Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890 · 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

Biomolecular condensates: organizers of cellular biochemistry

Banani, S. F., Lee, H. O., Hyman, A., & Rosen, M. (2017) · Nature reviews. Molecular cell biology · doi:10.1038/nrm.2017.7 · Cited by 5,574 · see citing works

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · see citing works

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,658 · see citing works

Phase transitions in the assembly of multivalent signalling proteins

Li, P., Banjade, S., Cheng, H., Kim, S., Chen, B., Guo, L., Llaguno, M. C., Hollingsworth, J. V., King, D., Banani, S. F., et al. (2012) · Nature · doi:10.1038/nature10879 · Cited by 2,565 · see citing works

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · see citing works

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works

Decoding ALS: from genes to mechanism

Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,047 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · see citing works

Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles

Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803 · see citing works

Coexisting liquid phases underlie nucleolar sub-compartments

Feric, M., Vaidya, N., Harmon, T., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R., Pappu, R., & Brangwynne, C. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,798 · see citing works

Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins

Lin, Y., Protter, D. S. W., Rosen, M. K., & Parker, R. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.018 · Cited by 1,594 · see citing works

Object recognition test in mice

Leger, M., Quiedeville, A., Bouet, V., Haelewyn, B., Boulouard, M., Schumann-Bard, P., & Freret, T. (2013) · Nature Protocols · doi:10.1038/nprot.2013.155 · Cited by 1,357 · see citing works

Compositional Control of Phase-Separated Cellular Bodies

Banani, S. F., Rice, A. M., Peeples, W. B., Lin, Y., Jain, S., Parker, R., & Rosen, M. K. (2016) · Cell · doi:10.1016/j.cell.2016.06.010 · Cited by 1,257 · see citing works

Stress granules: the Tao of RNA triage.

Anderson, P., & Kedersha, N. (2008) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2007.12.003 · Cited by 1,156 · see citing works

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works

Stress granules as crucibles of ALS pathogenesis

Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 913 · see citing works

RNA phase transitions in repeat expansion disorders

(2017) · doi:10.1038/nature22386 · Cited by 911 · see citing works

The neurobiological basis of spontaneous alternation

Lalonde, R. (2002) · Neuroscience & Biobehavioral Reviews · doi:10.1016/s0149-7634(01)00041-0 · Cited by 842 · see citing works

The genetics of myelodysplastic syndrome: from clonal haematopoiesis to secondary leukaemia

Sperling, A. S., Gibson, C. J., & Ebert, B. L. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.112 · Cited by 676 · see citing works

Assessing rodent hippocampal involvement in the novel object recognition task. A review

Cohen, S. J., & Stackman, R. W. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.08.002 · Cited by 592 · see citing works

Caspase activation precedes and leads to tangles

de Calignon, A., Fox, L. M., Pitstick, R., Carlson, G. A., Bacskai, B. J., Spires-Jones, T. L., & Hyman, B. T. (2010) · Nature · doi:10.1038/nature08890 · Cited by 517 · see citing works

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

Berger, Z., Roder, H. M., Hanna, A., Carlson, A. M., Rangachari, V., Yue, M., Wszołek, Z. K., Ashe, K. H., Knight, J. A., Dickson, D. W., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 485 · see citing works

Mechanistic insights into mammalian stress granule dynamics

Panas, M. D., Ivanov, P. V., & Anderson, P. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609081 · Cited by 374 · see citing works

Interaction 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

Regulated protein aggregation: stress granules and neurodegeneration

Wolozin, B. L. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-56 · Cited by 338 · see citing works

C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease

Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V. L., Berry, R. W., Kuret, J., & Binder, L. I. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3737 · Cited by 326 · see citing works

RNA stores tau reversibly in complex coacervates

Zhang, X., Lin, Y., Eschmann, N. A., Zhou, H., Rauch, J. N., Hernández, I., Guzman, E., Kosik, K. S., & Han, S. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2002183 · Cited by 308 · see citing works

Lost after translation: missorting of Tau protein and consequences for Alzheimer disease

Zempel, H., & Mandelkow�, E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.08.004 · Cited by 272 · see citing works

Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine

Irwin, D. J., Cairns, N. J., Grossman, M., McMillan, C. T., Lee, E. B., Deerlin, V. M. V., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1380-1 · Cited by 262 · see citing works

P301S Mutant Human Tau Transgenic Mice Manifest Early Symptoms of Human Tauopathies with Dementia and Altered Sensorimotor Gating

Takeuchi, H., Iba, M., Inoue, H., Higuchi, M., Takao, K., Tsukita, K., Karatsu, Y., Iwamoto, Y., Miyakawa, T., Suhara, T., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021050 · Cited by 247 · see citing works

Contrasting Pathology of the Stress Granule Proteins TIA-1 and G3BP in Tauopathies

Vanderweyde, T. E., Yu, W. H., Varnum, M. M., Liu‐Yesucevitz, L., Citro, A., Ikezu, T., Duff, K., & Wolozin, B. L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1592-12.2012 · Cited by 235 · see citing works

Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor α, cyclooxygenase 2, and inflammatory arthritis

Phillips, K., Kedersha, N., Shen, L., Blackshear, P. J., & Anderson, P. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400148101 · Cited by 199 · see citing works

Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo

Kuchibhotla, K. V., Wegmann, S., Kopeikina, K. J., Hawkes, J., Rudinskiy, N., Andermann, M. L., Spires-Jones, T. L., Bacskai, B. J., & Hyman, B. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318807111 · Cited by 193 · see citing works

Pathological tau promotes neuronal damage by impairing ribosomal function and decreasing protein synthesis

Meier, S., Bell, M., Lyons, D. N., Rodriguez-Rivera, J., Ingram, A., Fontaine, S. N., Mechas, E., Chen, J., Wolozin, B., LeVine, H., et al. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.3029-15.2016 · Cited by 190 · see citing works

Structural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs

Rocher, A. B., Crimins, J. L., Amatrudo, J. M., Kinson, M. S., Todd-Brown, M. A., Lewis, J., & Luebke, J. I. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.029 · Cited by 187 · see citing works

RNA Protein Interaction in Neurons

Darnell, R. B. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062912-114322 · Cited by 181 · see citing works

RNA-binding proteins with prion-like domains in ALS and FTLD-U

Gitler, A. D., & Shorter, J. (2011) · Prion · doi:10.4161/pri.5.3.17230 · Cited by 161 · see citing works

Dysregulation of RNA Binding Protein Aggregation in Neurodegenerative Disorders

Maziuk, B. F., Ballance, H. I., & Wolozin, B. L. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00089 · Cited by 144 · see citing works

Pathological stress granules in Alzheimer’s disease

Ash, P. E. A., Vanderweyde, T. E., Youmans, K. L., Apicco, D. J., & Wolozin, B. (2014) · Brain Research · doi:10.1016/j.brainres.2014.05.052 · Cited by 129 · see citing works

Site-specific Phosphorylation and Caspase Cleavage Differentially Impact Tau-Microtubule Interactions and Tau Aggregation

Ding, H., Matthews, T. A., & Johnson, G. V. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511697200 · Cited by 114 · see citing works

Characteristics of TBS-Extractable Hyperphosphorylated Tau Species: Aggregation Intermediates in rTg4510 Mouse Brain

Sahara, N., Deture, M. A., Ren, Y., Ebrahim, A.-S., Kang, D., Knight, J. A., Volbracht, C., Pedersen, J. T., Dickson, D. W., Yen, S.-H. C., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121093 · Cited by 107 · see citing works

Pathological conformations involving the amino terminus of tau occur early in Alzheimer's disease and are differentially detected by monoclonal antibodies

Combs, B., Hamel, C., & Kanaan, N. M. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.016 · Cited by 86 · see citing works

Internalized Tau sensitizes cells to stress by promoting formation and stability of stress granules

Brunello, C. A., Yan, X., & Huttunen, H. J. (2016) · Scientific Reports · doi:10.1038/srep30498 · Cited by 83 · see citing works

Protein Phase Separation: A New Phase in Cell Biology

Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 1,954 · see citing works

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing

Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,137 · 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

Converging pathways in neurodegeneration, from genetics to mechanisms

Gan, L., Cookson, M. R., Petrucelli, L., & Spada, A. R. L. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0237-7 · Cited by 475 · see citing works

Stress Granule Assembly Disrupts Nucleocytoplasmic Transport

Zhang, K., Daigle, J. G., Cunningham, K. M., Coyne, A. N., Ruan, K., Grima, J. C., Bowen, K., Wadhwa, H., Yang, P., Rigo, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.025 · Cited by 423 · see citing works

Liquid-liquid phase separation induces pathogenic tau conformations in vitro

Kanaan, N. M., Hamel, C., Grabinski, T., & Combs, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16580-3 · Cited by 397 · see citing works

Selective removal of astrocytic APOE4 strongly protects against tau-mediated neurodegeneration and decreases synaptic phagocytosis by microglia

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

Mechanisms of secretion and spreading of pathological tau protein

Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304 · see citing works

Small-Molecule Modulation of TDP-43 Recruitment to Stress Granules Prevents Persistent TDP-43 Accumulation in ALS/FTD

Fang, M. Y., Markmiller, S., Vu, A. Q., Javaherian, A., Dowdle, W. E., Jolivet, P., Bushway, P., Castello, N. A., Baral, A., Chan, M. Y., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.05.048 · Cited by 289 · see citing works

Alzheimer’s disease brain-derived extracellular vesicles spread tau pathology in interneurons

Ruan, Z., Pathak, D., Venkatesan Kalavai, S., Yoshii-Kitahara, A., Muraoka, S., Bhatt, N., Takamatsu-Yukawa, K., Hu, J., Wang, Y., Hersh, S., et al. (2021) · Brain · doi:10.1093/brain/awaa376 · Cited by 283 · see citing works

Disruption of RNA Metabolism in Neurological Diseases and Emerging Therapeutic Interventions

Nussbacher, J. K., Tabet, R., Yeo, G. W.-M., & Lagier‐Tourenne, C. (2019) · Neuron · doi:10.1016/j.neuron.2019.03.014 · Cited by 264 · see citing works

Tau: Enabler of diverse brain disorders and target of rapidly evolving therapeutic strategies

Chang, C.-W., Shao, E., & Mucke, L. (2021) · Science · doi:10.1126/science.abb8255 · Cited by 263 · see citing works

Lysine/RNA-interactions drive and regulate biomolecular condensation

Ukmar, T., Hutten, S., Grieshop, M. P., Rezaei‐Ghaleh, N., Cima‐Omori, M., Biernat, J., Mandelkow�, E., Söding, J., Dormann, D., & Zweckstetter, M. (2019) · Nature Communications · doi:10.1038/s41467-019-10792-y · Cited by 250 · see citing works

Tau 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

Tau liquid‐liquid phase separation in neurodegenerative diseases

Boyko, S., & Surewicz, W. K. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.01.011 · Cited by 215 · see citing works

Selective Neuronal Vulnerability in Alzheimer’s Disease: A Network-Based Analysis

Roussarie, J.-P., Yao, V., Rodriguez-Rodriguez, P., Oughtred, R., Rust, J., Plautz, Z., Kasturia, S., Albornoz, C., Wang, W., Schmidt, E. F., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.010 · Cited by 180 · see citing works

Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy

Jiang, L., Lin, W., Zhang, C., Ash, P. E. A., Verma, M., Kwan, J., van Vliet, E., Yang, Z., Cruz, A. L., Boudeau, S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.038 · Cited by 177 · see citing works

The RNA-Binding Protein PUM2 Impairs Mitochondrial Dynamics and Mitophagy During Aging

D’Amico, D., Mottis, A., Potenza, F., Sorrentino, V., Li, H., Romani, M., Lemos, V., Schoonjans, K., Zamboni, N., Knott, G., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.034 · Cited by 159 · see citing works

TIA1 potentiates tau phase separation and promotes generation of toxic oligomeric tau

Ash, P. E. A., Lei, S., Shattuck, J., Boudeau, S., Carlomagno, Y., Medalla, M., Mashimo, B. L., Socorro, G., Al-Mohanna, L. F. A., Jiang, L., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014188118 · Cited by 159 · see citing works

Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrum

Baradaran‐Heravi, Y., Broeckhoven, C. V., & van der Zee, J. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104639 · Cited by 157 · 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

New Insights Into Drug Discovery Targeting Tau Protein

Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 133 · see citing works

Liquid–liquid phase separation of tau: From molecular biophysics to physiology and disease

Rai, S. K., Savastano, A., Singh, P., Mukhopadhyay, S., & Zweckstetter, M. (2021) · Protein Science · doi:10.1002/pro.4093 · Cited by 123 · see citing works

Dysregulation of autophagy and stress granule-related proteins in stress-driven Tau pathology

Silva, J. M., Rodrigues, S., Sampaio‐Marques, B., Gomes, P., Neves‐Carvalho, A., Dioli, C., Soares‐Cunha, C., Mazuik, B. F., Takashima, A., Ludovico, P., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0217-1 · Cited by 123 · see citing works

Tau drives translational selectivity by interacting with ribosomal proteins

Koren, S. A., Hamm, M. J., Meier, S. E., Weiss, B. E., Nation, G. K., Chishti, E. A., Arango, J. P., Chen, J., Zhu, H., Blalock, E. M., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01970-9 · Cited by 122 · see citing works

Zinc promotes liquid–liquid phase separation of tau protein

Singh, V. P., Xu, L., Boyko, S., Surewicz, K. A., & Surewicz, W. K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ac120.013166 · Cited by 120 · see citing works

Stress granule subtypes: an emerging link to neurodegeneration

Advani, V. M., & Ivanov, P. V. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03565-0 · Cited by 119 · see citing works

Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Corsi, A., Bombieri, C., Valenti, M. T., & Romanelli, M. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315383 · Cited by 118 · see citing works

Decreased synthesis of ribosomal proteins in tauopathy revealed by non‐canonical amino acid labelling

Evans, H. T., Benetatos, J., van Roijen, M., Bodea, L., & Götz, J. (2019) · The EMBO Journal · doi:10.15252/embj.2018101174 · Cited by 115 · see citing works

Tau interactome and RNA binding proteins in neurodegenerative diseases

Kavanagh, T., Halder, A., & Drummond, E. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00572-6 · Cited by 105 · see citing works

Amyloid, tau, pathogen infection and antimicrobial protection in Alzheimer’s disease –conformist, nonconformist, and realistic prospects for AD pathogenesis

Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0139-3 · Cited by 103 · see citing works

TIA1 regulates the generation and response to toxic tau oligomers

Jiang, L., Ash, P. E. A., Maziuk, B. F., Ballance, H. I., Boudeau, S., Abdullatif, A. A., Orlando, M., Petrucelli, L., Ikezu, T., & Wolozin, B. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1937-5 · Cited by 99 · see citing works

Chronic Sleep Disruption Advances the Temporal Progression of Tauopathy in P301S Mutant Mice

Zhu, Y., Zhan, G., Fenik, P., Brandes, M., Bell, P., François, N., Shulman, K., & Veasey, S. C. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0275-18.2018 · Cited by 106 · see citing works

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

Abskharon, R. N. N., Sawaya, M. R., Boyer, D. R., Cao, Q., Nguyen, B. A., Cascio, D., & Eisenberg, D. S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2119952119 · Cited by 97 · see citing works

Multifunctional Selenium Quantum Dots for the Treatment of Alzheimer’s Disease by Reducing Aβ-Neurotoxicity and Oxidative Stress and Alleviate Neuroinflammation

Guo, X., Lie, Q., Liu, Y., Zhi, J., Gong, Y., Yuan, X., & Liu, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c00690 · Cited by 94 · see citing works

Trilobatin rescues cognitive impairment of Alzheimer’s disease by targeting HMGB1 through mediating SIRT3/SOD2 signaling pathway

Gao, J.-M., Zhang, X., Shu, G., Chen, N., Zhang, J., Xu, F., Li, F., Liu, Y., Wei, Y., He, Y., et al. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00888-5 · Cited by 95 · 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

SFPQ 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 94 · see citing works

RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction

Montalbano, M., McAllen, S., Puangmalai, N., Sengupta, U., Bhatt, N. N., Johnson, O. D., Kharas, M. G., & Kayed, R. (2020) · Nature Communications · doi:10.1038/s41467-020-18022-6 · Cited by 86 · see citing works

Combating 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

Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies

Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 87 · see citing works

Myricetin slows liquid–liquid phase separation of Tau and activates ATG5-dependent autophagy to suppress Tau toxicity

Dai, B., Zhong, T., Chen, Z.-X., Chen, W., Zhang, N., Liu, X., Wang, L., Chen, J., & Liang, Y. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101222 · Cited by 83 · 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 79 · see citing works

Fyn Kinase Controls Tau Aggregation In Vivo

Briner, A., Götz, J., & Polanco, J. C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108045 · Cited by 80 · see citing works

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

Friend or foe: The role of stress granule in neurodegenerative disease

Cui, Q., Liu, Z., & Bai, G. (2024) · Neuron · doi:10.1016/j.neuron.2024.04.025 · Cited by 82 · see citing works

Zika Virus Subverts Stress Granules To Promote and Restrict Viral Gene Expression

Bonenfant, G., Williams, N., Netzband, R., Schwarz, M. C., Evans, M. J., & Pager, C. T. (2019) · Journal of Virology · doi:10.1128/jvi.00520-19 · Cited by 79 · see citing works

Ordered Assembly of Tau Protein and Neurodegeneration

Goedert, M., & Spillantini, M. G. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_1 · Cited by 71 · see citing works

RNAs, Phase Separation, and Membrane‐Less Organelles: Are Post‐Transcriptional Modifications Modulating Organelle Dynamics?

Drino, A., & Schaefer, M. (2018) · BioEssays · doi:10.1002/bies.201800085 · Cited by 72 · see citing works

Fyn kinase inhibition reduces protein aggregation, increases synapse density and improves memory in transgenic and traumatic Tauopathy

Tang, S. J., Fesharaki‐Zadeh, A., Takahashi, H., Nies, S. H., Smith, L. M., Luo, A., Chyung, A. S., Chiasseu, M., & Strittmatter, S. M. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00976-9 · Cited by 72 · see citing works

Altered ribosomal function and protein synthesis caused by tau

Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01208-4 · Cited by 70 · see citing works

Intracellular energy controls dynamics of stress-induced ribonucleoprotein granules

Wang, T., Tian, X., Kim, H. B., Jang, Y., Huang, Z., Na, C. H., & Wang, J. (2022) · Nature Communications · doi:10.1038/s41467-022-33079-1 · Cited by 67 · see citing works

Unraveling the Pathways to Neuronal Homeostasis and Disease: Mechanistic Insights into the Role of RNA-Binding Proteins and Associated Factors

Ravanidis, S., Kattan, F.-G., & Doxakis, E. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082280 · Cited by 65 · see citing works

FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments

Kaniyappan, S., Tepper, K., Biernat, J., Chandupatla, R., Hübschmann, S., Irsen, S. H., Bicher, S., Klatt, C., Mandelkow, E., & Mandelkow�, E. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00389-1 · Cited by 62 · see citing works

Liquid-liquid phase separation of protein tau: An emerging process in Alzheimer's disease pathogenesis

Ainani, H., Bouchmaa, N., Ben Mrid, R., & El Fatimy, R. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106011 · Cited by 54 · see citing works

Identification of circRNAs linked to Alzheimer's disease and related dementias

Puri, S., Hu, J., Sun, Z., Lin, M., Stein, T. D., Farrer, L. A., Wolozin, B. L., & Zhang, X. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.12960 · Cited by 54 · see citing works

Bond-selective intensity diffraction tomography

Zhao, J., Matlock, A. C., Zhu, H., Song, Z., Zhu, J., Wang, B., Chen, F., Zhan, Y., Chen, Z., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35329-8 · Cited by 50 · see citing works

USP10 is a critical factor for Tau-positive stress granule formation in neuronal cells

Piatnitskaia, S., Takahashi, M., Kitaura, H., Katsuragi, Y., Kakihana, T., Zhang, L., Kakita, A., Iwakura, Y., Nawa, H., Miura, T., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-47033-7 · Cited by 50 · see citing works

Zinc enhances liquid-liquid phase separation of Tau protein and aggravates mitochondrial damages in cells

Gao, Y., Zhong, T., Wang, L., Zhang, N., Zeng, Y., Hu, J.-Y., Dang, H.-B., Chen, J., & Liang, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.04.034 · Cited by 49 · see citing works

A new andrographolide derivative ADA targeting SIRT3-FOXO3a signaling mitigates cognitive impairment by activating mitophagy and inhibiting neuroinflammation in Apoe4 mice

Zhou, Y., Zhao, Q., Zhang, Y., Di, L., Feng, X., Xu, W., Gao, W.-P., Guo, Y., He, Y., Kou, J., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155298 · Cited by 46 · see citing works

Tau oligomers mediate aggregation of RNA‐binding proteins Musashi1 and Musashi2 inducing Lamin alteration

Montalbano, M., McAllen, S., Sengupta, U., Puangmalai, N., Bhatt, N. N., Ellsworth, A., & Kayed, R. (2019) · Aging Cell · doi:10.1111/acel.13035 · Cited by 45 · see citing works

Cannabinoid receptor CB2 ablation protects against TAU induced neurodegeneration

Galán-Ganga, M., Rodríguez‐Cueto, C., Merchán‐Rubira, J., Hernández, F., Ávila, J., Posada-Ayala, M., Lanciego, J. L., Luengo, E., López, M. G., Rábano, A., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01196-5 · Cited by 44 · 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

Pathophysiology of stress granules: An emerging link to diseases (Review)

Wang, J., Gan, Y., Cao, J. P., Dong, X.-F., & Ouyang, W. (2022) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2022.5099 · Cited by 43 · see citing works

Formation of Toxic Oligomeric Assemblies of RNA-binding Protein: Musashi in Alzheimer’s disease

Sengupta, U., Montalbano, M., McAllen, S., Minuesa, G., Kharas, M. G., & Kayed, R. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0615-0 · Cited by 43 · see citing works

Tau-mediated dysregulation of RNA: Evidence for a common molecular mechanism of toxicity in frontotemporal dementia and other tauopathies

Koren, S. A., Escobar, S. M. G., & Abisambra, J. F. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104939 · Cited by 43 · see citing works

Tau–RNA complexes inhibit microtubule polymerization and drive disease-relevant conformation change

McMillan, P. J., Benbow, S. J., Uhrich, R. L., Saxton, A. D., Baum, M., Strovas, T. J., Wheeler, J. M., Baker, J. D., Liachko, N. F., Keene, C. D., et al. (2023) · Brain · doi:10.1093/brain/awad032 · Cited by 41 · see citing works

Stress and the Etiopathogenesis of Alzheimer's Disease and Depression.

Sotiropoulos, I., Silva, J., Gomes, P. A., Sousa, N., & Almeida, O. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-32-9358-8_20 · Cited by 33 · see citing works

Exosomal and vesicle‐free tau seeds—propagation and convergence in endolysosomal permeabilization

Polanco, J. C., & Götz, J. (2021) · FEBS Journal · doi:10.1111/febs.16055 · Cited by 43 · see citing works

The Pathophysiology of Tau and Stress Granules in Disease

Cruz, A. L., Verma, M., & Wolozin, B. L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_26 · Cited by 40 · see citing works

The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation

Webber, C. J., Lei, S. (., & Wolozin, B. L. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.04.021 · Cited by 41 · see citing works

Tau secretion and propagation: Perspectives for potential preventive interventions in Alzheimer's disease and other tauopathies

Annadurai, N., Sanctis, J. B. D., Hajdúch, M., & Das, V. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113756 · Cited by 41 · see citing works

Emerging Roles of RNA-Binding Proteins in Neurodevelopment

Parra, A. S., & Johnston, C. A. (2022) · Journal of Developmental Biology · doi:10.3390/jdb10020023 · Cited by 41 · see citing works

RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding

Zacco, E., Broglia, L., Kurihara, M., Monti, M. M., Gustincich, S., Pastore, A., Plath, K., Nagakawa, S., Cerase, A., de Groot, N. S., et al. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00575 · Cited by 40 · see citing works

Single cell transcriptomic profiling of a neuron-astrocyte assembloid tauopathy model

Rickner, H., Jiang, L., Hong, R., O’Neill, N. K., Mojica, C. A., Snyder, B. J., Zhang, L., Shaw, D., Medalla, M., Wolozin, B. L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34005-1 · Cited by 41 · see citing works

Cytosolic condensates rich in polyserine define subcellular sites of tau aggregation

Lester, E., Alstyne, M. V., McCann, K. L., Reddy, S., Cheng, L. Y., Kuo, J., Pratt, J., & Parker, R. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217759120 · Cited by 37 · see citing works

Disrupting pathologic phase transitions in neurodegeneration

Hurtle, B. T., Xie, L., & Donnelly, C. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168549 · Cited by 39 · see citing works

Reduction of the RNA Binding Protein TIA1 Exacerbates Neuroinflammation in Tauopathy

LeBlang, C. J., Medalla, M., Nicoletti, N. W., Hays, E. C., Zhao, J., Shattuck, J. E., Cruz, A. L., Wolozin, B. L., & Luebke, J. I. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00285 · Cited by 38 · see citing works

Biomolecular condensation of the microtubule-associated protein tau

Ukmar, T., Wegmann, S., & Zweckstetter, M. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.06.007 · Cited by 39 · see citing works

Mechanisms and regulation underlying membraneless organelle plasticity control

Ismail, H., Liu, X., Yang, F., Li, J., Zahid, A., Dou, Z., Liu, X., & Yao, X. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab028 · Cited by 39 · see citing works

DrosophilaTau Negatively Regulates Translation and Olfactory Long-Term Memory, But Facilitates Footshock Habituation and Cytoskeletal Homeostasis

Papanikolopoulou, K., Roussou, I. G., Gouzi, J. Y., Samiotaki, M. K., Panayotou, G., Turin, L., & Skoulakis, E. M. C. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.0391-19.2019 · Cited by 37 · see citing works

Age‐related neurodegenerative diseases

Duggan, M. R., Torkzaban, B., Ahooyi, T. M., Khalili, K., & Gordon, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29248 · Cited by 37 · see citing works

Loganin alleviated cognitive impairment in 3×Tg-AD mice through promoting mitophagy mediated by optineurin

Zhou, Y., Luo, D., Shi, J.-Z., Yang, X., Xu, W., Gao, W.-P., Guo, Y., Zhao, Q., Xie, X., He, Y., et al. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116455 · Cited by 35 · see citing works

Where Dopaminergic and Cholinergic Systems Interact: A Gateway for Tuning Neurodegenerative Disorders

Amalric, M., Pattij, T., Sotiropoulos, I., Silva, J. M., Sousa, N., Ztaou, S., Chiamulera, C., Wahlberg, L. U., Emerich, D. F., & Paolone, G. (2021) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2021.661973 · Cited by 35 · see citing works

Stress granules: emerging players in neurodegenerative diseases

Yuan, L., Mao, L.-H., Huang, Y.-Y., Outeiro, T. F., Li, W., Vieira, T. C. R. G., & Li, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00482-9 · Cited by 36 · see citing works

Saturated fatty acids entrap PDX1 in stress granules and impede islet beta cell function

Zhang, M., Yang, C., Zhu, M., Li, Q., Luo, Y., Cheng, H., Geng, R., Xu, X., Cheng, Q., & Liu, Y. (2021) · Diabetologia · doi:10.1007/s00125-021-05389-4 · Cited by 34 · see citing works

Liquid-liquid phase separation in Alzheimer’s disease

Fu, Q., Zhang, B., Chen, X., & Chu, L. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02407-3 · Cited by 33 · see citing works

Neuronal biomolecular condensates and their implications in neurodegenerative diseases

Nam, J., & Gwon, Y. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1145420 · Cited by 32 · see citing works

Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation

Wang, C., Terrigno, M., Li, J., Distler, T., Pandya, N. J., Ebeling, M., Tyanova, S., Hoozemans, J. J. M., Dijkstra, A. A., Fuchs, L., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.05.033 · Cited by 34 · see citing works

RNA G-quadruplexes and calcium ions synergistically induce Tau phase transition in vitro

Yabuki, Y., Matsuo, K., Komiya, G., Kudo, K., Hori, K., Ikenoshita, S., Kawata, Y., Mizobata, T., & Shioda, N. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107971 · Cited by 33 · see citing works

Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective Responses

Verde, E. M., Secco, V., Ghezzi, A., Mandrioli, J., & Carra, S. (2025) · Cells · doi:10.3390/cells14100680 · Cited by 32 · see citing works

Reduced progranulin increases tau and α-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase

Takahashi, H., Bhagwagar, S. Z., Nies, S. H., Ye, H., Han, X., Chiasseu, M., Wang, G., Mackenzie, I. R., & Strittmatter, S. M. (2024) · Nature Communications · doi:10.1038/s41467-024-45692-3 · Cited by 32 · see citing works

Translational control in brain pathologies: biological significance and therapeutic opportunities

Delaidelli, A., Jan, A., Herms, J. W., & Sorensen, P. H. B. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01971-8 · Cited by 30 · see citing works

Selective neuronal vulnerability in Alzheimer’s disease: a network-based analysisPreprint

Roussarie, J.-P., Yao, V., Plautz, Z., Kasturia, S. E., Albornoz, C. A., Schmidt, E. F., Brichta, L., Barnea-Cramer, A. O., Heintz, N., Hof, P. R., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/499897 · Cited by 31 · see citing works

Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications

Li, P., Chen, J., Wang, X., Su, Z., Gao, M., & Huang, Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106167 · Cited by 30 · see citing works

Connecting the dots: Neuronal senescence, stress granules, and neurodegeneration

Ma, Y., & Farny, N. G. (2023) · Gene · doi:10.1016/j.gene.2023.147437 · Cited by 30 · see citing works

New roles for the de-ubiquitylating enzyme OTUD4 in an RNA-protein network and RNA granules

Das, R., Schwintzer, L., Vinopal, S., Roca, E. A., Sylvester, M., Oprişoreanu, A., Schoch, S., Bradke, F., & Broemer, M. (2019) · Journal of Cell Science · doi:10.1242/jcs.229252 · Cited by 30 · see citing works

Tau Oligomers and Fibrils Exhibit Differential Patterns of Seeding and Association With RNA Binding Proteins

Jiang, L., Zhao, J., Cheng, J., & Wolozin, B. L. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.579434 · Cited by 30 · see citing works

Early alterations of neurovascular unit in the retina in mouse models of tauopathy

Xia, F., Ha, Y., Shi, S., Li, Y., Li, S., Luisi, J. D., Kayed, R., Motamedi, M., Liu, H., & Zhang, W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01149-y · Cited by 30 · see citing works

A reduction in the RNA binding protein TIA1 protects against neurodegeneration, rescues behavioral deficits and prolongs survival

Randhawa, A. (2018) · OpenBU (Boston University)

[O2–03–03]: TAU‐INDUCED NEURODEGENERATION IS MEDIATED BY RNA BINDING PROTEINS

Wolozin, B. L., Apicco, D. J., Zhang, C., Ash, P. E. A., Maziuk, B. F., Abdullatif, A. A., Ballance, H. I., Goldberg, L. R., Yazdani, N., Ung, C. Y., et al. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.07.157

TIA1 regulates the generation and response to toxic tau oligomers

Jiang, L., Ash, P. E. A., Maziuk, B. F., Ballance, H. I., Boudeau, S., Abdullatif, A. A., Orlando, M., Petrucelli, L., Ikezu, T., & Wolozin, B. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1937-5 · Cited by 99 · see citing works

Modulation of neuroinflammation and tauopathy by RNA-binding protein TIA1 in the P301S mouse model of tauopathy

LeBlang, C. J. (2020) · OpenBU (Boston University)

Interaction 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