citing works
Progranulin Mediates Caspase-Dependent Cleavage of TAR DNA Binding Protein-43
Zhang, Y., Xu, Y.-F., Dickey, C. A., Buratti, E., Baralle, F. E., Bailey, R. M., Pickering-Brown, S. M., Dickson, D. W., & Petrucelli, L. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3421-07.2007 · Cited by 371 · see citing works
BAG3 mediates chaperone‐based aggresome‐targeting and selective autophagy of misfolded proteins
Gamerdinger, M., Kaya, A. M., Uwe Wolfrum, B., Clement, A. M., & Behl, C. (2011) · EMBO Reports · doi:10.1038/embor.2010.203 · Cited by 362 · see citing works
Muscle expression of a local Igf-1 isoform protects motor neurons in an ALS mouse model
Dobrowolny, G., Giacinti, C., Pelosi, L., Nicoletti, C., Winn, N., Barberi, L., Molinaro, M., Rosenthal, N. A., & Musarò, A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200407021 · Cited by 352 · see citing works
Carra, S., Seguin, S. J., Lambert, H., & Landry, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706304200 · Cited by 347 · see citing works
Self-citationCrippa, V., Sau, D., Rusmini, P., Boncoraglio, A., Onesto, E., Bolzoni, E., Galbiati, M., Fontana, E., Marino, M., Carra, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq257 · Cited by 330 · see citing works
Self-citationHspB8 and Bag3: A new chaperone complex targeting misfolded proteins to macroautophagy
Carra, S., Seguin, S. J., & Landry, J. (2008) · Autophagy · doi:10.4161/auto.5407 · Cited by 240 · see citing works
Self-citationColchicine in clinical medicine. A guide for internists
Cocco, G., Chu, D. C. C., & Pandolfi, S. (2010) · European Journal of Internal Medicine · doi:10.1016/j.ejim.2010.09.010 · Cited by 222 · see citing works
Mutation of SOD1 in ALS: a gain of a loss of function
Sau, D., Biasi, S. D., Vitellaro‐Zuccarello, L., Riso, P., Guarnieri, S., Porrini, M., Simeoni, S., Crippa, V., Onesto, E., Palazzolo, I., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm110 · Cited by 214 · see citing works
Self-citationPalazzolo, I., Stack, C. M., Kong, L., Musarò, A., Adachi, H., Katsuno, M., Sobue, G., Taylor, J. P., Sumner, C. J., Fischbeck, K. H., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.07.019 · Cited by 213 · see citing works
Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
Wang, X., Fan, H., Ying, Z., Li, B., Wang, H., & Wang, G. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.055 · Cited by 207 · see citing works
Sun, W., Chen, J., Wang, Y., & Zheng, H. (2011) · Autophagy · doi:10.4161/auto.7.9.16521 · Cited by 189 · see citing works
Lieberman, A. P., Yu, Z., Murray, S., Peralta, R., Low, A., Guo, S., Yu, X. X., Cortes, C. J., Bennett, C. F., Monia, B. P., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.008 · Cited by 169 · see citing works
Overexpression of wild-type androgen receptor in muscle recapitulates polyglutamine disease
Monks, D. A., Johansen, J. A., Mo, K., Rao, P., Eagleson, B., Yu, Z., Lieberman, A. P., Breedlove, S. M., & Jordan, C. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705501104 · Cited by 169 · see citing works
Cortés, C. J., Ling, S., Guo, L. T., Hung, G., Tsunemi, T., Ly, L. T., Tokunaga, S., Lopez, E., Sopher, B. L., Bennett, C. F., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.001 · Cited by 167 · see citing works
Carra, S., Sivilotti, M., Chávez-Zobel, A. T., Lambert, H., & Landry, J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi174 · Cited by 163 · see citing works
Self-citationSorarú, G., D’Ascenzo, C., Polo, A., Palmieri, A., Baggio, L., Vergani, L., Gellera, C., Moretto, G., Pegoraro, E., & Angelini, C. I. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.08.012 · Cited by 159 · see citing works
BAG3 induces the sequestration of proteasomal clients into cytoplasmic puncta
Minoia, M., Boncoraglio, A., Vinet, J., Morelli, F., Brunsting, J. F., Poletti, A., Schipper-Krom, S., Reits, E. A., Kampinga, H. H., & Carra, S. (2014) · Autophagy · doi:10.4161/auto.29409 · Cited by 159 · see citing works
Self-citationDeftereos, S. G., Γιαννόπουλος, Γ., Efremidis, M., Kossyvakis, C., Katsivas, A. G., Panagopoulou, V., Papadimitriou, C., Karageorgiou, S., Doudoumis, K., Raisakis, K., et al. (2014) · Heart Rhythm · doi:10.1016/j.hrthm.2014.02.002 · Cited by 159 · see citing works
Vesicle associated membrane protein B (VAPB) is decreased in ALS spinal cord
Anagnostou, G., Akbar, M. T., Paul, P., Angelinetta, C., Steiner, T. J., & de Belleroche, J. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.07.005 · Cited by 138 · see citing works
Autophagy upregulation promotes survival and attenuates doxorubicin-induced cardiotoxicity
Sishi, B., Loos, B., van Rooyen, J., & Engelbrecht, A. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.10.005 · Cited by 137 · see citing works
BAG3 and friends: Co-chaperones in selective autophagy during aging and disease
Behl, C. (2011) · Autophagy · doi:10.4161/auto.7.7.15844 · Cited by 128 · see citing works
Cleator, S. J., Tsimelzon, A. I., Ashworth, A., Dowsett, M., Dexter, T., Powles, T. J., Hilsenbeck, S. G., Wong, H. H., Osborne, C. K., O'Connell, P., et al. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-9009-7 · Cited by 127 · see citing works
Simeoni, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.1.133 · Cited by 127 · see citing works
Durham, H. D., Dahrouge, S., & Cashman, N. R. (1993) · PubMed · Cited by 124 · see citing works
Piccioni, F., Pinton, P., Simeoni, S., Pozzi, P., Fascio, U., Vismara, G., Martini, L., Rizzuto, R., & Poletti, A. (2002) · The FASEB Journal · doi:10.1096/fj.01-1035fje · Cited by 123 · see citing works
Self-citationInhibition of α‐synuclein aggregation by small heat shock proteins
Bruinsma, I. B., Bruggink, K. A., Kinast, K., Versleijen, A., Segers-Nolten, I., Subramaniam, V., Kuiperij, H., Boelens, W., de Waal, R., & Verbeek, M. (2011) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.23152 · Cited by 121 · see citing works
Barcoding heat shock proteins to human diseases: looking beyond the heat shock response
Kakkar, V., Meister-Broekema, M., Minoia, M., Carra, S., & Kampinga, H. H. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014563 · Cited by 116 · see citing works
Self-citationbag3 gene expression is regulated by heat shock factor 1
Franceschelli, S., Rosati, A., Lerose, R., Nicola, S. D., Turco, M. C., & Pascale, M. C. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21397 · Cited by 112 · see citing works
Androgen‐induced neurite outgrowth is mediated by neuritin in motor neurones
Marron, T. U., Guerini, V., Rusmini, P., Sau, D., Brevini, T. A. L., Martini, L., & Poletti, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02836.x · Cited by 108 · see citing works
Self-citationMetabolism and mis-metabolism of the neuropathological signature protein TDP-43
Huang, C., Bose, J. K., Majumder, P., Lee, K., Huang, J.-T. J., Huang, J. K., & Shen, C.-K. J. (2014) · Journal of Cell Science · doi:10.1242/jcs.136150 · Cited by 104 · see citing works
Crippa, V., Carra, S., Rusmini, P., Sau, D., Bolzoni, E., Bendotti, C., De Biasi, S., & Poletti, A. (2010) · Autophagy · doi:10.4161/auto.6.7.13042 · Cited by 101 · see citing works
Self-citationSeidel, K., Vinet, J., den Dunnen, W. F. A., Brunt, E. R. P., Meister, M., Boncoraglio, A., Zijlstra, M. P., Boddeke, H. W. G. M., Rüb, U., Kampinga, H. H., et al. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01198.x · Cited by 98 · see citing works
Self-citationMutant HSPB8 causes motor neuron-specific neurite degeneration
Irobi, J., Almeida-Souza, L., Asselbergh, B., Winter, V. D., Goethals, S., Dierick, I., Krishnan, J., Timmermans, J., Robberecht, W., Jonghe, P. D., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq234 · Cited by 92 · see citing works
Carra, S., Rusmini, P., Crippa, V., Giorgetti, E., Boncoraglio, A., Cristofani, R., Naujock, M., Meister, M., Minoia, M., Kampinga, H. H., et al. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0409 · Cited by 87 · see citing works
Self-citationAbnormal small heat shock protein interactions involving neuropathy‐associated HSP22 (HSPB8) mutants
Fontaine, J., Sun, X., Hoppe, A. D., Simon, S., Vicart, P., Michael J. Welsh, *., & Benndorf, R. (2006) · The FASEB Journal · doi:10.1096/fj.06-5911fje · Cited by 80 · see citing works
Carra, S., Crippa, V., Rusmini, P., Boncoraglio, A., Minoia, M., Giorgetti, E., Kampinga, H. H., & Poletti, A. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.009 · Cited by 76 · see citing works
Self-citationChen, L. X., & Schumacher, H. R. (2008) · JCR Journal of Clinical Rheumatology · doi:10.1097/rhu.0b013e3181896921 · Cited by 75 · see citing works
Dimitrakis, P., Romay-Ogando, M.-I., Timolati, F., Suter, T. M., & Zuppinger, C. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1475-8 · Cited by 73 · see citing works
Rusmini, P., Sau, D., Crippa, V., Palazzolo, I., Simonini, F., Onesto, E., Martini, L., & Poletti, A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.05.015 · Cited by 67 · see citing works
Self-citationDerrubone, an Inhibitor of the Hsp90 Protein Folding Machinery
Hadden, M. K., Galam, L., Gestwicki, J. E., Matts, R. L., & Blagg, B. S. J. (2007) · Journal of Natural Products · doi:10.1021/np070190s · Cited by 66 · see citing works
A Novel High Throughput Biochemical Assay to Evaluate the HuR Protein-RNA Complex Formation
D’Agostino, V., Adami, V., & Provenzani, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072426 · Cited by 66 · see citing works
Self-citationRusmini, P., Crippa, V., Giorgetti, E., Boncoraglio, A., Cristofani, R., Carra, S., & Poletti, A. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.026 · Cited by 64 · see citing works
Self-citationOnesto, E., Rusmini, P., Crippa, V., Ferri, N., Zito, A., Galbiati, M., & Poletti, A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07298.x · Cited by 63 · see citing works
Self-citationDifferential autophagy power in the spinal cord and muscle of transgenic ALS mice
Crippa, V., Boncoraglio, A., Galbiati, M., Aggarwal, T., Rusmini, P., Giorgetti, E., Cristofani, R., Carra, S., Pennuto, M., & Poletti, A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00234 · Cited by 63 · see citing works
Self-citationGregory, J. M., de Barros, T. P., Meehan, S., Dobson, C. M., & Luheshi, L. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031899 · Cited by 61 · see citing works
Kwok, A. W. S., Phadwal, K., Turner, B. J., Oliver, P. L., Raw, A., Simon, A. K., Talbot, K., & Agashe, V. R. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07521.x · Cited by 58 · see citing works
Silencing neuronal mutant androgen receptor in a mouse model of spinal and bulbar muscular atrophy
Sahashi, K., Katsuno, M., Hung, G., Adachi, H., Kondo, N., Nakatsuji, H., Tohnai, G., Iida, M., Bennett, C. F., & Sobue, G. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv300 · Cited by 57 · see citing works
Rusmini, P., Polanco, M. J., Cristofani, R., Cicardi, M. E., Meroni, M., Galbiati, M., Piccolella, M., Messi, E., Giorgetti, E., Lieberman, A. P., et al. (2015) · Scientific Reports · doi:10.1038/srep15174 · Cited by 56 · see citing works
Self-citationXiao, Y., Ma, C., Yi, J., Wu, S., Guo, L., Xu, X., Lin, P., Sun, J., & Zhou, J. (2015) · Physiological Reports · doi:10.14814/phy2.12271 · Cited by 56 · see citing works
Sun, X., Fontaine, J., Bartl, I., Behnam, B., Welsh, M. J., & Benndorf, R. (2007) · Cell Stress and Chaperones · doi:10.1379/csc-276.1 · Cited by 55 · see citing works
Dobrowolny, G., Aucello, M., Molinaro, M., & Musarò, A. (2008) · Neurological Research · doi:10.1179/174313208x281235 · Cited by 54 · see citing works
Proteasomal and autophagic degradative activities in spinal and bulbar muscular atrophy
Rusmini, P., Bolzoni, E., Crippa, V., Onesto, E., Sau, D., Galbiati, M., Piccolella, M., & Poletti, A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.06.016 · Cited by 48 · see citing works
Self-citationGiorgetti, E., Rusmini, P., Crippa, V., Cristofani, R., Boncoraglio, A., Cicardi, M. E., Galbiati, M., & Poletti, A. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu419 · Cited by 47 · see citing works
Self-citationRecovery of function in a myogenic mouse model of spinal bulbar muscular atrophy
Johansen, J. A., Yu, Z., Mo, K., Monks, D. A., Lieberman, A. P., Breedlove, S. M., & Jordan, C. L. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.12.009 · Cited by 47 · see citing works
The effect of colchicine on pyrin and pyrin interacting proteins
Taşkıran, E. Z., Çetinkaya, A., Balcı‐Peynircioğlu, B., Akkaya‐Ulum, Y. Z., & Yılmaz, E. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24231 · Cited by 44 · see citing works
Colchicine toxicity in renal patients – Are we paying attention?
Medani, S. A., & Wall, C. A. M. (2015) · Clinical Nephrology · doi:10.5414/cn108343 · Cited by 43 · see citing works
The Role of the Protein Quality Control System in SBMA
Rusmini, P., Crippa, V., Cristofani, R., Rinaldi, C., Cicardi, M. E., Galbiati, M., Carra, S., Malik, B. A., Greensmith, L., & Poletti, A. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0675-6 · Cited by 41 · see citing works
Self-citationALS-related misfolded protein management in motor neurons and muscle cells
Galbiati, M., Crippa, V., Rusmini, P., Cristofani, R., Cicardi, M. E., Giorgetti, E., Onesto, E., Messi, E., & Poletti, A. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.10.007 · Cited by 40 · see citing works
Self-citationMotoneuronal and muscle-selective removal of ALS-related misfolded proteins
Crippa, V., Galbiati, M., Boncoraglio, A., Rusmini, P., Onesto, E., Giorgetti, E., Cristofani, R., Zito, A., & Poletti, A. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130118 · Cited by 39 · see citing works
Self-citationHuguenard, A. L., Fernando, S. M., Monks, D. A., & Sengelaub, D. R. (2010) · Endocrinology · doi:10.1210/en.2010-1197 · Cited by 33 · see citing works
van der Velden, W. J. F. M., Huussen, J., Laak, H. T., & de Sévaux, R. G. L. (2008) · PubMed · Cited by 33 · see citing works
Ramírez-Rodríguez, G. B., Babu, H., Klempin, F., Krylyshkina, O., Baekelandt, V., Gijsbers, R., Debyser, Z., Overall, R. W., Nicola, Z., Fabel, K. S., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.6452-11.2013 · Cited by 30 · see citing works
Ramzan, F., McPhail, M. G., Rao, P., Mo, K., Halievski, K., Swift‐Gallant, A., Mendoza-Viveros, L., Cheng, H. M., & Monks, D. A. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3599-14.2015 · Cited by 29 · see citing works
Khalid, S., & Paul, S. (2014) · Medical Hypotheses · doi:10.1016/j.mehy.2014.04.013 · Cited by 29 · see citing works
Effects of proteasome inhibitor, MG132, on proteasome activity and oxidative status of rat liver
Alexandrova, A., Petrov, L., Georgieva, A. P., Kirkova, M., & Kukan, M. (2008) · Cell Biochemistry and Function · doi:10.1002/cbf.1459 · Cited by 25 · see citing works
Gültekin, N., & Küçükateş, E. (2014) · PubMed · Cited by 19 · see citing works
Androgen-dependent loss of muscle BDNF mRNA in two mouse models of SBMA
Halievski, K., Henley, C. L., Domino, L., Poort, J. E., Fu, M., Katsuno, M., Adachi, H., Sobue, G., Breedlove, S. M., & Jordan, C. L. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.04.013 · Cited by 18 · see citing works
Colchicine myoneuropathy in chronic renal failure patients with gout (Case Report)
Lai, I., CHENG, C., Chen, H.-H., Chen, W., & CHEN, P. (2006) · Nephrology · doi:10.1111/j.1440-1797.2006.00542.x · Cited by 17 · see citing works
Effects and Metabolism of Steroid Hormones in Human Neuroblastoma Cells
Maggi, R., Poletti, A., Casulari, L. A., Pimpinelli, F., Piva, F., ZANISI, M., & Martini, L. (1998) · Steroids · doi:10.1016/s0039-128x(98)00038-5 · Cited by 14 · see citing works
Self-citationOrsucci, D., Rocchi, A., Ienco, E. C., Alì, G., LoGerfo, A., Petrozzi, L., Scarpelli, M., Filosto, M., Carlesi, C., Siciliano, G., et al. (2014) · Current Molecular Medicine · doi:10.2174/1566524014666140603100131 · Cited by 11 · see citing works
The Small Heat Shock Protein HspB8: Role in Nervous System Physiology and Pathology
Vicario, M., Skaper, S. D., & Negro, A. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140711093344 · Cited by 11 · see citing works
Halievski, K., Mo, K., Westwood, J. T., & Monks, D. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118120 · Cited by 10 · see citing works
Taking the stress out of managing gout.
Laubscher, T. A., Dumont, Z. J., Regier, L. D., & Jensen, B. (2009) · PubMed Central · Cited by 6 · see citing works
Acewicz, A., Wierzba‐Bobrowicz, T., Lewandowska, E., Sienkiewicz‐Jarosz, H., Sułek, A., Antczak, J. M., Rakowicz, M. J., & Ryglewicz, D. (2015) · Clinical Neuropathology · doi:10.5414/np300829 · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Cortés, C. J., & Spada, A. R. L. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.012 · Cited by 197 · 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
“HSPB8 overexpression also enhances autophagic clearance of TARDBP via elevations in TFEB, SQSTM1, and LC3 [355,356].”
BackgroundSmall Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease
Webster, J. M., Darling, A. L., Uversky, V. N., & Blair, L. J. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01047 · Cited by 159 · see citing works
Autophagy in neurodegeneration: New insights underpinning therapy for neurological diseases
Corti, O., Blomgren, K., Poletti, A., & Beart, P. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15002 · Cited by 141 · see citing works
Self-citationSmall-molecule dissolution of stress granules by redox modulation benefits ALS models
Uechi, H., Sridharan, S., Nijssen, J., Bilstein, J., Iglesias‐Artola, J. M., Kishigami, S., Casablancas-Antràs, V., Poser, I., Martinez, E. J., Boczek, E. E., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01893-5 · Cited by 133 · see citing works
Heat-Shock Proteins in Neuroinflammation
Dukay, B., Csoboz, B., & Tóth, M. E. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00920 · Cited by 132 · see citing works
The chaperone-assisted selective autophagy complex dynamics and dysfunctions
Tedesco, B., Vendredy, L., Timmerman, V., & Poletti, A. (2023) · Autophagy · doi:10.1080/15548627.2022.2160564 · Cited by 130 · see citing works
Self-citationMolecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Tittelmeier, J., Nachman, E., & Nussbaum-Krammer, C. I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.581374 · Cited by 107 · see citing works
Cristofani, R., Crippa, V., Vezzoli, G., Rusmini, P., Galbiati, M., Cicardi, M. E., Meroni, M., Ferrari, V., Tedesco, B., Piccolella, M., et al. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0806-9 · Cited by 96 · see citing works
Self-citationSmall heat shock proteins in neurodegenerative diseases
Vendredy, L., Adriaenssens, E., & Timmerman, V. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01101-4 · Cited by 96 · see citing works
Crippa, V., Cicardi, M. E., Ramesh, N., Seguin, S. J., Ganassi, M., Bigi, I., Diacci, C., Zelotti, E., Baratashvili, M., Gregory, J. M., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw232 · Cited by 95 · see citing works
Self-citationAutophagy and Its Impact on Neurodegenerative Diseases: New Roles for TDP-43 and C9orf72
Budini, M., Buratti, E., Morselli, E., & Criollo, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00170 · Cited by 91 · see citing works
Molecular chaperones and Parkinson's disease
Hu, S., Tan, J., Qin, L., Lv, L., Yan, W., Zhang, H., Tang, B., & Wang, C. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105527 · Cited by 90 · see citing works
Quality Control of Membraneless Organelles
Alberti, S., & Carra, S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.013 · Cited by 89 · see citing works
Self-citationNeuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results
Sarparanta, J., Jonson, P. H., Kawan, S., & Udd, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041409 · Cited by 84 · see citing works
TDP-43 Promotes Neurodegeneration by Impairing Chromatin Remodeling
Berson, A., Sartoris, A., Nativio, R., Deerlin, V. M. V., Toledo, J. B., Porta, S., Liu, S., Chung, C., Garcia, B. A., Lee, V. M. ‐., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.024 · Cited by 83 · see citing works
Emerging Therapies and Novel Targets for TDP-43 Proteinopathy in ALS/FTD
Hayes, L. R., & Kaláb, P. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01260-5 · Cited by 81 · see citing works
Sever, B., Ciftci, H. I., DeMi̇rci̇, H., Sever, H., Ocak, F., Yuluğ, B., Tateishi, H., Tateishi, T., Otsuka, M., Fujita, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052400 · Cited by 78 · see citing works
Bouhy, D., Juneja, M., Katona, I., Holmgren, A., Asselbergh, B., Winter, V. D., Hochepied, T., Goosens, S., Haigh, J. J., Libert, C., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1756-0 · Cited by 77 · see citing works
Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases
Tedesco, B., Cristofani, R., Ferrari, V., Cozzi, M., Rusmini, P., Casarotto, E., Chierichetti, M., Mina, F., Galbiati, M., Piccolella, M., et al. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.842149 · Cited by 76 · see citing works
Self-citationCristofani, R., Crippa, V., Rusmini, P., Cicardi, M. E., Meroni, M., Licata, N. V., Sala, G., Giorgetti, E., Grunseich, C., Galbiati, M., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1308985 · Cited by 75 · see citing works
Self-citationMaintaining proteostasis under mechanical stress
Höhfeld, J., Benzing, T. R., Bloch, W., Fürst, D. O., Gehlert, S., Hesse, M., Hoffmann, B., Hoppe, T., Huesgen, P. F., Köhn, M., et al. (2021) · EMBO Reports · doi:10.15252/embr.202152507 · Cited by 72 · see citing works
Huang, C., Yan, S., & Zhang, Z. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00219-w · Cited by 71 · see citing works
Bodas, M., Patel, N., Silverberg, D., Walworth, K., & Vij, N. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6842 · Cited by 70 · see citing works
Cicardi, M. E., Cristofani, R., Rusmini, P., Meroni, M., Ferrari, V., Vezzoli, G., Tedesco, B., Piccolella, M., Messi, E., Galbiati, M., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-29658-2 · Cited by 70 · see citing works
Self-citationMandrioli, J., Crippa, V., Cereda, C., Bonetto, V., Zucchi, E., Gessani, A., Ceroni, M., Chiò, A., D’Amico, R., Monsurrò, M. R., et al. (2019) · BMJ Open · doi:10.1136/bmjopen-2018-028486 · Cited by 70 · see citing works
Self-citationRegulation of neuronal autophagy and the implications in neurodegenerative diseases
Cai, Q., & Ganesan, D. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105582 · Cited by 67 · see citing works
Ma, X., Mani, K. M., Liu, H., Kovács, A. D., Murphy, J. T., Foroughi, L., French, B. A., Weinheimer, C. J., Kraja, A. T., Benjamin, I. J., et al. (2019) · Journal of the American Heart Association · doi:10.1161/jaha.118.010866 · Cited by 65 · see citing works
Guilbert, S. M., Lambert, H., Rodrigue, M., Fuchs, M., Landry, J., & Lavoie, J. N. (2018) · The FASEB Journal · doi:10.1096/fj.201700558rr · Cited by 56 · see citing works
The Role of HSPB8, a Component of the Chaperone-Assisted Selective Autophagy Machinery, in Cancer
Cristofani, R., Piccolella, M., Crippa, V., Tedesco, B., Marelli, M. M., Poletti, A., & Moretti, R. M. (2021) · Cells · doi:10.3390/cells10020335 · Cited by 56 · see citing works
Self-citationThe small heat shock protein B8 (HSPB8) modulates proliferation and migration of breast cancer cells
Piccolella, M., Crippa, V., Cristofani, R., Rusmini, P., Galbiati, M., Cicardi, M. E., Meroni, M., Ferri, N., Morelli, F. F., Carra, S., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14422 · Cited by 53 · see citing works
Self-citationTherapeutic Approaches Targeting Protein Aggregation in Amyotrophic Lateral Sclerosis
Malik, R., & Wiedau‐Pazos, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00098 · Cited by 53 · see citing works
Targeting TDP‐43 proteinopathy with drugs and drug‐like small molecules
Buratti, E. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15148 · Cited by 50 · see citing works
Li, F., Yang, B., Li, T., Gong, X., Zhou, F., & Hu, Z. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14626 · Cited by 46 · see citing works
Neuroinflammation in Amyotrophic Lateral Sclerosis: Role of Redox (dys)Regulation
D’Ambrosi, N., Cozzolino, M., & Carrı̀, M. T. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7271 · Cited by 44 · see citing works
Small heat shock proteins in ageing and age-related diseases
Charmpilas, N., Kyriakakis, E., & Tavernarakis, N. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-016-0761-x · Cited by 43 · see citing works
Li, F., Tan, J., Zhou, F., Hu, Z., & Yang, B. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000492259 · Cited by 43 · see citing works
Nuclear Phospho-SOD1 Protects DNA from Oxidative Stress Damage in Amyotrophic Lateral Sclerosis
Bordoni, M., Pansarasa, O., Dell’Orco, M., Crippa, V., Gagliardi, S., Sproviero, D., Bernuzzi, S., Diamanti, L., Ceroni, M., Tedeschi, G., et al. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8050729 · Cited by 43 · see citing works
Self-citationAutophagy as an Emerging Common Pathomechanism in Inherited Peripheral Neuropathies
Haidar, M., & Timmerman, V. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00143 · Cited by 39 · see citing works
Advances in the role and mechanism of BAG3 in dilated cardiomyopathy
Liu, L., Sun, K., Zhang, X., Tang, Y., & Xu, D. (2019) · Heart Failure Reviews · doi:10.1007/s10741-019-09899-7 · Cited by 38 · see citing works
Pompa, A., Marchis, F. D., Pallotta, M. T., Benitez‐Alfonso, Y., Jones, A. M. E., Schipper, K., Moreau, K., Žárský, V., Sansebastiano, G. P. D., & Bellucci, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040703 · Cited by 37 · see citing works
Exploring the multifaceted roles of heat shock protein B8 (HSPB8) in diseases
Li, F., Xiao, H., Hu, Z., Zhou, F., & Yang, B. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.03.003 · Cited by 36 · see citing works
Praja1 RING ‐finger E3 ubiquitin ligase suppresses neuronal cytoplasmic TDP ‐43 aggregate formation
Watabe, K., Kato, Y., Sakuma, M., Murata, M., Niida‐Kawaguchi, M., Takemura, T., Hanagata, N., Tada, M., Kakita, A., & Shibata, N. (2020) · Neuropathology · doi:10.1111/neup.12694 · Cited by 36 · see citing works
Filareti, M., Luotti, S., Pasetto, L., Pignataro, M., Paolella, K., Messina, P., Pupillo, E., Filosto, M., Lunetta, C., Mandrioli, J., et al. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00099 · Cited by 36 · see citing works
Cristofani, R., Rusmini, P., Galbiati, M., Cicardi, M. E., Ferrari, V., Tedesco, B., Casarotto, E., Chierichetti, M., Messi, E., Piccolella, M., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00796 · Cited by 35 · see citing works
Self-citationProteostasis in neurodegenerative diseases
Kinger, S., Jagtap, Y. A., Kumar, P., Choudhary, A., Prasad, A., Prajapati, V. K., Kumar, A., Mehta, G., & Mishra, A. (2024) · Advances in clinical chemistry · doi:10.1016/bs.acc.2024.04.002 · Cited by 33 · see citing works
Verde, E. M., Secco, V., Ghezzi, A., Mandrioli, J., & Carra, S. (2025) · Cells · doi:10.3390/cells14100680 · Cited by 32 · see citing works
Self-citationYao, J., Chen, Y., Nguyen, D. T., Thompson, Z., Eroshkin, A. M., Nerlakanti, N., Patel, A. K., Agarwal, N., Teer, J. K., Dhillon, J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-46064-4 · Cited by 32 · see citing works
Modifiers of GRN -Associated Frontotemporal Lobar Degeneration
Wauters, E., Mossevelde, S. V., van der Zee, J., Cruts, M., & Broeckhoven, C. V. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.004 · Cited by 32 · see citing works
Autophagy and lysosomal pathways in nervous system disorders
Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 31 · see citing works
Licata, N. V., Cristofani, R., Salomonsson, S. E., Wilson, K. M., Kempthorne, L., Vaizoglu, D., D’Agostino, V., Pollini, D., Loffredo, R., Pancher, M., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020105026 · Cited by 29 · see citing works
Self-citationTargeting common disease pathomechanisms to treat amyotrophic lateral sclerosis
Faller, K. M. E., Chaytow, H., & Gillingwater, T. H. (2025) · Nature Reviews Neurology · doi:10.1038/s41582-024-01049-4 · Cited by 28 · see citing works
Casarotto, E., Sproviero, D., Corridori, E., Gagliani, M. C., Cozzi, M., Chierichetti, M., Cristofani, R., Ferrari, V., Galbiati, M., Mina, F., et al. (2022) · Cells · doi:10.3390/cells11030516 · Cited by 27 · see citing works
Self-citationPotential application of heat shock proteins as therapeutic targets in Parkinson's disease
Guo, H., Yi, J., Wang, F., Lei, T., & Du, H. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105453 · Cited by 26 · see citing works
Roles of Stress Response in Autophagy Processes and Aging-Related Diseases
Watanabe, Y., Taguchi, K., & Tanaka, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813804 · Cited by 26 · see citing works
Qu, Z., Titus, A. S. C. L. S., Xuan, Z., & D’Mello, S. R. (2018) · Scientific Reports · doi:10.1038/s41598-018-35610-1 · Cited by 26 · see citing works
A novel microtubule inhibitor promotes tumor ferroptosis by attenuating SLC7A11/GPX4 signaling
Ning, N., Shang, Z., Liu, Z., Xia, Z., Li, Y., Ren, R., Wang, H., & Zhang, Y. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01713-6 · Cited by 25 · see citing works
Ho, P., Hsieh, T., & Tsai, K. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102441 · Cited by 25 · see citing works
Molecular Chaperones’ Potential against Defective Proteostasis of Amyotrophic Lateral Sclerosis
Kinger, S., Dubey, A. R., Kumar, P., Jagtap, Y. A., Choudhary, A., Kumar, A., Prajapati, V. K., Dhiman, R., & Mishra, A. (2023) · Cells · doi:10.3390/cells12091302 · Cited by 24 · see citing works
Sun, J.-T., Cheng, G.-X., Huang, L.-J., Liu, S., Ali, M., Khan, A., Yu, Q., Yang, S., Luo, D.-X., & Gong, Z. (2019) · Scientia Horticulturae · doi:10.1016/j.scienta.2019.02.008 · Cited by 24 · see citing works
A Crucial Role for the Protein Quality Control System in Motor Neuron Diseases
Cristofani, R., Crippa, V., Cicardi, M. E., Tedesco, B., Ferrari, V., Chierichetti, M., Casarotto, E., Piccolella, M., Messi, E., Galbiati, M., et al. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00191 · Cited by 22 · see citing works
Self-citationIn a search for efficient treatment for amyotrophic lateral sclerosis: Old drugs for new approaches
Kukharsky, M. S., Skvortsova, V. I., Бачурин, С. О., & Buchman, V. L. (2020) · Medicinal Research Reviews · doi:10.1002/med.21725 · Cited by 21 · see citing works
Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles
Albinhassan, T. H., Alharbi, B. M., AlSuhaibani, E. S., Mohammad, S., & Malik, S. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26041525 · Cited by 19 · see citing works
The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases
Tedesco, B., Ferrari, V., Cozzi, M., Chierichetti, M., Casarotto, E., Pramaggiore, P., Mina, F., Galbiati, M., Rusmini, P., Crippa, V., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911759 · Cited by 19 · see citing works
Self-citationFan, B., Sun, Y., Liu, S.-Y., Che, L., & Li, G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010201 · Cited by 18 · see citing works
Bonavita, R., Scerra, G., Martino, R. D., Nuzzo, S., Polishchuk, E., Gennaro, M. D., Williams, S. V., Caporaso, M. G., Caiazza, C., Polishchuk, R., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad047 · Cited by 18 · see citing works
Small heat shock proteins and neurodegeneration: recent developments
Kourtis, N., & Tavernarakis, N. (2018) · BioMolecular Concepts · doi:10.1515/bmc-2018-0009 · Cited by 17 · see citing works
Targeted Profiling of Heat Shock Proteome in Radioresistant Breast Cancer Cells
Miao, W., Fan, M., Huang, M., Li, J. J., & Wang, Y. (2018) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00330 · Cited by 16 · see citing works
Seo, E., Klauck, S. M., Efferth, T., & Panossian, A. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.11.011 · Cited by 14 · see citing works
Chierichetti, M., Cerretani, M., Ciammaichella, A., Crippa, V., Rusmini, P., Ferrari, V., Tedesco, B., Casarotto, E., Cozzi, M., Mina, F., et al. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121323 · Cited by 13 · see citing works
Self-citationEmerging clinical investigational drugs for the treatment of amyotrophic lateral sclerosis
Martínez‐González, L., & Martı́nez, A. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2178416 · Cited by 12 · see citing works
Emerging Drugs for the Treatment of Amyotrophic Lateral Sclerosis: A Focus on Recent Phase 2 Trials
Barp, A., Gerardi, F., Lizio, A., Sansone, V., & Lunetta, C. (2020) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2020.1769067 · Cited by 12 · see citing works
Zhu, Y., Zhang, Y., Fan, Z., Fang, Y., Zheng, Y., Li, Y., Yang, M. G., Guo, C., Li, Y., Zhou, X., et al. (2022) · Small · doi:10.1002/smll.202204310 · Cited by 12 · see citing works
Olivé, M., Winter, L., Fürst, D. O., Schröder, R., Béhin, A., Breukel, A. I. M., Brumhard, M., Bryson‐Richardson, R. J., Claeys, K. G., Ferreiro, A., et al. (2020) · Neuromuscular Disorders · doi:10.1016/j.nmd.2020.11.003 · Cited by 11 · see citing works
Ojaimi, Y. A., Dangoumau, A., Alarcan, H., Hergesheimer, R. C., Vourc’h, P., Corcia, P., Lanznaster, D., & Blasco, H. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2083958 · Cited by 10 · see citing works
Gianferrari, G., Costantini, R. C., Crippa, V., Carra, S., Bonetto, V., Pansarasa, O., Cereda, C., Zucchi, E., Martinelli, I., Simonini, C., et al. (2024) · Brain Communications · doi:10.1093/braincomms/fcae304 · Cited by 10 · see citing works
Self-citationChierichetti, M., Cristofani, R., Crippa, V., Ferrari, V., Cozzi, M., Casarotto, E., Pramaggiore, P., Cornaggia, L., Patelli, G., Mohamed, A. A., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00517 · Cited by 10 · see citing works
Self-citationDiaz, J. R., Martá-Ariza, M., Khodadadi‐Jamayran, A., Heguy, A., Tsirigos, A., Pankiewicz, J. E., Sullivan, P. M., & Sadowski, M. J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.845291 · Cited by 10 · see citing works
The Spectrum of Small Heat Shock Protein B8 (HSPB8)-Associated Neuromuscular Disorders
Rashed, H. R., Nath, S. R., & Milone, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26072905 · Cited by 8 · see citing works
Bonavita, R., Vitale, F., Verdicchio, L. V., Williams, S. V., Caporaso, M. G., Fleming, A., & Renna, M. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1538377 · Cited by 8 · see citing works
The role of autophagy-lysosomal pathway in motor neuron diseases
Tedesco, B., Ferrari, V., Cozzi, M., Chierichetti, M., Casarotto, E., Pramaggiore, P., Mina, F., Piccolella, M., Cristofani, R., Crippa, V., et al. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220778 · Cited by 8 · see citing works
Self-citationTargeting Protein Aggregation in ALS
Perni, M., & Mannini, B. (2024) · Biomolecules · doi:10.3390/biom14101324 · Cited by 7 · see citing works
Wen, J., Li, Y., Qin, Y., Yan, L., Zhang, K., Li, A., Wang, Z., Yu, F., Lai, J., Yang, W., et al. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107518 · Cited by 7 · see citing works
Kuczmarski, T. M., Stommel, E. W., Riley, K., Tandan, R., Chaudhry, V., Clawson, L., Caller, T. A., Henegan, P. L., Facciponte, D. N., Bradley, W. G., et al. (2017) · Journal of Neurology · doi:10.1007/s00415-017-8564-2 · Cited by 6 · see citing works
Unlocking Disease‐Modifying Treatments for TDP‐43‐Mediated Neurodegeneration
Gil, R. S., & Walker, A. K. (2025) · BioEssays · doi:10.1002/bies.202400257 · Cited by 5 · see citing works
Heat increases full-length SMN splicing: promise for splice-augmenting therapies for SMA
Dominguez, C. E., Cunningham, D., Venkataramany, A. S., & Chandler, D. S. (2022) · Human Genetics · doi:10.1007/s00439-021-02408-7 · Cited by 5 · see citing works
Universal Adapter Protein Bag3 and Small Heat Shock Proteins
Zamotina, M. A., Muranova, L. K., Zabolotskii, A. I., Tyurin‐Kuzmin, P. A., Kulebyakin, K. Y., & Gusev, N. B. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924090013 · Cited by 4 · see citing works
A chemogenomic approach is required for effective treatment of amyotrophic lateral sclerosis
Pampalakis, G., Angelis, G., Zingkou, E., Vekrellis, K., & Sotiropoulou, G. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.657 · Cited by 4 · see citing works
Diseases of Motor Neurons and Neuromuscular Junctions
Sontheimer, H. W. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821228-8.00006-8 · Cited by 3 · see citing works
Bayraktar, A., Önal-Süzek, T., Süzek, B. E., & Baysal, Ö. (2019) · arXiv (Cornell University) · doi:10.48550/arxiv.1909.07469 · Cited by 2 · see citing works
Vendredy, L., Winter, V. D., Lent, J. V., Orije, J. E. M. J., Authier, T. D. S., Katona, I., Asselbergh, B., Adriaenssens, E., Weis, J., Verhoye, M., et al. (2025) · The Journal of Gene Medicine · doi:10.1002/jgm.70013 · Cited by 2 · see citing works
Rest Induces a Distinct Transcriptional Program in the Nervous System of the Exercised L. stagnalis
Rozenberg, J. M., Boguslavsky, D., Chistopolsky, I. A., Zakharov, I., & Dyakonova, V. E. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146970 · Cited by 2 · see citing works
Diseases of Motor Neurons and Neuromuscular Junctions
Sontheimer, H. W. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800244-5.00006-9 · Cited by 2 · see citing works
Immunotherapy for Neurodegenerative Movement Disorders
Mosley, R. L., Saleh, M., & Olson, K. E. (2024) · Springer eBooks · doi:10.1007/978-3-031-68237-7_52 · Cited by 1 · see citing works
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 · see citing works
THE PHYSIOPATHOLOGICAL ROLES OF ANDROGENS IN MOTONEURONS
Poletti, A. (2020) · Istituto Lombardo - Accademia di Scienze e Lettere - Incontri di Studio · doi:10.4081/incontri.2019.607
Self-citationMolecular Mechanisms Underlying the Role of HSPB8 in Neurodegeneration
Patil, R., Wankhede, N. L., Upaganlawar, A. B., & Ingale, S. P. (2022) · Springer eBooks · doi:10.1007/978-981-16-7606-2_8
Zhou, W., Marchesi, V., McLeod, M., Kordala, A. J., Szwec, S., Mielcarz, J. A., Poletti, A., & Tedesco, B. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168244
Self-citationAmin, Z., & Chugh, J. (2026) · Research Square · doi:10.21203/rs.3.rs-9968919/v1
- Authors
- Crippa, V., D’Agostino, V. G., Cristofani, R., Rusmini, P., Cicardi, M. E., Messi, E., Loffredo, R., Pancher, M., Piccolella, M., Galbiati, M., Meroni, M., Cereda, C., Carra, S., Provenzani, A., & Poletti, A.
- Affiliations
- Fondazione Istituto Neurologico Nazionale Casimiro Mondino (IT)
- University of Trento (IT)
- University of Milan (IT)
- University of Modena and Reggio Emilia (IT)
- Corresponding author
- Poletti, Angelo
- ORCID
- Venue
- Scientific Reports
- Published
- 2016-03-10
- Volume
- 6
- Issue
- 1
- Pages
- 22827-22827
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC4785366
- OpenAlex
- W2296135919
- Cited by
- 101
- References
- 87
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 8 · 2023: 6 · 2022: 14 · 2021: 7 · 2020: 13 · 2019: 11 · 2018: 13 · 2017: 14 · 2016: 2 · 2015: 1
- FWCI
- 6.93
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- IRIS UNIMORE (University of Modena and Reggio Emilia) (submittedVersion, cc-by)
- Institutional Research Information System (Università degli Studi di Trento) (submittedVersion, cc-by)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
- Funders
- Università degli Studi di Milano
- EU Joint Programme – Neurodegenerative Disease Research
- Fondazione Telethon (GGP14039)
- Fondazione Cariplo (GGP14039, 2014-0686)
- Ministero della Salute (GR-2011-02347198)
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Regione Lombardia
- Hsinchu Science Park Bureau, Ministry of Science and Technology, Taiwan
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- HSPB8, TDP-43, amyotrophic lateral sclerosis, motor neuron disease, neurodegeneration, misfolded protein clearance, autophagy, BAG3, colchicine, doxorubicin, TFEB, p62, LC3, small molecule screening, transcriptional induction
- MeSH terms
- Amyotrophic Lateral Sclerosis, Animals, Autophagy, Cell Line, Colchicine, DNA-Binding Proteins, Doxorubicin, Heat-Shock Proteins, Humans, Motor Neurons, Peptide Fragments, Transcription, Genetic, Protein Serine-Threonine Kinases, Protein Folding, Molecular Chaperones, Heat-Shock Response, Mice, High-Throughput Screening Assays, Frontotemporal Dementia
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