Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 1× · 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

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works

Intrinsically disordered proteins in cellular signalling and regulation

Wright, P. E., & Dyson, H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3920 · Cited by 2,371 · 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

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works

Profound Loss of Layer II Entorhinal Cortex Neurons Occurs in Very Mild Alzheimer’s Disease

Gómez-Isla, T., Price, J. L., McKeel Jr., D. W., Morris, J. C., Growdon, J. H., & Hyman, B. T. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-14-04491.1996 · Cited by 1,796 · cited 1× · see citing works

Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works

The molecular architecture of the nuclear pore complex

Alber, F., Dokudovskaya, S., Veenhoff, L. M., Zhang, W., Kipper, J., Devos, D. P., Suprapto, A., Karni-Schmidt, O., Williams, R., Chait, B. T., et al. (2007) · Nature · doi:10.1038/nature06405 · Cited by 1,059 · see citing works

Aβ42‐driven cerebral amyloidosis in transgenic mice reveals early and robust pathology

Radde, R., Bolmont, T., Kaeser, S. A., Coomaraswamy, J., Lindau, D., Stoltze, L., Calhoun, M. E., Jäggi, F., Wolburg, H., Gengler, S., et al. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400784 · Cited by 986 · see citing works

The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.

Zhang, K., Donnelly, C. J., Haeusler, A. R., Grima, J. C., Machamer, J. B., Steinwald, P., Daley, E. L., Miller, S. J., Cunningham, K. M., Vidensky, S., et al. (2015) · Nature · doi:10.1038/nature14973 · Cited by 982 · see citing works

TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease

Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916 · see citing works

GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport

Freibaum, B. D., Lu, Y., Lopez-Gonzalez, R., Kim, N. C., Almeida, S., Lee, K.-H., Badders, N., Valentine, M., Miller, B. L., Wong, P. C., et al. (2015) · Nature · doi:10.1038/nature14974 · Cited by 841 · see citing works

Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.

Mertens, J., Paquola, A. C. M., Ku, M., Hatch, E., Böhnke, L., Ladjevardi, S., McGrath, S., Campbell, B., Lee, H., Herdy, J. R., et al. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2015.09.001 · Cited by 765 · see citing works

REST and stress resistance in ageing and Alzheimer’s disease

Lu, T., Aron, L., Zullo, J., Pan, Y., Kim, H., Chen, Y., Yang, T.-H., Kim, H., Drake, D., Liu, X., et al. (2014) · Nature · doi:10.1038/nature13163 · Cited by 760 · see citing works

FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties

Frey, S., Richter, R. P., & Görlich, D. (2006) · Science · doi:10.1126/science.1132516 · Cited by 691 · see citing works

The Nuclear Pore Complex and Nuclear TransportPreprint

Wente, S. R., & Rout, M. P. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000562 · Cited by 688 · see citing works

Regulating Access to the Genome

Weis, K. (2003) · Cell · doi:10.1016/s0092-8674(03)00082-5 · Cited by 668 · see citing works

Disturbance of Nuclear and Cytoplasmic TAR DNA-binding Protein (TDP-43) Induces Disease-like Redistribution, Sequestration, and Aggregate Formation

Winton, M. J., Igaz, L. M., Wong, M. M., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800342200 · Cited by 660 · see citing works

Hyperphosphorylation of Microtubule-Associated Protein Tau: A Promising Therapeutic Target for Alzheimer Disease

Gong, C., & Iqbal, K. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909111 · Cited by 649 · see citing works

Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS

Jovičić, A., Mertens, J., Boeynaems, S., Bogaert, E., Chai, N., Yamada, S. B., Paul, J. W., Sun, S., Herdy, J. R., Bieri, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4085 · Cited by 598 · see citing works

TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD

Chou, C., Zhang, Y., Umoh, M. E., Vaughan, S. W., Lorenzini, I., Liu, F., Sayegh, M., Donlin-Asp, P., Chen, Y. H., Duong, D. M., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0047-3 · Cited by 583 · see citing works

A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes

Frey, S., & Görlich, D. (2007) · Cell · doi:10.1016/j.cell.2007.06.024 · Cited by 570 · see citing works

Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.

D'Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. W. (2009) · Cell · doi:10.1016/j.cell.2008.11.037 · Cited by 565 · see citing works

RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01386-5 · Cited by 548 · see citing works

Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy

DeVos, S. L., Miller, R. L., Schoch, K. M., Holmes, B. B., Kebodeaux, C. S., Wegener, A. J., Chen, G., Shen, T., Tran, H., Nichols, B., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aag0481 · Cited by 516 · see citing works

Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded

Denning, D. P., Patel, S. S., Uversky, V. N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437902100 · Cited by 503 · see citing works

OPTIMIZING LONG INTRINSIC DISORDER PREDICTORS WITH PROTEIN EVOLUTIONARY INFORMATION

PENG, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., Dunker, A. K., & Zoran Obradovic, A. (2005) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720005000886 · Cited by 497 · see citing works

Mapping the dynamic organization of the nuclear pore complex inside single living cells

Rabut, G. E. E., Doye, V., & Ellenberg, J. (2004) · Nature Cell Biology · doi:10.1038/ncb1184 · Cited by 476 · see citing works

Simple rules for passive diffusion through the nuclear pore complex

Timney, B. L., Raveh, B., Mironska, R., Trivedi, J. M., Kim, S. J., Russel, D., Wente, S. R., Šali, A., & Rout, M. P. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201601004 · Cited by 461 · see citing works

Predicting intrinsic disorder from amino acid sequence

Zoran Obradovic, A., Peng, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., & Dunker, A. K. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10532 · Cited by 455 · see citing works

Architecture and design of the nuclear pore complex

Hinshaw, J. E., Carragher, B. O., & Milligan, R. A. (1992) · Cell · doi:10.1016/0092-8674(92)90635-p · Cited by 454 · 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

Nuclear Tau, a Key Player in Neuronal DNA Protection

Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · cited 1× · see citing works

Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

Woerner, A. C., Frottin, F., Hornburg, D., Feng, L., Meissner, F., Patra, M., Tatzelt, J., Mann, M., Winklhofer, K. F., Hartl, F. U., et al. (2015) · Science · doi:10.1126/science.aad2033 · Cited by 386 · see citing works

Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer’s disease brain

Takeda, S., Wegmann, S., Cho, H., DeVos, S. L., Commins, C., Roe, A. D., Nicholls, S. B., Carlson, G. A., Pitstick, R., Nobuhara, C. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms9490 · Cited by 371 · see citing works

Mutant Huntingtin Disrupts the Nuclear Pore Complex

Grima, J. C., Daigle, J. G., Arbez, N., Cunningham, K. M., Zhang, K., Ochaba, J., Smith-Geater, C., Morozko, E. L., Stocksdale, J. T., Glatzer, J. C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.023 · Cited by 358 · see citing works

Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity

Schmidt, H. B., & Görlich, D. (2014) · eLife · doi:10.7554/elife.04251 · Cited by 351 · 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

Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance

Cook, C. N., Carlomagno, Y., Gendron, T. F., Dunmore, J. H., Scheffel, K., Stetler, C. T., Davis, M., Dickson, D. W., Jarpe, M. B., Deture, M. A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 309 · see citing works

Missorting of Tau in Neurons Causes Degeneration of Synapses That Can Be Rescued by the Kinase MARK2/Par-1

Thies, E., & Mandelkow, E.-M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4674-06.2007 · Cited by 293 · see citing works

A major role for Tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic conditions

Violet, M., Delattre, L., Tardivel, M., Sultan, A., Chauderlier, A., Caillierez, R., Talahari, S., Nesslany, F., Lefebvre, B., Bonnefoy, E., et al. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00084 · Cited by 251 · see citing works

Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells

Dultz, E., Zanin, E., Wurzenberger, C., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707026 · Cited by 249 · see citing works

Single-molecule transport across an individual biomimetic nuclear pore complex

Kowalczyk, S. W., Kapinos, L. E., Blosser, T. R., et al. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2011.88 · Cited by 238 · see citing works

Huntington's disease is a four-repeat tauopathy with tau nuclear rods

Fernández-Nogales, M., Cabrera, J. R., Santos-Galindo, M., Hoozemans, J. J. M., Ferrer, I., Rozemuller, A. J. M., Hernández, F., Avila, J., & Lucas, J. J. (2014) · Nature Medicine · doi:10.1038/nm.3617 · Cited by 231 · see citing works

Polyglutamine-Expanded Huntingtin Exacerbates Age-Related Disruption of Nuclear Integrity and Nucleocytoplasmic Transport

Gasset-Rosa, F., Chillón-Marinas, C., Goginashvili, A., Atwal, R. S., Artates, J. W., Tabet, R., Wheeler, V. C., Bang, A. G., Cleveland, D. W., & Lagier‐Tourenne, C. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.027 · Cited by 231 · see citing works

The Vertebrate GLFG Nucleoporin, Nup98, Is an Essential Component of Multiple RNA Export Pathways

Powers, M. A., Forbes, D. J., Dahlberg, J. E., & Lund, E. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.2.241 · Cited by 224 · see citing works

The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly

Hetzer, M. W., Gruß, O. J., & Mattaj, I. W. (2002) · Nature Cell Biology · doi:10.1038/ncb0702-e177 · Cited by 221 · see citing works

Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration

Li, X., Kumar, Y., Zempel, H., Mandelkow, E., Biernat, J., & Mandelkow, E. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.376 · Cited by 218 · see citing works

Identification of nuclear tau isoforms in human neuroblastoma cells.

Loomis, P. A., Howard, T. H., Castleberry, R. P., & Binder, L. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8422 · Cited by 217 · see citing works

Systematic analysis of barrier‐forming FG hydrogels from Xenopus nuclear pore complexes

Labokha, A. A., Gradmann, S., Frey, S., Hülsmann, B. B., Urlaub, H., Baldus, M., & Görlich, D. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.302 · Cited by 213 · see citing works

The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush

Wegmann, S., Medalsy, I. D., Mandelkow�, E., & Müller, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212100110 · Cited by 196 · see citing works

In Vivo Formation of Vacuolated Multi-phase Compartments Lacking Membranes

Schmidt, H. B., & Rohatgi, R. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.088 · Cited by 178 · see citing works

A G protein involved in nucleocytoplasmic transport: the role of Ran

Moore, M. S., & Blobel, G. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90024-8 · Cited by 158 · see citing works

Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes

Lénárt, P., Rabut, G. E. E., Daigle, N., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211076 · Cited by 153 · see citing works

Oligomer Formation of Tau Protein Hyperphosphorylated in Cells

Tepper, K., Biernat, J., Kumar, S., Wegmann, S., Timm, T., Hübschmann, S., Redecke, L., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611368 · Cited by 151 · see citing works

FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

Mair, W., Muntel, J., Tepper, K., Tang, S., Biernat, J., Seeley, W. W., Kosik, K. S., Mandelkow�, E., Steen, H., & Steen, J. A. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04509 · Cited by 144 · 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

Understanding the Kinetic Roles of the Inducer Heparin and of Rod-like Protofibrils during Amyloid Fibril Formation by Tau Protein

Ramachandran, G., & Udgaonkar, J. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.271874 · Cited by 140 · see citing works

Mutated nup62 causes autosomal recessive infantile bilateral striatal necrosis

Basel‐Vanagaite, L., Muncher, L., Straussberg, R., Pasmanik‐Chor, M., Yahav, M., Rainshtein, L., Walsh, C. A., Magal, N., Taub, E., Drasinover, V., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20902 · Cited by 133 · see citing works

Karyopherin-Centric Control of Nuclear Pores Based on Molecular Occupancy and Kinetic Analysis of Multivalent Binding with FG Nucleoporins

Kapinos, L. E., Schoch, R. L., Wagner, R. S., et al. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.02.021 · Cited by 130 · see citing works

Deleterious mutations in the essential mRNA metabolism factor, hGle1, in amyotrophic lateral sclerosis

Kaneb, H., Folkmann, A. W., Belzil, V., Jao, L.-E., Leblond, C. S., Girard, S., Daoud, H., Noreau, A., Rochefort, D. L., Hince, P., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu545 · Cited by 130 · see citing works

Complex Formation among the RNA Export Proteins Nup98, Rae1/Gle2, and TAP

Blevins, M. B., Smith, A. M., Phillips, E. M., & Powers, M. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302061200 · Cited by 129 · see citing works

Neuronal Nuclei Isolation from Human Postmortem Brain Tissue

Matevossian, A., & Akbarian, S. (2008) · Journal of Visualized Experiments · doi:10.3791/914 · Cited by 126 · see citing works

Nuclear Pore Complex Proteins in Alzheimer Disease

Sheffield, L. G., Miskiewicz, H. B., Tannenbaum, L. B., & Mirra, S. S. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000195939.40410.08 · Cited by 115 · see citing works

Altered Tau Isoform Ratio Caused by Loss of FUS and SFPQ Function Leads to FTLD-like Phenotypes

Ishigaki, S., Fujioka, Y., Okada, Y., Riku, Y., Udagawa, T., Honda, D., Yokoi, S., Endo, K., Ikenaka, K., Takagi, S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.01.013 · Cited by 115 · see citing works

Single Molecule Study of the Intrinsically Disordered FG-Repeat Nucleoporin 153

Milles, S., & Lemke, E. A. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.08.025 · Cited by 111 · see citing works

The Defective Nuclear Lamina in Hutchinson-Gilford Progeria Syndrome Disrupts the Nucleocytoplasmic Ran Gradient and Inhibits Nuclear Localization of Ubc9

Kelley, J. B., Datta, S., Snow, C. J., Chatterjee, M., Ni, L., Spencer, A., Yang, C., Cubeñas-Potts, C., Matunis, M. J., & Paschal, B. M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05087-11 · Cited by 109 · see citing works

Human tau increases amyloid β plaque size but not amyloid β‐mediated synapse loss in a novel mouse model of Alzheimer's disease

Jackson, R. J., Rudinskiy, N., Herrmann, A. G., Croft, S., Kim, J. M., Petrova, V., Ramos‐Rodríguez, J. J., Pitstick, R., Wegmann, S., Garcı́a-Alloza, M., et al. (2016) · European Journal of Neuroscience · doi:10.1111/ejn.13442 · Cited by 109 · see citing works

Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushes

Schoch, R. L., Kapinos, L. E., & Lim, R. Y. H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208440109 · Cited by 106 · see citing works

Tau reduction in the presence of amyloid-β prevents tau pathology and neuronal death in vivo

DeVos, S. L., Corjuc, B. T., Commins, C., Dujardin, S., Bannon, R. N., Corjuc, D., Moore, B. D., Bennett, R. E., Jorfi, M., Gonzales, J. A., et al. (2018) · Brain · doi:10.1093/brain/awy117 · Cited by 106 · see citing works

Tau-Mediated Nuclear Depletion and Cytoplasmic Accumulation of SFPQ in Alzheimer's and Pick's Disease

Ke, Y. D., Dramiga, J., Schütz, U., Kril, J. J., Ittner, L. M., Schröder, H., & Götz, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035678 · Cited by 104 · see citing works

The Multiple Faces of Disordered Nucleoporins

Lemke, E. A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.01.002 · Cited by 86 · see citing works

Assembly of paired helical filaments from mouse tau: implications for the neurofibrillary pathology in transgenic mouse models for Alzheimer's disease

Kampers, T., Pangalos, M. N., Geerts, H., Wiech, H., & Mandelkow, E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00522-0 · Cited by 85 · see citing works

TAR-DNA Binding Protein 43 in Pick Disease

Freeman, S. H., Spires‐Jones, T. L., Hyman, B. T., Growdon, J. H., & Frosch, M. P. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181609361 · Cited by 81 · see citing works

Promiscuous Binding of Karyopherin β 1 Modulates FG Nucleoporin Barrier Function and Expedites NTF2 Transport Kinetics

Wagner, R. S., Kapinos, L. E., Marshall, N. J., et al. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2014.12.041 · Cited by 80 · see citing works

The Nucleoporin Nup98 Is a Site for GDP/GTP Exchange on Ran and Termination of Karyopherin β2-mediated Nuclear Import

Fontoura, B. M. A., Blobel, G., & Yaseen, N. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004651200 · Cited by 79 · see citing works

Reduced RAN Expression and Disrupted Transport between Cytoplasm and Nucleus; A Key Event in Alzheimer’s Disease Pathophysiology

Mastroeni, D., Chouliaras, L., Grover, A., Liang, W. S., Hauns, K., Rogers, J., & Coleman, P. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053349 · Cited by 72 · see citing works

Defective nuclear import of Tpr in Progeria reflects the Ran sensitivity of large cargo transport

Snow, C. J., Dar, A., Dutta, A., Kehlenbach, R. H., & Paschal, B. M. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201212117 · Cited by 71 · see citing works

Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex

Vovk, A., Gu, C., Opferman, M. G., et al. (2016) · eLife · doi:10.7554/elife.10785 · Cited by 70 · see citing works

Fifty Years of Nuclear Pores and Nucleocytoplasmic Transport Studies

Floch, A. G., Palancade, B., & Doye, V. (2014) · Methods in cell biology · doi:10.1016/b978-0-12-417160-2.00001-1 · Cited by 59 · see citing works

Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae

Lord, C. L., Timney, B. L., Rout, M. P., & Wente, S. R. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201412024 · Cited by 58 · see citing works

Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms

Iwamoto, M., Asakawa, H., Hiraoka, Y., & Haraguchi, T. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01415.x · Cited by 56 · see citing works

Nuclear Pore Complex Protein Sequences Determine Overall Copolymer Brush Structure and Function

Ando, D., Zandi, R., Kim, Y. W., et al. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.03.021 · Cited by 55 · see citing works

The Dynamic Multisite Interactions between Two Intrinsically Disordered Proteins

Wu, S., Wang, D., Liu, J., et al. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201701883 · Cited by 52 · see citing works

Physical modelling of the nuclear pore complex

Osmanović, D., Fassati, A., Ford, I. J., et al. (2013) · Soft Matter · doi:10.1039/c3sm50722j · Cited by 31 · see citing works

Neuronal Nuclei Isolation from Human Postmortem Brain Tissue

Matevossian, A., & Akbarian, S. (2008) · Journal of Visualized Experiments · doi:10.3791/914-v · Cited by 30 · see citing works

Structural Characterization of Nanoscale Meshworks within a Nucleoporin FG Hydrogel

Petri, M., Frey, S., Menzel, A., et al. (2012) · Biomacromolecules · doi:10.1021/bm300412q · Cited by 29 · see citing works

Nuclear Transport: Run by Ran?

Dasso, M., & Pu, R. T. (1998) · The American Journal of Human Genetics · doi:10.1086/301990 · Cited by 25 · see citing works

Astroglia in Thick Tissue with Super Resolution and Cellular Reconstruction

Miller, S., & Rothstein, J. D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160391 · Cited by 23 · see citing works

Alzheimer disease

Knopman, D. S., Amieva, H., Petersen, R. C., Chételat, G., Holtzman, D. M., Hyman, B. T., Nixon, R. A., & Jones, D. T. (2021) · Nature Reviews Disease Primers · doi:10.1038/s41572-021-00269-y · Cited by 2,606 · see citing works

Synergy between amyloid-β and tau in Alzheimer’s disease

Busche, M. A., & Hyman, B. T. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0687-6 · Cited by 1,242 · 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-mediated disruption of the spliceosome triggers cryptic rna splicing and neurodegeneration in Alzheimer's Disease

Hsieh, 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

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

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

Nuclear pore complexes — a doorway to neural injury in neurodegeneration

Coyne, A. N., & Rothstein, J. D. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00653-6 · Cited by 96 · see citing works

Genetics of Amyotrophic Lateral Sclerosis

Gregory, J. M., Fagegaltier, D., Phatnani, H., & Harms, M. B. (2020) · Current Genetic Medicine Reports · doi:10.1007/s40142-020-00194-8 · Cited by 83 · see citing works

Pathological tau drives ectopic nuclear speckle scaffold protein SRRM2 accumulation in neuron cytoplasm in Alzheimer’s disease

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

Role of the Lipid Membrane and Membrane Proteins in Tau Pathology

Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61 · see citing works

Directly converted astrocytes retain the ageing features of the donor fibroblasts and elucidate the astrocytic contribution to human CNS health and disease.

Gatto, N., Dos Santos Souza, C., Shaw, A. C., Bell, S. M., Myszczynska, M. A., Powers, S., Meyer, K., Castelli, L. M., Karyka, E., Mortiboys, H., et al. (2021) · Aging Cell · doi:10.1111/acel.13281 · Cited by 58 · see citing works

All the Tau We Cannot See

Hyman, B. (2023) · Annual Review of Medicine · doi:10.1146/annurev-med-042921-023749 · Cited by 39 · see citing works

Lamivudine (3TC), a Nucleoside Reverse Transcriptase Inhibitor, Prevents the Neuropathological Alterations Present in Mutant Tau Transgenic Mice

Vallés-Saiz, L., Ávila, J., & Hernández, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311144 · Cited by 35 · see citing works

Tau; One Protein, So Many Diseases

Tabeshmehr, P., & Eftekharpour, E. (2023) · Biology · doi:10.3390/biology12020244 · Cited by 33 · see citing works

Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy

Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28 · see citing works

Elucidation of the GSK3α Structure Informs the Design of Novel, Paralog-Selective Inhibitors

Amaral, B., Capacci, A., Anderson, T., Tezer, C., Bajrami, B., Lulla, M., Lucas, B., Chodaparambil, J. V., Marcotte, D., Kumar, P. R., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00476 · Cited by 22 · see citing works

HMGCS2-Induced Autophagic Degradation of Tau Involves Ketone Body and ANKRD24

Hu, L.-T., Xie, X.-Y., Zhou, G.-F., Wen, Q.-X., Song, L., Luo, B., Deng, X.-J., Pan, Q.-L., & Chen, G.-J. (2023) · Journal of Alzheimer's Disease · doi:10.3233/jad-220640 · Cited by 14 · see citing works

Cytoplasmic Mislocalization of RNA Polymerase II Subunit RPB1 in Alzheimer Disease Is Linked to Pathologic Tau

Dickson, J. R., Yoon, H., Frosch, M. P., & Hyman, B. T. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab040 · Cited by 13 · see citing works

Several Phenylalanine-Glycine Motives in the Nucleoporin Nup214 Are Essential for Binding of the Nuclear Export Receptor CRM1

Roloff, S., Spillner, C., & Kehlenbach, R. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433243 · Cited by 38 · see citing works

The Ins & Outs of Nucleocytoplasmic Transport: Studies of the Nuclear Pore Complex

Tang, J. H. (2014)

The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins

Walther, T. C., Fornerod, M. W. J., Pickersgill, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.20.5703 · Cited by 247 · see citing works

The Mechanism of Nucleocytoplasmic Transport through the Nuclear Pore ComplexPreprint

Tetenbaum-Novatt, J. E., & Rout, M. P. (2010) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2010.75.033 · Cited by 44 · see citing works

Uncovering Nuclear Pore Complexity with Innovation

Adams, R. L., & Wente, S. R. (2013) · Cell · doi:10.1016/j.cell.2013.02.042 · Cited by 89 · see citing works