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Oligomeric, phosphorylated, and truncated tau and spliceosome pathology within the entorhinal–hippocampal connectome across stages of Alzheimer's disease

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Global analysis of the heparin-enriched plasma proteome captures matrisome-associated proteins in Alzheimer’s diseasePreprint

Guo, Q. J., Ping, L., Dammer, E. B., Duong, D. M., Yin, L., Xu, K., Shantaraman, A., Fox, E. J., Johnson, E. C. B., Roberts, B. R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.06.565824 · Cited by 11 · see citing works

Protein aggregation identified in olfactory neuronal cells is associated with cognitive impairments in a subset of living schizophrenia patients

Nucifora, L. G., Ishizuka, K., Demerdash, N. E., Lee, B. J., Imai, M. T., Ayala‐Grosso, C. A., Yenokyan, G., Cascella, N. G., Lin, S. Y., Schretlen, D. J., et al. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-02956-8 · Cited by 10 · see citing works

Evidence of Filamin A loss of solubility at the prodromal stage of neuropathologically-defined Alzheimer’s disease

Aumont, É., Tremblay, C., Levert, S., Bennett, D. A., Calon, F., & Leclerc, N. M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1038343 · Cited by 10 · see citing works

Application of Genomic Data in Translational Medicine During the Big Data Era

Zhang, Y., Yu, J. M., Xie, X., Jiang, F., & Wu, C. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2901007 · Cited by 10 · see citing works

Brain Cell Type-Specific Nuclear Proteomics Is Imperative to Resolve Neurodegenerative Disease Mechanisms

Nelson, R. S., Dammer, E. B., Santiago, J. V., Seyfried, N. T., & Rangaraju, S. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.902146 · Cited by 9 · see citing works

Effects of the therapeutic correction of U1 snRNP complex on Alzheimer’s disease

Leal, C. B. Q. S., Zimmer, C. G. M., Sinatti, V. V. C., Soares, E. S., Poppe, B., de Wiart, A. C., Chua, X. Y., da Silva, R. V., Magdesian, M. H., Rafii, M. S., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-81687-2 · Cited by 8 · see citing works

Spliceosome protein alterations differentiate hubs of the default mode connectome during the progression of Alzheimer's disease

Perez, S. E., Nadeem, M., He, B., Miguel, J. C., Moreno, D. G., Moreno‐Rodríguez, M., Malek‐Ahmadi, M. H., Hales, C. M., & Mufson, E. J. (2025) · Brain Pathology · doi:10.1111/bpa.70004 · Cited by 7 · see citing works

Proximity Labeling of the Tau Repeat Domain Enriches RNA-Binding Proteins That Are Altered in Alzheimer's Disease and Related Tauopathies

Shapley, S. M., Shantaraman, A., Gadhavi, J. D., Kearney, M. A., Dammer, E. B., Duong, D. M., Bowen, C. A., Watson, C. M., Bagchi, P., Guo, Q., et al. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101458 · Cited by 9 · see citing works

Identification of key mRNAs and signaling pathways in obsessive compulsive disorder based on weighted gene co‐expression network analysis and cytoHubba plugin

Zhang, X., Liu, Y., Guo, B., Li, B., Liu, H., & Wang, Z. (2024) · Brain and Behavior · doi:10.1002/brb3.3412 · Cited by 7 · see citing works

Implications of liquid-liquid phase separation and ferroptosis in Alzheimer's disease

Wang, F., Chen, Z., Zhou, Q., Sun, Q., Zheng, N., Chen, Z., Lin, J., Li, B., & Li, L. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.110083 · Cited by 8 · see citing works

U1 snRNP Biogenesis Defects in Neurodegenerative Diseases

Campagne, S. (2024) · ChemBioChem · doi:10.1002/cbic.202300864 · Cited by 6 · see citing works

Making tau amyloid models in vitro: a crucial and underestimated challenge

Broc, J., Piersson, C., & Fichou, Y. (2025) · FEBS Letters · doi:10.1002/1873-3468.70022 · Cited by 5 · see citing works

HAPLN2 forms aggregates and promotes microglial inflammation during brain aging in mice

Watanabe, A., Hirayama, S., Kominato, I., Marchese, S., Esposito, P., Metodieva, V., Kimura, T., Kameda, H., Sano, T., Takao, M., et al. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003006 · Cited by 7 · see citing works

U1‐70K and U1A and tau pathogenesis in demented and non‐demented individuals with Down syndrome

Perez, S. E., Miguel, J. C., Nadeem, M., Malek‐Ahmadi, M. H., Hales, C. M., Head, E., & Mufson, E. J. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70474 · Cited by 2 · see citing works

Similarities among Alzheimer's Disease, Parkinson's Disease and Dementia may Call for a Similar Treatment

Ashok, C., & Anil, D. (2022) · Journal of Neurodegenerative Disorders · doi:10.36959/459/608 · Cited by 1 · see citing works

U2-2 snRNA Mutations Alter the TranscriptomePreprint

Chi, Z., Gupta, V., & Query, C. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.12.642709 · Cited by 1 · see citing works

RNA Interference Therapeutics and Human Diseases

Sharma, D., Singh, S. N., & Chand, T. (2017) · IGI Global eBooks · doi:10.4018/978-1-5225-2255-3.ch042

Multi-omics analysis of human brain tissue and an animal model of Parkinson’s Disease

Gomes, L. C. (2020) · doi:10.53846/goediss-7812

Emerging role of RNA-binding proteins in sporadic and rapid progressive Alzheimer’s disease

Younas, N. (2020) · doi:10.53846/goediss-7836

Genetic regulators of stress-induced RNA mis-splicing in Caenorhabditis elegans

Chomyshen, S. C. (2021) · HARVEST (University of Saskatchewan)

RNA Interference Therapeutics and Human Diseases

Sharma, D., Singh, S. N., & Chand, T. (2018) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-5225-7489-7.ch006

Expression and Purification of Human U1‐70K (snRNP70) and its BAD Domains Using an E. coli Expression System

Paul, T. M., Jamal, S., Ekpenyong, E., Prevelige, P. E., Fargason, T., Zhang, Z., & Zhang, J. (2024) · Current Protocols · doi:10.1002/cpz1.1059

NAD + - and EVA1-C-dependent reversal of neurological deficits is mediated by differential alternative RNA splicing in tauopathic animal modelsPreprint

Ai, R., Mao, L., Jin, X., Zhang, S., Pan, J., Lagartos-Donate, M. J., Cao, S., Yang, G., Xie, C., Kang, X., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.27.620478

Aggregation of HAPLN2, a component of the perinodal extracellular matrix, is a hallmark of physiological brain aging in micePreprint

Watanabe, A., Hirayama, S., Kominato, I., Marchese, S., Esposito, P., Metodieva, V., Kimura, T., Kameda, H., Sano, T., Takao, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.09.632092

The spliceosome component U1-70k loads nascent transcripts onto FVE/SGS3 via co-condensation to embark on RNA silencingPreprint

Oh, T., Liu, K., Li, N., Li, C., Zhong, S., Zhu, J., Laubinger, S., & Zhang, X. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.22.650084

Aβ Aggregates Bind the U1 Spliceosomal Ribonucleoprotein in Alzheimer Disease BrainPreprint

Tao, Y., Francis, A. E., Liu, W., Watkins, C., Bennett, D. A., Selkoe, D. J., Flynn, R. A., & Stern, A. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.02.729610

Fluorescence imaging-based investigation of tau-mediated promotion of U1 small nuclear ribonucleoprotein 70 kDa co-phase separation

Peng, B., Zou, S., Shi, Y., Zhu, X., Liu, M., Li, H., & Zhang, Y. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153818

Bacopa monnieri attenuates Alzheimer's pathology by modulating RNA metabolism, cellular stress responses, and Rho GTPase signaling: Phosphoproteomic insights from a cellular model of Alzheimer's disease

Palollathil, A., Najar, M. A., Pervaje, R., Raju, R., Prasad, T. S. K., & Modi, P. K. (2026) · Neurochemistry International · doi:10.1016/j.neuint.2026.106268

Investigating the aggregation of Alzheimer’s disease-associated proteins in S. cerevisiae

Denniss, J. M. (2019) · SMARTech Repository (Georgia Institute of Technology)

An Intrinsically Disordered Low Complexity Domain is Required for U1‐70K Self‐association

Bishof, I., Diner, I., & Seyfried, N. T. (2015) · The FASEB Journal · doi:10.1096/fasebj.29.1_supplement.712.3 · Cited by 1 · see citing works

O2‐02‐05: RNA‐BINDING PROTEINS WITH MIXED CHARGE DOMAINS SELF‐ASSEMBLE AND AGGREGATE IN ALZHEIMER'S DISEASE

Bishof, I., Dammer, E. B., Duong, D. M., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.06.2649

Aβ Aggregates Bind the U1 Spliceosomal Ribonucleoprotein in Alzheimer Disease BrainPreprint

Tao, Y., Francis, A. E., Liu, W., Watkins, C., Bennett, D. A., Selkoe, D. J., Flynn, R. A., & Stern, A. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.02.729610

RNA-binding proteins with basic-acidic dipeptide (BAD) domains self-assemble and aggregate in Alzheimer's disease

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