U1 small nuclear ribonucleoprotein complex and RNA splicing alterations in Alzheimer’s disease
Open accessAbstract
Deposition of insoluble protein aggregates is a hallmark of neurodegenerative diseases. The universal presence of β-amyloid and tau in Alzheimer’s disease (AD) has facilitated advancement of the amyloid cascade and tau hypotheses that have dominated AD pathogenesis research and therapeutic development. However, the underlying etiology of the disease remains to be fully elucidated. Here we report a comprehensive study of the human brain-insoluble proteome in AD by mass spectrometry. We identify 4,216 proteins, among which 36 proteins accumulate in the disease, including U1-70K and other U1 small nuclear ribonucleoprotein (U1 snRNP) spliceosome components. Similar accumulations in mild cognitive impairment cases indicate that spliceosome changes occur in early stages of AD. Multiple U1 snRNP subunits form cytoplasmic tangle-like structures in AD but not in other examined neurodegenerative disorders, including Parkinson disease and frontotemporal lobar degeneration. Comparison of RNA from AD and control brains reveals dysregulated RNA processing with accumulation of unspliced RNA species in AD, including myc box-dependent-interacting protein 1, clusterin, and presenilin-1 . U1-70K knockdown or antisense oligonucleotide inhibition of U1 snRNP increases the protein level of amyloid precursor protein. Thus, our results demonstrate unique U1 snRNP pathology and implicate abnormal RNA splicing in AD pathogenesis.
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?
Prior aggregated proteome analysis detected deposition of U1 snRNP and a deficit of RNA splicing in AD brain.
“We performed a comprehensive analysis of the aggregated proteome, detecting the deposition of U1 small nuclear ribonucleoprotein (U1 snRNP) and a deficit of RNA splicing in AD brain (Bai et al., 2013; Lutz and Peng, 2018).”
From Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer’s Disease Progression (2020) · cites this paper as Bai et al., 2013
RNA splicing deficits have previously been identified in AD brain and could impact transcription of many genes including tau, APP, and presenilins.
“We and others have previously identified RNA splicing deficits in AD brain which could have profound impact on transcription of many genes, including tau, APP, and presenilins (Bai et al., 2013; Tollervey et al., 2011).”
From A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer’s Disease (2017) · cites this paper as Bai et al., 2013
U1 snRNPs are mislocalized in AD to the cytoplasm of neuronal cell bodies where they aggregate with NFTs and contribute to widespread alterations in RNA processing.
“These ribonucleoproteins, constituents of the spliceosome complex responsible for RNA processing, are mislocalized in AD to the cytoplasm of neuronal cell bodies where they aggregate with NFTs and contribute to widespread alterations in RNA processing [134].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [134]
Aggregation of U1 snRNPs with tau appears unique to the AD brain and absent among other primary tauopathies, such as FTLD.
“this aggregation of U1 snRNPs with tau appears to be unique to the AD brain and absent among other primary tauopathies, such as FTLD [134, 138].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [134]
U1 small nuclear ribonucleoproteins and other RNA-binding proteins are associated with tau tangles in the AD brain detergent-insoluble proteome.
“previous analyses of the AD brain detergent-insoluble proteome, which have repeatedly demonstrated the association of U1 small nuclear ribonucleoproteins (U1 snRNPs) and other RNA-binding proteins with tau tangles [133–137].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [134]
Many U1 snRNPs colocalize with neurofibrillary tangles and paired helical filaments in AD brain.
“Interestingly, our previous studies demonstrated that many of the U1 snRNPs colocalize with neurofibrillary tangles and paired helical filaments in AD brain [24, 32–34], and that accumulation of insoluble snRNPs correlates strongly with both amyloid and Tau pathology [32–37].”
From Deep proteomic network analysis of Alzheimer’s disease brain reveals alterations in RNA binding proteins and RNA splicing associated with disease (2018) · cites this paper as [24]
U1 snRNPs are a major component of the AD insoluble proteome.
“We have previously shown that U1 snRNPs are a major component of the AD insoluble proteome [24, 32–34].”
From Deep proteomic network analysis of Alzheimer’s disease brain reveals alterations in RNA binding proteins and RNA splicing associated with disease (2018) · cites this paper as [24]
snRNP alterations are associated with deficits in RNA splicing in AD brain, a finding recently confirmed by others.
“Although we have previously observed that snRNP alterations are associated with deficits in RNA splicing in AD brain [24, 32]—a finding recently confirmed by others [52]”
From Deep proteomic network analysis of Alzheimer’s disease brain reveals alterations in RNA binding proteins and RNA splicing associated with disease (2018) · cites this paper as [24]
U1 spliceosome proteins undergo a dramatic shift in solubility in AD brain and aggregate in close proximity to neurofibrillary tangles.
“This may be due to the fact that U1 spliceosome proteins undergo a dramatic shift in solubility in AD brain, and aggregate in close proximity to neurofibrillary tangles [24, 32–34].”
From Deep proteomic network analysis of Alzheimer’s disease brain reveals alterations in RNA binding proteins and RNA splicing associated with disease (2018) · cites this paper as [24]
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
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Mapping and quantifying mammalian transcriptomes by RNA-Seq
Mortazavi, A., Williams, B. A., McCue, K., Schaeffer, L., & Wold, B. (2008) · Nature Methods · doi:10.1038/nmeth.1226 · Cited by 13,696 · see citing works
Amyloid 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
Mild Cognitive Impairment: Clinical Characterization and Outcome
Petersen, R. C., Smith, G. E., Waring, S. C., Ivnik, R. J., Tangalos, E. G., & Kokmen, E. (1999) · Archives of Neurology · doi:10.1001/archneur.56.3.303 · Cited by 8,980 · see citing works
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382 · see citing works
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240 · see citing works
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
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404 · see citing works
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961 · see citing works
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431 · see citing works
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454 · see citing works
Consortium to Establish a Registry for Alzheimer's Disease (CERAD)
Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859 · see citing works
Diagnostic Criteria for Parkinson Disease
Gelb, D. J., Oliver, E., & Gilman, S. (1999) · Archives of Neurology · doi:10.1001/archneur.56.1.33 · Cited by 2,822 · see citing works
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works
Direct multiplexed measurement of gene expression with color-coded probe pairs
Geiss, G. K., Bumgarner, R. E., Birditt, B., Dahl, T., Dowidar, N., Dunaway, D. L., Fell, H. P., Ferree, S., George, R. D., Grogan, T., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt1385 · Cited by 2,066 · see citing works
α-Synuclein is phosphorylated in synucleinopathy lesions
Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 1,906 · see citing works
HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542 · see citing works
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Kim, H. J., Kim, N. C., Wang, Y., Scarborough, E. A., Moore, J., Diaz, Z., MacLea, K. S., Freibaum, B. D., Li, S., Molliex, A., et al. (2013) · Nature · doi:10.1038/nature11922 · Cited by 1,476 · see citing works
Self-citationClinical and Pathological Diagnosis of Frontotemporal Dementia
McKhann, G. M. (2001) · Archives of Neurology · doi:10.1001/archneur.58.11.1803 · Cited by 1,475 · see citing works
A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · see citing works
Wyss-Coray (2006) · doi:10.1038/nm1484 · Cited by 1,284 · see citing works
Toxic Proteins in Neurodegenerative Disease
Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251 · see citing works
Mechanical Devices of the Spliceosome: Motors, Clocks, Springs, and Things
Staley, J. P., & Guthrie, C. (1998) · Cell · doi:10.1016/s0092-8674(00)80925-3 · Cited by 1,127 · see citing works
Classification criteria for mild cognitive impairment
Ritchie, K. A., Artéro, S., & Touchon, J. (2001) · Neurology · doi:10.1212/wnl.56.1.37 · Cited by 831 · see citing works
Office of Rare Diseases Neuropathologic Criteria for Corticobasal Degeneration
Dickson, D. W., Bergeron, C., Chin, S. S., Duyckaerts, C., Horoupian, D., Ikeda, K., Jellinger, K., Lantos, P. L., Lippa, C. F., Mirra, S. S., et al. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.11.935 · Cited by 724 · see citing works
Characterization of the Drosophila melanogaster genome at the nuclear lamina
Pickersgill, H., Kalverda, B., de Wit, E., Talhout, W., Fornerod, M., & van Steensel, B. (2006) · Nature Genetics · doi:10.1038/ng1852 · Cited by 656 · see citing works
U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation
Kaida, D., Berg, M. G., Younis, I., Kasim, M., Singh, L. N., Wan, L., & Dreyfuss, G. (2010) · Nature · doi:10.1038/nature09479 · Cited by 638 · see citing works
Decoding signalling networks by mass spectrometry-based proteomics
Choudhary, C., & Mann, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2900 · Cited by 575 · see citing works
U1 snRNP Determines mRNA Length and Regulates Isoform Expression
Berg, M. G., Singh, L. N., Younis, I., Liu, Q., Pinto, A. M., Kaida, D., Zhang, Z., Cho, S., Sherrill-Mix, S. A., Wan, L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.029 · Cited by 464 · see citing works
Proteome-based plasma biomarkers for Alzheimer's disease
Hye, A., Lynham, S., Thambisetty, M., Čaušević, M., Campbell, J., Byers, H. L., Hooper, C., Rijsdijk, F. V., Tabrizi, S. J., Banner, S. J., et al. (2006) · Brain · doi:10.1093/brain/awl279 · Cited by 463 · see citing works
Applying mass spectrometry-based proteomics to genetics, genomics and network biology
Gstaiger, M., & Aebersold, R. H. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2633 · Cited by 441 · see citing works
Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution
Krummel, D. P., Oubridge, C., Leung, A. K.-W., Li, J., & Nagai, K. (2009) · Nature · doi:10.1038/nature07851 · Cited by 358 · see citing works
Immunology and immunotherapy of Alzheimer's disease
Weiner, H. L., & Frenkel, D. (2006) · Nature Reviews Immunology · doi:10.1038/nri1843 · Cited by 335 · see citing works
Spillantini, M. G., Goedert, M., Crowther, R. A., Murrell, J. R., Farlow, M. R., & Ghetti, B. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4113 · Cited by 334 · see citing works
Proteomic Characterization of Postmortem Amyloid Plaques Isolated by Laser Capture Microdissection
Liao, L., Cheng, D., Wang, J., Duong, D. M., Losik, T. G., Gearing, M., Rees, H. D., Lah, J. J., Levey, A. I., & Peng, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403672200 · Cited by 323 · see citing works
Self-citationAmyloid-Independent Mechanisms in Alzheimer's Disease Pathogenesis
Pimplikar, S. W., Nixon, R. A., Robakis, N. K. R. K., Shen, J., & Tsai, L. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4305-10.2010 · Cited by 281 · see citing works
Rockenstein, E. M., McConlogue, L., Tan, H. T., Power, M., Masliah, E., & Mucke, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28257 · Cited by 259 · see citing works
Proteomics Analysis of the Alzheimer's Disease Hippocampal Proteome
Rukhsana Sultana, A., Debra Boyd-kimball, A., Cai, J., Pierce, W. M. J., Klein, J. B., Merchant, M. L., & Butterfield, D. A. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11203 · Cited by 231 · see citing works
Ince (1998) · doi:10.1046/j.1365-2990.1998.00108.x · Cited by 224 · see citing works
Proteomic identification of novel proteins associated with Lewy bodies
Xia, Q. (2008) · Frontiers in bioscience · doi:10.2741/2973 · Cited by 176 · see citing works
Self-citationBerson, A., Barbash, S., Shaltiel, G., Goll, Y., Hanin, G., Greenberg, D., Ketzef, M., Becker, A. J., Friedman, A., & Soreq, H. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100995 · Cited by 167 · see citing works
Discovery and verification of amyotrophic lateral sclerosis biomarkers by proteomics
Ryberg, H., An, J., Darko, S. W., Lustgarten, J. L., Jaffa, M., Gopalakrishnan, V., Lacomis, D., Cudkowicz, M., & Bowser, R. P. (2010) · Muscle & Nerve · doi:10.1002/mus.21683 · Cited by 128 · see citing works
Ringman, J. M. (2012) · Archives of Neurology · doi:10.1001/archneurol.2011.642 · Cited by 124 · see citing works
Rudrabhatla, P., Jaffe, H., & Pant, H. C. (2011) · The FASEB Journal · doi:10.1096/fj.11-181297 · Cited by 121 · see citing works
Neuropathology of Pick’s disease
Dickson, D. W. (2001) · Neurology · doi:10.1212/wnl.56.suppl_4.s16 · Cited by 119 · see citing works
Alternative splicing of mRNA in the molecular pathology of neurodegenerative diseases
Mills, J. D., & Janitz, M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.10.030 · Cited by 114 · see citing works
Gozal, Y. M., Duong, D. M., Gearing, M., Cheng, D., Hanfelt, J., Funderburk, C. D., Peng, J., Lah, J. J., & Levey, A. I. (2009) · Journal of Proteome Research · doi:10.1021/pr900474t · Cited by 92 · see citing works
Self-citationPhosphoproteomic Analysis of Human Brain by Calcium Phosphate Precipitation and Mass Spectrometry
Xia, Q., Cheng, D., Duong, D. M., Gearing, M., Lah, J. J., Levey, A. I., & Peng, J. (2008) · Journal of Proteome Research · doi:10.1021/pr8000496 · Cited by 88 · see citing works
Self-citationUpdate on the Neuropathological Diagnosis of Frontotemporal Dementias
Trojanowski, J. Q., & Dickson, D. W. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.12.1123 · Cited by 87 · see citing works
Analysis of a membrane‐enriched proteome from postmortem human brain tissue in A lzheimer's disease
Donovan, L. E., Higginbotham, L. A., Dammer, E. B., Gearing, M., Rees, H. D., Xia, Q., Duong, D. M., Seyfried, N. T., Lah, J. J., & Levey, A. I. (2012) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201100068 · Cited by 82 · see citing works
Self-citationSerum biomarkers for Alzheimer's disease: Proteomic discovery
German, D. C., Gurnani, P., Nandi, A., Garner, H. R., Fisher, W. G., Diaz-Arrastia, R. R., O’Suilleabhain, P. E., & Rosenblatt, K. P. (2007) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2007.05.009 · Cited by 58 · see citing works
A novel peptidomics approach to detect markers of Alzheimer’s disease in cerebrospinal fluid
Wijte, D., McDonnell, L. A., Balog, C. I. A., Bossers, K., Deelder, A. M., Swaab, D. F., Verhaagen, J., & Mayboroda, O. A. (2012) · Methods · doi:10.1016/j.ymeth.2012.03.018 · Cited by 51 · see citing works
Clinical proteomics in neurodegenerative diseases
Zhou, J., Hanfelt, J., & Peng, J. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200700378 · Cited by 23 · see citing works
Self-citationGozal, Y. M., Dammer, E. B., Duong, D. M., Cheng, D., Gearing, M., Rees, H. D., Peng, J., Lah, J. J., & Levey, A. I. (2011) · Frontiers in Neurology · doi:10.3389/fneur.2011.00024 · Cited by 23 · see citing works
Self-citationWada‐Isoe, K., Michio, K., Imamura, K., Nakaso, K., Kusumi, M., Kowa, H., & Nakashima, K. (2007) · Journal of Neural Transmission · doi:10.1007/s00702-007-0794-5 · Cited by 14 · see citing works
Flagged first, then by citations
1 of the 58 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Scotti, M. M., & Swanson, M. S. (2015) · Nature Reviews Genetics · doi:10.1038/nrg.2015.3 · Cited by 1,130 · see citing works
Johnson, E. C. B., Dammer, E. B., Duong, D. M., Ping, L., Zhou, M., Yin, L., Higginbotham, L. A., Guajardo, A., White, B., Troncoso, J. C., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0815-6 · Cited by 1,001 · see citing works
Self-citationConnecting genetic risk to disease end points through the human blood plasma proteome
Suhre, K., Arnold, M., Bhagwat, A. M., Cotton, R. J., Engelke, R., Raffler, J., Sarwath, H., Thareja, G., Wahl, A., DeLisle, R. K., et al. (2017) · Nature Communications · doi:10.1038/ncomms14357 · Cited by 800 · see citing works
Stress granules and neurodegeneration
Wolozin, B. L., & Ivanov, P. V. (2019) · Nature reviews. Neuroscience · doi:10.1038/s41583-019-0222-5 · Cited by 782 · see citing works
Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer’s Disease Progression
Bai, B., Wang, X., Li, Y., Chen, P.-C., Yu, K., Dey, K. K., Yarbro, J. M., Han, X., Lutz, B. M., Rao, S., et al. (2020) · Neuron · doi:10.1016/j.neuron.2019.12.015 · Cited by 632 · see citing works
“We performed a comprehensive analysis of the aggregated proteome, detecting the deposition of U1 small nuclear ribonucleoprotein (U1 snRNP) and a deficit of RNA splicing in AD brain (Bai et al., 2013; Lutz and Peng, 2018).”
BackgroundMethodInfluentialSelf-citationRaja, W. K., Mungenast, A. E., Lin, Y.-T., Ko, T., Abdurrob, F., Seo, J., & Tsai, L.-H. (2016) · PLOS ONE · doi:10.1371/journal.pone.0161969 · Cited by 569 · see citing works
Johnson, E. C. B., Carter, E. K., Dammer, E. B., Duong, D. M., Gerasimov, E. S., Liu, Y., Liu, J., Betarbet, R., Ping, L., Yin, L., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-021-00999-y · Cited by 561 · see citing works
Self-citationNuclear speckles: molecular organization, biological function and role in disease
Gałgański, Ł., Urbanek-Trzeciak, M. O., & Krzyżosiak, W. J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx759 · Cited by 489 · see citing works
A new view of transcriptome complexity and regulation through the lens of local splicing variations
Vaquero-Garcia, J., Barrera, A., Gazzara, M. R., González-Vallinas, J., Lahens, N. F., Hogenesch, J. B., Lynch, K. W., & Barash, Y. (2016) · eLife · doi:10.7554/elife.11752 · Cited by 488 · see citing works
Seyfried, N. T., Dammer, E. B., Swarup, V., Nandakumar, D., Duong, D. M., Yin, L., Deng, Q., Nguyen, T., Hales, C. M., Wingo, T., et al. (2017) · Cell Systems · doi:10.1016/j.cels.2016.11.006 · Cited by 477 · see citing works
Self-citationRaj, T., Li, Y. I., Wong, G., Humphrey, J., Wang, M., Ramdhani, S., Wang, Y.-C., Ng, B., Gupta, I., Haroutunian, V., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0238-1 · Cited by 430 · see citing works
Self-citationPosttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains
Arakhamia, T., Lee, C. E., Carlomagno, Y., Kumar, M., Duong, D. M., Wesseling, H., Kundinger, S. R., Wang, K., Williams, D., Deture, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.01.027 · Cited by 400 · see citing works
Self-citationInteraction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity
Vanderweyde, T. E., Apicco, D. J., Youmans-Kidder, K., Ash, P. E. A., Cook, C. N., da Rocha, E. L., Jansen‐West, K. R., Frame, A. A., Citro, A., Leszyk, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.045 · Cited by 346 · see citing works
Wang, C., Xiong, M., Gratuze, M., Bao, X., Shi, Y., Andhey, P. S., Manis, M., Schroeder, C., Yin, Z., Madore, C., et al. (2021) · Neuron · doi:10.1016/j.neuron.2021.03.024 · Cited by 334 · see citing works
Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease
Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331 · see citing works
Machine learning identifies candidates for drug repurposing in Alzheimer’s disease
Rodriguez, S., Hug, C., Todorov, P., Moret, N., Boswell, S. A., Evans, K., Zhou, G., Johnson, N. T., Hyman, B. T., Sorger, P. K., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21330-0 · Cited by 299 · see citing works
Proteomic landscape of Alzheimer’s Disease: novel insights into pathogenesis and biomarker discovery
Bai, B., Vanderwall, D., Li, Y., Wang, X., Poudel, S., Wang, H., Dey, K. K., Chen, P., Yang, K., & Peng, J. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00474-z · Cited by 252 · see citing works
Self-citationProteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease
Drummond, E., Nayak, S., Faustin, A., Pires, G., Hickman, R. A., Askenazi, M., Cohen, M., Haldiman, T., Kim, C., Han, X., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1691-0 · Cited by 239 · see citing works
Spliceosome-targeted therapies trigger an antiviral immune response in triple-negative breast cancer
Bowling, E. A., Wang, J. H., Gong, F., Wu, W., Neill, N. J., Kim, I. S., Tyagi, S., Orellana, M. C., Kurley, S. J., Domínguez-Vidaña, R., et al. (2021) · Cell · doi:10.1016/j.cell.2020.12.031 · Cited by 221 · see citing works
Johnson, E. C. B., Dammer, E. B., Duong, D. M., Yin, L., Thambisetty, M., Troncoso, J. C., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0282-4 · Cited by 225 · see citing works
Self-citationTau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220 · see citing works
Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components
Lester, E., Ooi, F. K., Bakkar, N., Ayers, J. I., Woerman, A. L., Wheeler, J., Bowser, R. P., Carlson, G. A., Prusiner, S. B., & Parker, R. (2021) · Neuron · doi:10.1016/j.neuron.2021.03.026 · Cited by 212 · see citing works
Defective control of pre–messenger RNA splicing in human disease
Chabot, B., & Shkreta, L. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201510032 · Cited by 209 · see citing works
Wang, H., Dey, K. K., Chen, P.-C., Li, Y., Niu, M., Cho, J.-H., Wang, X., Bai, B., Jiao, Y., Chepyala, S. R., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00384-6 · Cited by 210 · see citing works
Self-citationHsieh, Y.-C., Guo, C., Yalamanchili, H. K., Abreha, M., Al-Ouran, R., Li, Y., Dammer, E. B., Lah, J. J., Levey, A. I., Bennett, D. A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.104 · Cited by 196 · see citing works
Self-citationUnderstanding Alzheimer Disease at the Interface between Genetics and Transcriptomics
Verheijen, J., & Sleegers, K. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.02.007 · Cited by 189 · see citing works
Deregulation of purine metabolism in Alzheimer's disease
Ansoleaga, B., Jové, M., Schlüter, A., Garcia‐Esparcia, P., Moreno, J. R., Pujol, A., Pamplona, R., Portero‐Otín, M., & Ferrer, I. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.08.004 · Cited by 160 · see citing works
Daguenet, É., Dujardin, G., & Valcárcel, J. (2015) · EMBO Reports · doi:10.15252/embr.201541116 · Cited by 151 · see citing works
RNA binding proteins co-localize with small tau inclusions in tauopathy
Maziuk, B. F., Apicco, D. J., Cruz, A. L., Jiang, L., Ash, P. E. A., da Rocha, E. L., Zhang, C., Yu, W. H., Leszyk, J., Abisambra, J. F., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0574-5 · Cited by 151 · see citing works
Watson, C. N., Belli, A., & Pietro, V. D. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00364 · Cited by 148 · see citing works
Gupta, V. B., Chitranshi, N., den Haan, J., Mirzaei, M., You, Y., Lim, J. K. H., Basavarajappa, D. K., Godinez, A., Angelantonio, S. D., Sachdev, P. S., et al. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100899 · Cited by 143 · see citing works
Mirzaei, M., Gupta, V. B., Chick, J. M., Greco, T. M., Wu, Y., Chitranshi, N., Wall, R. V., Hone, E., Deng, L., Dheer, Y., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-12858-7 · Cited by 140 · see citing works
Implications of polyadenylation in health and disease
Curinha, A., Bráz, S., Pereira‐Castro, I., Cruz, A., & Moreira, A. (2014) · Nucleus · doi:10.4161/nucl.36360 · Cited by 137 · see citing works
Adusumalli, S., Ngian, Z., Lin, W., Benoukraf, T., & Ong, C. (2019) · Aging Cell · doi:10.1111/acel.12928 · Cited by 137 · see citing works
Hinrich, A. J., Jodelka, F. M., Chang, J. L., Brutman, D., Bruno, A. M., Briggs, C. A., James, B. D., Stutzmann, G. E., Bennett, D. A., Miller, S. A., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505846 · Cited by 127 · see citing works
Self-citationThe miRNome of Alzheimer's disease: consistent downregulation of the miR-132/212 cluster
Pichler, S., Gu, W., Hartl, D., Gasparoni, G., Leidinger, P., Keller, A., Meese, E. U., Mayhaus, M., Hampel, H. J., & Riemenschneider, M. J. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.09.019 · Cited by 129 · see citing works
Bai, B., Tan, H., Pagala, V., High, A. A., Ichhaporia, V. P., Hendershot, L. M., & Peng, J. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.10.007 · Cited by 119 · see citing works
Self-citationSystems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau
Rayaprolu, S., Higginbotham, L., Bagchi, P., Watson, C. M., Zhang, T., Levey, A. I., Rangaraju, S., & Seyfried, N. T. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-00840-3 · Cited by 118 · see citing works
Self-citationStilling, R. M., Benito, E., Barth, J., Gertig, M., Capece, V., Burckhardt, S., Bonn, S., & Fischer, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00373 · Cited by 116 · see citing works
Noncoding translation mitigation
Kesner, J. S., Chen, Z., Shi, P., Aparicio, A. O., Murphy, M. R., Guo, Y., Trehan, A., Lipponen, J. E., Recinos, Y., Myeku, N., et al. (2023) · Nature · doi:10.1038/s41586-023-05946-4 · Cited by 116 · see citing works
Hales, C. M., Dammer, E. B., Deng, Q., Duong, D. M., Gearing, M., Troncoso, J. C., Thambisetty, M., Lah, J. J., Shulman, J. M., Levey, A. I., et al. (2016) · PROTEOMICS · doi:10.1002/pmic.201600057 · Cited by 99 · see citing works
Self-citationMoving beyond amyloid and tau to capture the biological heterogeneity of Alzheimer’s disease
Young‐Pearse, T. L., Lee, H., Hsieh, Y., Chou, V., & Selkoe, D. J. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.03.005 · Cited by 99 · see citing works
Brain pathology in myotonic dystrophy: when tauopathy meets spliceopathy and RNAopathy
Caillet‐Boudin, M., Fernández-Gómez, F.-J., Tran, H., Dhaenens, C., Buée, L., & Sergeant, N. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2013.00057 · Cited by 99 · see citing works
Piras, I. S., Krate, J., Delvaux, E., Nolz, J., Mastroeni, D., Persico, A. M., Jepsen, W. M., Beach, T. G., Huentelman, M. J., & Coleman, P. D. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181113 · Cited by 98 · see citing works
Wang, H., Yang, Y., Li, Y., Bai, B., Wang, X., Tan, H., Liu, T., Beach, T. G., Peng, J., & Wu, Z. (2015) · Journal of Proteome Research · doi:10.1021/pr500882h · Cited by 96 · see citing works
Self-citationSFPQ and Tau: critical factors contributing to rapid progression of Alzheimer’s disease
Younas, N., Zafar, S., Shafiq, M., Noor, A., Siegert, A., Arora, A. S., Galkin, A. P., Zafar, A., Schmitz, M., Stadelmann, C., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02178-y · Cited by 93 · see citing works
Hales, C. M., Dammer, E. B., Diner, I., Yi, H., Seyfried, N. T., Gearing, M., Glass, J. D., Montine, T. J., Levey, A. I., & Lah, J. J. (2014) · Brain Pathology · doi:10.1111/bpa.12133 · Cited by 89 · see citing works
Self-citationLSD1 protects against hippocampal and cortical neurodegeneration
Christopher, M. A., Myrick, D. A., Barwick, B. G., Engstrom, A., Porter‐Stransky, K. A., Boss, J. M., Weinshenker, D., Levey, A. I., & Katz, D. J. (2017) · Nature Communications · doi:10.1038/s41467-017-00922-9 · Cited by 88 · see citing works
Self-citationCombating deleterious phase transitions in neurodegenerative disease
Darling, A. L., & Shorter, J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118984 · Cited by 85 · see citing works
Hypoxia-induced autophagy as an additional mechanism in human osteosarcoma radioresistance
Feng, H., Wang, J., Chen, W., Shan, B., Guo, Y., Xu, J., Wang, L., Guo, P., & Zhang, Y. (2016) · Journal of bone oncology · doi:10.1016/j.jbo.2016.03.001 · Cited by 85 · see citing works
Dysregulation of RNA Splicing in Tauopathies
Apicco, D. J., Zhang, C., Maziuk, B. F., Jiang, L., Ballance, H. I., Boudeau, S., Ung, C. Y., Li, H., & Wolozin, B. L. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.093 · Cited by 82 · see citing works
Bishof, I., Dammer, E. B., Duong, D. M., Kundinger, S. R., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001747 · Cited by 80 · see citing works
Self-citationNon-Coding RNAs in Psychiatric Disorders and Suicidal Behavior
Yoshino, Y., & Dwivedi, Y. (2020) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.543893 · Cited by 82 · see citing works
Quadros, A. R. A. D. A., Li, Z., Wang, X., Ndayambaje, I. S., Aryal, S., Ramesh, N., Nolan, M., Jayakumar, R., Han, Y., Stillman, H., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02655-0 · Cited by 74 · see citing works
Self-citationModeling Neurodegenerative Microenvironment Using Cortical Organoids Derived from Human Stem Cells
Yan, Y., Song, L., Bejoy, J., Zhao, J., Kanekiyo, T., Bu, G., Zhou, Y., & Li, Y. (2018) · Tissue Engineering Part A · doi:10.1089/ten.tea.2017.0423 · Cited by 80 · see citing works
Self-citationDrummond, E. S., Nayak, S., Ueberheide, B., & Wisniewski, T. (2015) · Scientific Reports · doi:10.1038/srep15456 · Cited by 78 · see citing works
Xue, S., Gong, R., He, F., Yan-qin, L., Wang, Y., Tan, T., & Luo, S. (2019) · Science Advances · doi:10.1126/sciadv.aax5349 · Cited by 77 · see citing works
Huang, J.-L., Qin, M.-C., Zhou, Y., Xu, Z., Yang, S., Zhang, F., Zhong, J., Liang, M.-K., Chen, B., Zhang, W., et al. (2018) · Aging · doi:10.18632/aging.101387 · Cited by 78 · see citing works
Nuclear ULK1 promotes cell death in response to oxidative stress through PARP1
Joshi, A., Iyengar, R. V., Joo, J. H., Li-Harms, X., Wright, C., Marino, R., Winborn, B. J., Phillips, A. H., Temirov, J. P., Sciarretta, S., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.88 · Cited by 77 · see citing works
Self-citationAlternative splicing in Alzheimer’s disease
Biamonti, G., Amato, A. M., Belloni, E., Matteo, A. D., Infantino, L., Pradella, D., & Ghigna, C. (2019) · Aging Clinical and Experimental Research · doi:10.1007/s40520-019-01360-x · Cited by 77 · see citing works
Wang, Z., Zhang, F., He, J., Wu, P., Tay, L. W. R., Cai, M., Nian, W., Weng, Y., Qin, L., Chang, J. T., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.09.012 · Cited by 74 · see citing works
Self-citationBernstein, A. I., Lin, Y., Street, R. C., Lin, L., Dai, Q., Yu, L., Bao, H., Gearing, M., Lah, J. J., Nelson, P. T., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw109 · Cited by 73 · see citing works
Self-citationGallart‐Palau, X., Lee, B. S. T., Adav, S. S., Qian, J., Serra, A., Park, J. E., Lai, M. K. P., Chen, C., Kalaria, R. N., & Sze, S. K. (2016) · Molecular Brain · doi:10.1186/s13041-016-0205-7 · Cited by 70 · see citing works
Wang, S., Yu, L., Yang, H., Li, C., Hui, Z., Xu, Y., & Zhu, X. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151397 · Cited by 70 · see citing works
Splicing alterations in healthy aging and disease
Angarola, B. L., & Anczuków, O. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1643 · Cited by 69 · see citing works
RNA Dynamics in Alzheimer’s Disease
Rybak‐Wolf, A., & Plass, M. (2021) · Molecules · doi:10.3390/molecules26175113 · Cited by 70 · see citing works
Biomaterial design inspired by membraneless organelles
Liu, J., Zhorabek, F., & Chau, Y. (2022) · Matter · doi:10.1016/j.matt.2022.07.001 · Cited by 68 · see citing works
Alternative Splicing in Alzheimer’s Disease
Love, J. E., Hayden, E. J., & Rohn, T. T. (2015) · Journal of Parkinson’s Disease and Alzheimer’s Disease · doi:10.13188/2376-922x.1000010 · Cited by 67 · see citing works
Splicing and neurodegeneration: Insights and mechanisms
Nik, S., & Bowman, T. V. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1532 · Cited by 65 · see citing works
Nourse, J. P., Spada, S., & Danckwardt, S. (2020) · Biomolecules · doi:10.3390/biom10060915 · Cited by 64 · see citing works
The intellectual disability gene PQBP1 rescues Alzheimer’s disease pathology
Tanaka, H., Kondo, K., Chen, X., Homma, H., Tagawa, K., Kerever, A., Aoki, S., Saito, T., Saido, T. C., Muramatsu, S., et al. (2018) · Molecular Psychiatry · doi:10.1038/s41380-018-0253-8 · Cited by 62 · see citing works
McMillan, P. J., Strovas, T. J., Baum, M., Mitchell, B. K., Eck, R. J., Hendricks, N., Wheeler, J. M., Latimer, C. S., Keene, C. D., & Kraemer, B. C. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01219-1 · Cited by 64 · see citing works
Wang, Z.-H., Liu, P., Liu, X., Manfredsson, F. P., Sandoval, I. M., Yu, S. P., Wang, J., & Ye, K. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.018 · Cited by 64 · see citing works
Aggregation Properties of the Small Nuclear Ribonucleoprotein U1-70K in Alzheimer Disease
Diner, I., Hales, C. M., Bishof, I., Rabenold, L., Duong, D. M., Yi, H., Laur, O., Gearing, M., Troncoso, J., Thambisetty, M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562959 · Cited by 63 · see citing works
Self-citationProteomics of protein post-translational modifications implicated in neurodegeneration
Ren, R., Dammer, E. B., Wang, G., Seyfried, N. T., & Levey, A. I. (2014) · Translational Neurodegeneration · doi:10.1186/2047-9158-3-23 · Cited by 63 · see citing works
Self-citationA network approach to clinical intervention in neurodegenerative diseases
Santiago, J. A., & Potashkin, J. A. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.10.002 · Cited by 62 · see citing works
Chen, P., Han, X., Shaw, T. I., Fu, Y., Sun, H., Niu, M., Wang, Z., Jiao, Y., Teubner, B. J. W., Eddins, D. M., et al. (2022) · Nature Aging · doi:10.1038/s43587-022-00290-0 · Cited by 60 · see citing works
Self-citationTan, H., Wu, Z., Wang, H., Bai, B., Li, Y., Wang, X., Zhai, B., Beach, T. G., & Peng, J. (2014) · PROTEOMICS · doi:10.1002/pmic.201400171 · Cited by 60 · see citing works
Self-citationGuennewig, B., Lim, J., Marshall, L. L., McCorkindale, A. N., Paasila, P. J., Patrick, E., Kril, J. J., Halliday, G. M., Cooper, A. A., & Sutherland, G. T. (2021) · Scientific Reports · doi:10.1038/s41598-021-83872-z · Cited by 59 · see citing works
RNA dysregulation in neurodegenerative diseases
Li, Y., & Sun, S. (2025) · The EMBO Journal · doi:10.1038/s44318-024-00352-6 · Cited by 62 · see citing works
Self-citationKarri, V., Ramos, D., Bauzá‐Martinez, J., Odena, M. A., de Oliveira, E., Coort, S. L., Evelo, C. T., Mariman, E. C. M., Schuhmacher, M., & Kumar, V. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.06.020 · Cited by 63 · see citing works
Hales, C. M., Seyfried, N. T., Dammer, E. B., Duong, D., Yi, H., Gearing, M., Troncoso, J. C., Mufson, E. J., Thambisetty, M., Levey, A. I., et al. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-15 · Cited by 58 · see citing works
Self-citationSaurat, N. G., Minotti, A. P., Rahman, M. T., Sikder, T., Zhang, C., Cornacchia, D., Jungverdorben, J., Ciceri, G., Betel, D., & Studer, L. (2024) · Cell stem cell · doi:10.1016/j.stem.2024.06.001 · Cited by 58 · see citing works
Levites, Y., Dammer, E. B., Ran, Y., Tsering, W., Duong, D. M., Abreha, M. H., Gadhavi, J. D., Lolo, K., Trejo‐Lopez, J. A., Phillips, J., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101669 · Cited by 57 · see citing works
Self-citationCholinergic Surveillance over Hippocampal RNA Metabolism and Alzheimer's-Like Pathology
Kolisnyk, B., Al‐Onaizi, M., Soreq, L., Barbash, S., Bekenstein, U., Haberman, N., Hanin, G., Kish, M. T., da Silva, J. S., Fahnestock, M. L., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw177 · Cited by 57 · see citing works
Prema, A., Thenmozhi, A. J., Manivasagam, T., Essa, M. M., Akbar, M. D., & Akbar, M. D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165955 · Cited by 57 · see citing works
Huang, Y., Driedonks, T. A. P., Cheng, L., Turchinovich, A., Rajapaksha, H., Arab, T., Powell, B. H., Pletniková, O., Redding‐Ochoa, J., Troncoso, J. C., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220322 · Cited by 55 · see citing works
A multiomic approach to characterize the temporal sequence in Alzheimer's disease-related pathology
Marttinen, M., Paananen, J., Neme, A., Mitra, V., Takalo, M., Natunen, T., Paldanius, K. M. A., Mäkinen, P. M., Bremang, M., Kurki, M., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.12.009 · Cited by 54 · see citing works
Satoh, J.-I., Yamamoto, Y., Asahina, N., Kitano, S., & Kino, Y. (2014) · Disease Markers · doi:10.1155/2014/123165 · Cited by 46 · see citing works
Mills, J. D., van Vliet, E. A., Chen, B. J., Janitz, M., Anink, J. J., Baayen, J. C., Idema, S., Devore, S., Friedman, D., Diehl, B., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104612 · Cited by 52 · see citing works
Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
Diner, I., Nguyen, T. T. H., & Seyfried, N. T. (2017) · Journal of Visualized Experiments · doi:10.3791/55835 · Cited by 48 · see citing works
Self-citationRamos‐Miguel, A., Hercher, C., Beasley, C. L., Barr, A. M., Bayer, T. A., Falkai, P., Leurgans, S. E., Schneider, J. A., Bennett, D. A., & Honer, W. G. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0061-4 · Cited by 46 · see citing works
Self-citationPatel, R. J., Brophy, C., Hickling, M., Neve, J., & Furger, A. (2019) · BMC Medical Genomics · doi:10.1186/s12920-019-0509-4 · Cited by 46 · see citing works
The Neat Dance of COVID-19: NEAT1, DANCR, and Co-Modulated Cholinergic RNAs Link to Inflammation
Meydan, C., Madrer, N., & Soreq, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.590870 · Cited by 46 · see citing works
Caldas, P., Luz, M., Baseggio, S., Andrade, R., Sobral, D., & Grosso, A. R. (2024) · Communications Biology · doi:10.1038/s42003-024-05779-5 · Cited by 45 · see citing works
Deconstructing and targeting the genomic architecture of human neurodegeneration
Jager, P. L. D., Yang, H., & Bennett, D. A. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0240-z · Cited by 46 · see citing works
Self-citationBottero, V., & Potashkin, J. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215403 · Cited by 46 · see citing works
RNA induces unique tau strains and stabilizes Alzheimer’s disease seeds
Zwierzchowski-Zarate, A. N., Mendoza‐Oliva, A., Kashmer, O. M., Collazo-Lopez, J. E., White, C. L., & Diamond, M. I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102132 · Cited by 45 · see citing works
Köhler, J., Schüler, M., Gauler, T. C., Nöpel‐Dünnebacke, S., Ahrens, M., Hoffmann, A.-C., Kasper, S., Nensa, F., Gomez, B., Hahnemann, M. L., et al. (2015) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-015-2095-y · Cited by 44 · see citing works
Yagensky, O., Kohansal-Nodehi, M., Gunaseelan, S., Rabe, T., Zafar, S., Zerr, I., Härtig, W., Urlaub, H., & Chua, J. J. E. (2019) · eLife · doi:10.7554/elife.47498 · Cited by 44 · see citing works
- Authors
- Bai, B., Hales, C. M., Chen, P.-C., Gozal, Y., Dammer, E. B., Fritz, J. J., Wang, X., Xia, Q., Duong, D. M., Street, C., Cantero, G., Cheng, D., Jones, D. R., Wu, Z., Li, Y., Diner, I., Heilman, C. J., Rees, H. D., Wu, H., Lin, L., Szulwach, K. E., Gearing, M., Mufson, E. J., Bennett, D. A., Montine, T. J., Seyfried, N. T., Wingo, T. S., Sun, Y. E., Jin, P., Hanfelt, J., Willcock, D. M., Levey, A., Lah, J. J., & Peng, J.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Emory University (US)
- Departments of Structural Biology and Developmental Neurobiology and
- Human Genetics,
- University of California, Los Angeles (US)
- Biostatistics and Bioinformatics,
- Rush University Medical Center (US)
- University of Washington (US)
- University of Kentucky (US)
- ORCID
- Bai, Bing
- Hales, Chadwick M.
- Chen, Ping-Chung
- Dammer, Eric B.
- Wang, Xusheng
- Xia, Qiangwei
- Duong, Duc M.
- Cantero, Gloria
- Cheng, Dongmei
- Jones, Drew R.
- Wu, Zhiping
- Li, Yuxin
- Wu, Hao
- Gearing, Marla
- Mufson, Elliott J.
- Bennett, David A.
- Montine, Thomas J.
- Seyfried, Nicholas T.
- Wingo, Thomas S.
- Sun, Yi E.
- Jin, Peng
- Hanfelt, John
- Levey, Allan
- Lah, James J.
- Peng, Junmin
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-09-10
- Volume
- 110
- Issue
- 41
- Pages
- 16562-16567
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3799305
- OpenAlex
- W2075426349
- Semantic Scholar
- b4638372c5d5e262f0ad2963dd66aed83aac9d24
- Cited by
- 335
- References
- 58
- Citations by year
- 2026: 20 · 2025: 34 · 2024: 23 · 2023: 29 · 2022: 23 · 2021: 43 · 2020: 29 · 2019: 24 · 2018: 27 · 2017: 24 · 2016: 30 · 2015: 12 · 2014: 17
- FWCI
- 13.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- American Lebanese Syrian Associated Charities
- National Institutes of Health
- Instituto de Salud Carlos III
- National Institute on Aging (P01AG014449, F32AG038259, R01AG015819, P30AG010161, R01AG043375, P50AG005136, P50AG025688)
- National Institute of Mental Health (R01MH082068)
- National Cancer Institute (P30CA021765)
- National Institute of General Medical Sciences (P01GM081621, T32GM008169)
- National Institute of Neurological Disorders and Stroke (T32NS007480, F32NS007480, P30NS055077, F30NS057902)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, U1 snRNP, U1-70K, RNA splicing, spliceosome, protein aggregates, amyloid precursor protein, unspliced RNA, mild cognitive impairment, antisense oligonucleotides, clusterin, presenilin 1, neurodegeneration
- MeSH terms
- Alzheimer Disease, Brain, Chromatography, Liquid, Fluorescent Antibody Technique, Humans, Immunohistochemistry, Blotting, Western, Spliceosomes, Alternative Splicing, Ribonucleoprotein, U1 Small Nuclear, Reverse Transcriptase Polymerase Chain Reaction, Proteome, Proteomics, Tandem Mass Spectrometry, High-Throughput Nucleotide Sequencing
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
