nELAV Proteins Alteration in Alzheimer's Disease Brain: A Novel Putative Target for Amyloid-β Reverberating on AβPP Processing
Open accessAbstract
Neuronal ELAV (nELAV) proteins are RNA-binding proteins which play a physiological role in controlling gene expression in memory formation, and their alteration may contribute to cognitive impairment associated with neurodegenerative pathologies such as Alzheimer's disease (AD). Indeed, we found that the content of nELAV proteins is significantly decreased along with clinical dementia progression in the hippocampi of AD brains, where it inversely correlates with the amount of amyloid-beta (Abeta). To check the direct influence of Abeta on nELAV, we performed in vitro experiments using human SH-SY5Y cells, finding that Abeta(1-42) specifically determines nELAV proteins reduction. Since ADAM10 mRNA has the predicted sequences targeted by nELAV, we investigated whether Abeta, through nELAV proteins, could originate a vicious circle affecting amyloid-beta protein precursor (AbetaPP) processing. Immunoprecipitation experiments showed that indeed nELAV proteins bind to ADAM10 mRNA and that this binding is disrupted by Abeta(1-42) exposure, resulting in a decreased ADAM10 protein expression. ADAM10 protein diminution was also found in AD hippocampi. These data show for the first time the involvement of nELAV in AD pathology and suggest that their alteration may affect genes implicated in AbetaPP processing.
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?
In the hippocampus of AD patients, nELAV protein abundance decreases in parallel with clinical dementia progression, and their expression is inversely correlated with Aβ peptide levels both in vitro and in vivo.
“In the hippocampus of AD patients, nELAV protein abundance was found to decrease in parallel with clinical dementia progression, and their expression was inversely correlated with Aβ peptide levels both in vitro and in vivo (Amadio et al. 2009).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Amadio et al. 2009
The Results section, “The nELAV are decreased in postmortem AD patients” (page unavailable), reports that hippocampal nELAV levels fell with dementia progression and were inversely correlated with hippocampal Aβ content. The Results section, “Aβ intracellular accumulation induces a reduction of nELAV in SH-SY5Y cells” (page unavailable), reports that Aβ exposure reduced nELAV in vitro, but does not establish an inverse correlation between their measured levels in vitro. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe interaction between nELAV proteins and ADAM10 mRNA is disrupted following exposure to Aβ1-42 leading to reduced ADAM10 protein levels.
“The authors also determined that the interaction between nELAV proteins and ADAM10 mRNA was disrupted following exposure to Aβ1–42 leading to reduced ADAM10 protein levels (Amadio et al. 2009).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Amadio et al. 2009
The Results report that Aβ1–42 exposure disrupted detectable nELAV–ADAM10 mRNA binding and reduced ADAM10 protein levels. The Discussion says the reduced protein expression may result from disrupted binding, but notes that post-translational effects cannot be excluded. Thus, the causal link implied by “leading to” is stronger than the paper establishes (page numbers not supplied). (LLM, conf=0.86)
Experimental — accuracy not yet measurednELAVs have recently been linked to Alzheimer's disease.
“In accordance with its direct or indirect function in learning and memory, nELAVs have recently been linked to Alzheimer’s disease (AD), a condition characterized by neuronal death, memory loss and eventual dementia.”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Amadio et al. 2009
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
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1× · see citing works
“The Aβ oligomers, which have been reported to be the most pathological aggregation form of Aβ, are able to impair cognitive function [27], to inhibit long-term potentiation [28], and to disrupt memory in transgenic mouse models [29].”
RetractedAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022 · see citing works
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942 · see citing works
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,677 · see citing works
Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., & LaFerla, F. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.040 · Cited by 1,294 · see citing works
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 1× · see citing works
“Hippocampal samples were treated according to a previous published method [12].”
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991 · see citing works
Self-citationMattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I. M., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 795 · see citing works
Clinical Dementia Rating (CDR)
Gauthier, S. G. (2001) · CRC Press eBooks · doi:10.3109/9780203213896-34 · Cited by 696 · see citing works
RNA-binding protein HuR enhances p53 translation in response to ultraviolet light irradiation
Mazan-Mamczarz, K., Galbán, S., de Silanes, I. L., Martindale, J. L., Atasoy, U., Keene, J. D., & Gorospe, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1432104100 · Cited by 445 · see citing works
ADAMs family members as amyloid precursor protein α‐secretases
Allinson, T. M. J., Parkin, E. T., Turner, A. J., & Hooper, N. M. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10737 · Cited by 441 · see citing works
The role of cerebral amyloid accumulation in common forms of Alzheimer disease
Gandy, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25100 · Cited by 394 · see citing works
Self-citationTherapeutic effects of PKC activators in Alzheimer's disease transgenic mice
Etcheberrigaray, R., Tan, M., Dewachter, I., Kuipéri, C., der Auwera, I. V., Wera, S., Qiao, L., Bank, B., Nelson, T. J., Kozikowski, A. P., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403921101 · Cited by 343 · see citing works
Why is Hu where? Shuttling of early-response-gene messenger RNA subsets
Keene, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.5 · Cited by 294 · see citing works
Haroutunian, V. (1998) · Archives of Neurology · doi:10.1001/archneur.55.9.1185 · Cited by 289 · see citing works
Self-citationThe role of Aβ42 in Alzheimer's disease
Younkin, S. G. (1998) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(98)80035-1 · Cited by 282 · see citing works
Intraneuronal Aβ-Amyloid Precedes Development of Amyloid Plaques in Down Syndrome
Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E., & Troncoso, J. C. (2001) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2001-125-0489-iaapdo · Cited by 248 · see citing works
α-Secretase ADAM10 as Well as αAPPs Is Reduced in Platelets and CSF of Alzheimer Disease Patients
Colciaghi, F., Borroni, B., Pastorino, L., Marcello, E. E., Zimmermann, M., Cattabeni, F., Padovani, A., & Luca, M. D. (2002) · Molecular Medicine · doi:10.1007/bf03402076 · Cited by 246 · see citing works
Antic, D., Lu, N., & Keene, J. D. (1999) · Genes & Development · doi:10.1101/gad.13.4.449 · Cited by 202 · see citing works
Neurofibrillary tangles in nondemented elderly subjects and mild Alzheimer disease
Haroutunian, V., Purohit, D. P., Perl, D. P., Marin, D., Khan, K., Lantz, M., Davis, K. L., & Mohs, R. C. (1999) · Archives of Neurology · doi:10.1001/archneur.56.6.713 · Cited by 201 · see citing works
Self-citationJain, R. G., Andrews, L. G., McGowan, K. M., Pekala, P. H., & Keene, J. D. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.2.954 · Cited by 199 · see citing works
Role of HuD and other RNA‐binding proteins in neural development and plasticity
Perrone‐Bizzozero, N. I., & Bolognani, F. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10175 · Cited by 186 · see citing works
Pascale, A., Gusev, P. A., Amadio, M., Dottorini, T., Govoni, S., Alkon, D. L., & Quattrone, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307674100 · Cited by 174 · see citing works
Self-citationDefining a neuron: neuronal ELAV proteins
Pascale, A., Amadio, M., & Quattrone, A. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7017-y · Cited by 158 · see citing works
Self-citationJansen, R. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.3.455 · Cited by 150 · see citing works
Quattrone, A., Pascale, A., Nogues, X., Zhao, W., Gusev, P., Pacini, A., & Alkon, D. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191388398 · Cited by 137 · see citing works
Self-citationAntic, D., & Keene, J. D. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.2.183 · Cited by 134 · see citing works
Neuronal ELAV proteins enhance mRNA stability by a PKCα-dependent pathway
Pascale, A., Amadio, M., Scapagnini, G., Lanni, C., Racchi, M., Provenzani, A., Govoni, S., Alkon, D. L., & Quattrone, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504702102 · Cited by 129 · see citing works
Self-citationNeurotrophic and Neuroprotective Effects of hAPP in Transgenic Micea
Mucke, L., Abraham, C. R., & Masliah, E. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34405.x · Cited by 87 · see citing works
Pascale, A., Fortino, I., Govoni, S. M., Trabucchi, M., Wetsel, W. C., & Battaini, F. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67062471.x · Cited by 86 · see citing works
Self-citationBolognani, F., Merhege, M. A., Twiss, J., & Perrone-Bizzozero, N. I. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.08.074 · Cited by 68 · see citing works
The pharmacology of amyloid precursor protein processing
Racchi, M. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00158-4 · Cited by 62 · see citing works
Self-citation
Flagged first, then by citations
1 of the 35 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The Impact of Disease Comorbidities in Alzheimer’s Disease
Santiago, J. A., & Potashkin, J. A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.631770 · Cited by 259 · 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
GAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases
Chung, D., Shum, A. K., & Caraveo, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.567537 · Cited by 203 · see citing works
Viiri, J., Amadio, M., Marchesi, N., Hyttinen, J. M. T., Kivinen, N., Sironen, R. K., Rilla, K. J., Akhtar, S., Provenzani, A., D’Agostino, V., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069563 · Cited by 158 · see citing works
Self-citationScheckel, C., Drapeau, E., Frias, M. A., Park, C. Y., Fak, J., Zucker-Scharff, I., Kou, Y., Haroutunian, V., Ma'ayan, A., Buxbaum, J. D., et al. (2016) · eLife · doi:10.7554/elife.10421 · Cited by 139 · see citing works
Self-citationBronicki, L. M., & Jasmin, B. J. (2013) · RNA · doi:10.1261/rna.039164.113 · Cited by 126 · see citing works
miR-375 Inhibits Differentiation of Neurites by Lowering HuD Levels
Abdelmohsen, K., Hutchison, E. R., Lee, E. K., Kuwano, Y., Kim, M. M., Masuda, K., Srikantan, S., Subaran, S. S., Marasa, B. S., Mattson, M. P., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00316-10 · Cited by 134 · see citing works
Moncini, S., Lunghi, M., Valmadre, A., Grasso, M., Vescovo, V. D., Riva, P., Denti, M. A., & Venturin, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0002-4 · Cited by 93 · see citing works
Endres, K., & Deller, T. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00056 · Cited by 92 · see citing works
Pascale, A., & Govoni, S. M. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0810-7 · Cited by 88 · see citing works
Self-citationElavl3 is essential for the maintenance of Purkinje neuron axons
Ogawa, Y., Kakumoto, K., Yoshida, T., Kuwako, K.-I., Miyazaki, T., Yamaguchi, J., Konno, A., Hata, J., Uchiyama, Y., Hirai, H., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21130-5 · Cited by 77 · see citing works
Ravanidis, S., Kattan, F.-G., & Doxakis, E. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082280 · Cited by 65 · see citing works
Marchesi, N., Osera, C., Fassina, L., Amadio, M., Angeletti, F., Morini, M., Magenes, G., Venturini, L., Biggiogera, M., Ricevuti, G., et al. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24631 · Cited by 62 · see citing works
Self-citationmiR-129-5p: A key factor and therapeutic target in amyotrophic lateral sclerosis
Loffreda, A., Nizzardo, M., Arosio, A., Ruepp, M., Calogero, R., Volinia, S., Galasso, M., Bendotti, C., Ferrarese, C., Lunetta, C., et al. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101803 · Cited by 58 · see citing works
Talman, V., Pascale, A., Jäntti, M., Amadio, M., & Tuominen, R. (2016) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12581 · Cited by 56 · see citing works
Self-citationRole of HuD in nervous system function and pathology
Perrone‐Bizzozero, N. I. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s389 · Cited by 52 · see citing works
RNA-binding proteins as molecular links between cancer and neurodegeneration
Campos‐Melo, D., Droppelmann, C. A., Volkening, K., & Strong, M. J. (2014) · Biogerontology · doi:10.1007/s10522-014-9531-2 · Cited by 49 · see citing works
Osera, C., Fassina, L., Amadio, M., Venturini, L., Buoso, E., Magenes, G., Govoni, S. M., Ricevuti, G., & Pascale, A. (2011) · Tissue Engineering Part A · doi:10.1089/ten.tea.2011.0071 · Cited by 45 · see citing works
Self-citationMilani, P., Amadio, M., Laforenza, U., Dell’Orco, M., Diamanti, L., Sardone, V., Gagliardi, S., Govoni, S. M., Ceroni, M., Pascale, A., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.08.005 · Cited by 43 · see citing works
Self-citationWeighted Protein Interaction Network Analysis of Frontotemporal Dementia
Ferrari, R., Lovering, R. C., Hardy, J., Lewis, P. A., & Manzoni, C. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00934 · Cited by 42 · see citing works
Subhadra, B. G., Schaller, K., & Seeds, N. W. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.08.010 · Cited by 40 · see citing works
van der Linden, R. J., Gerritsen, J. S., Liao, M., Widomska, J., Pearse, R. V., White, F. M., Franke, B., Young‐Pearse, T. L., & Poelmans, G. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102316 · Cited by 40 · see citing works
RNA–Binding Protein HuD as a Versatile Factor in Neuronal and Non–Neuronal Systems
Jung, M., & Lee, E. K. (2021) · Biology · doi:10.3390/biology10050361 · Cited by 39 · see citing works
RNA binding proteins in senescence: A potential common linker for age-related diseases?
Varesi, A., Campagnoli, L. I. M., Barbieri, A., Rossi, L., Ricevuti, G., Esposito, C., Chirumbolo, S., Marchesi, N., & Pascale, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101958 · Cited by 28 · see citing works
Self-citationCopper, endoproteolytic processing of the prion protein and cell signalling
Haigh, C. L. (2010) · Frontiers in bioscience · doi:10.2741/3663 · Cited by 29 · see citing works
Emerging Roles for the RNA-Binding Protein HuD (ELAVL4) in Nervous System Diseases
Silvestri, B., Mochi, M., Garone, M. G., & Rosa, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314606 · Cited by 28 · see citing works
Dell’Orco, M., Sardone, V., Gardiner, A. S., Pansarasa, O., Bordoni, M., Perrone‐Bizzozero, N. I., & Cereda, C. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105211 · Cited by 26 · see citing works
Fragkouli, A., Koukouraki, P., Vlachos, I. S., Paraskevopoulou, M. D., Hatzigeorgiou, A. G., & Doxakis, E. (2017) · Scientific Reports · doi:10.1038/srep44507 · Cited by 27 · see citing works
Nasti, R., Rossi, D., Amadio, M., Pascale, A., Ünver, M. Y., Hirsch, A. K. H., & Collina, S. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01871 · Cited by 27 · see citing works
Self-citationLi, S., Weinstein, G., Zare, H., Teumer, A., Völker, U., Friedrich, N., Knol, M. J., Satizábal, C. L., Petyuk, V., Adams, H. H. H., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa176 · Cited by 26 · see citing works
Lim, C. S., & Alkon, D. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097756 · Cited by 24 · see citing works
Masi, M., Biundo, F., Fiou, A., Racchi, M., Pascale, A., & Buoso, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076639 · Cited by 20 · see citing works
Self-citationAmadio, M., Osera, C., Lupo, G., Motta, C., Drago, F., Govoni, S. M., & Pascale, A. (2012) · Europe PMC (PubMed Central) · Cited by 22 · see citing works
Self-citationEvaluation of the Common Molecular Basis in Alzheimer’s and Parkinson’s Diseases
Rana, P., Franco, E. F., Rao, Y., Syed, K., Barh, D., Azevedo, V., Ramos, R. T. J., & Ghosh, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153730 · Cited by 20 · see citing works
Rossi, D., Amadio, M., Baraglia, A. C., Azzolina, O., Ratti, A., Govoni, S. M., Pascale, A., & Collina, S. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900741e · Cited by 20 · see citing works
Self-citationDell’Orco, M., Elyaderani, A., Vannan, A., Sekar, S., Powell, G. L., Liang, W. S., Neisewander, J. L., & Perrone‐Bizzozero, N. I. (2021) · Biology · doi:10.3390/biology10090939 · Cited by 15 · see citing works
Trans-acting factors governing acetylcholinesterase mRNA metabolism in neurons
Bronicki, L., & Jasmin, B. J. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00036 · Cited by 14 · see citing works
Li, J., Chen, F., Zhang, Q., Meng, X., Yao, X., Risacher, S. L., Yan, J., Saykin, A. J., Liang, H., & Shen, L. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191121142558 · Cited by 14 · see citing works
Regulation of mRNA stability by ARE-binding proteins in synaptic plasticity and memory
Lee, Y., Lee, J., & Kaang, B. (2015) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2015.08.004 · Cited by 14 · see citing works
Vasile, F., Rossi, D., Collina, S., & Potenza, D. (2014) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201403014 · Cited by 14 · see citing works
Libard, S., Laurell, K., Cesarini, K. G., & Alafuzoff, I. I. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170446 · Cited by 14 · see citing works
Involvement of ELAV RNA-binding proteins in the post-transcriptional regulation of HO-1
Amadio, M., Scapagnini, G., Davinelli, S., Calabrese, V., Govoni, S. M., & Pascale, A. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00459 · Cited by 14 · see citing works
Self-citationBronicki, L., Bélanger, G., & Jasmin, B. J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2247-12.2012 · Cited by 13 · see citing works
PKC Activation Counteracts ADAM10 Deficit in HuD-Silenced Neuroblastoma Cells
Marchesi, N., Amadio, M., Colombrita, C., Govoni, S. M., Ratti, A., & Pascale, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160299 · Cited by 12 · see citing works
Self-citationThe role of autophagy in age‐related macular degeneration
Kivinen, N. (2018) · Acta Ophthalmologica · doi:10.1111/aos.13753 · Cited by 12 · see citing works
YRNAs: biosynthesis, structure, functions and involvment in cancer development
Campo, A., Aliquò, F., Velletri, T., & Campo, S. (2025) · Discover Oncology · doi:10.1007/s12672-025-01957-x · Cited by 11 · see citing works
Zuccotti, P., Colombrita, C., Moncini, S., Barbieri, A., Lunghi, M., Gelfi, C., Palma, S. D., Nicolin, A., Ratti, A., Venturin, M., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.04.018 · Cited by 11 · see citing works
Aplysia Neurons as a Model of Alzheimer’s Disease: Shared Genes and Differential Expression
Kron, N. S., & Fieber, L. A. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-021-01918-3 · Cited by 10 · see citing works
Murakami, K., Yoshimura, M., Nakagawa, S., Kume, T., Kondo, T., Inoue, H., & Irie, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041179 · Cited by 10 · see citing works
Modulation of Gene Expression by RNA Binding Proteins: mRNA Stability and Translation
Abdelmohsen, K. (2012) · InTech eBooks · doi:10.5772/48485 · Cited by 10 · see citing works
Bae, J. E., Park, S. J., Hong, Y., Jo, D. S., Lee, H., Park, N. Y., Kim, J. B., Park, H. J., Bunch, H., Chang, J. H., et al. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.06.091 · Cited by 9 · see citing works
Dorta, S., Alexandre-Silva, V., Popolin, C. P., de Sousa, D. B., Grigoli, M. M., Pelegrini, L. N. D. C., Manzine, P. R., Camins, A., Marcello, E. E., Endres, K., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102464 · Cited by 9 · see citing works
Ambrosio, F. A., Coricello, A., Costa, G., Lupia, A., Micaelli, M., Marchesi, N., Sala, F., Pascale, A., Rossi, D., Vasile, F., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00191 · Cited by 9 · see citing works
Self-citationAmadio, M., Pascale, A., Govoni, S. M., Laurini, E., Pricl, S., Gaggeri, R., Rossi, D., & Collina, S. (2013) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12117 · Cited by 9 · see citing works
Self-citationRNA processing-associated molecular mechanisms of neurodegenerative diseases
Tang, A. Y. (2015) · Journal of Applied Genetics · doi:10.1007/s13353-015-0330-5 · Cited by 6 · see citing works
HuD regulates apoptosis in N2a cells by regulating Msi2 expression
Gaikwad, N., Sarwade, R. D., Halder, S., Agarwal, G., & Seshadri, V. (2024) · PLoS ONE · doi:10.1371/journal.pone.0315535 · Cited by 3 · see citing works
Reducing HuD Levels Alleviates Alzheimer's Disease Pathology in 5xFAD Mice
Ji, E., Pal, A., Claybourne, Q. C., Michel, M., Munk, R. B., McDevitt, R. A., Cui, C., & Gorospe, M. (2025) · Aging Cell · doi:10.1111/acel.70080 · Cited by 2 · see citing works
Chakraborty, S., Subramanian, K., Rajesh, A., Majumder, R., Rupanagudi, K. V., Abhishek, M. L., TLSA study team, Issac, T. G., SANSCOG study team, Sundarakumar, J. S., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70429 · Cited by 1 · see citing works
Aberrant translation of proteins implicated in Alzheimer�s disease pathology
Bottley, A., & Kondrashov, A. (2013) · OA Genetics · doi:10.13172/2054-197x-1-1-918 · Cited by 2 · see citing works
Sensing the needs: Molecular basis of miRNA regulatory role of ELAVL protein HuR
Mukherjee, K. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2026.120200 · Cited by 1 · see citing works
Pascale, A., Osera, C., Moro, F., Clemente, A. D., Giannotti, G., Caffino, L., Govoni, S. M., Fumagalli, F., & Cervo, L. (2016) · Hippocampus · doi:10.1002/hipo.22572 · Cited by 1 · see citing works
Self-citationBird, C. W. (2012) · UNM’s Digital Repository (University of New Mexico)
ELAVL Proteins, miRNA Fate, and Extracellular RNA Communication in Brain Aging and Neurodegeneration
Mukherjee, K., & Bhattacharyya, S. N. (2026) · Cells · doi:10.3390/cells15181649
- Authors
- Amadio, M., Pascale, A., Wang, J., Ho, L., Quattrone, A., Gandy, S., Haroutunian, V., Racchi, M., & Pasinetti, G. M.
- Affiliations
- University of Pavia (IT)
- James J. Peters VA Medical Center (US)
- University of Trento (IT)
- Corresponding author
- Amadio, Marialaura
- ORCID
- Venue
- Journal of Alzheimer's Disease
- Publisher
- SAGE Publications
- Published
- 2009-02-16
- Volume
- 16
- Issue
- 2
- Pages
- 409-419
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- PMC
- PMC6057145
- OpenAlex
- W1567068661
- Cited by
- 63
- References
- 35
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 5 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 3 · 2016: 6 · 2015: 3 · 2014: 5 · 2013: 6 · 2012: 6
- FWCI
- 2.66
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Regione Lombardia
- National Institute on Aging (P01AG010491)
- European Social Fund
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- RNA-binding proteins
- MeSH terms
- ELAV-Like Protein 1, ADAM10 Protein, Aged, Aged, 80 and over, Alzheimer Disease, Analysis of Variance, Antigens, Surface, Brain, Cell Cycle, Enzyme-Linked Immunosorbent Assay, Female, Gene Expression Regulation, Humans, Male, Membrane Proteins, Neuroblastoma, Peptide Fragments, Postmortem Changes, RNA, Messenger, Tetrazolium Salts, Thiazoles, Case-Control Studies, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, RNA-Binding Proteins, Disease Progression, Cell Line, Tumor, ADAM Proteins, ELAV Proteins, Amyloid Precursor Protein Secretases
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
