Arginine methylation next to the PY‐NLS modulates Transportin binding and nuclear import of FUS

Amyotrophic lateral sclerosis

Kiernan, M. C., Vucic, S., Cheah, B. C., Turner, M. R., Eisen, A., Hardiman, O., Burrell, J. R., & Zoing, M. C. (2011) · The Lancet · doi:10.1016/s0140-6736(10)61156-7 · Cited by 2,603 · see citing works

Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6

Vance, C. A., Rogelj, B., Hortobágyi, T., Vos, K. J. D., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B. N., Ruddy, D., Wright, P. D., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,531 · see citing works

Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J. M., Kasarskis, E. J., Munsat, T. L., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,526 · see citing works

Protein Arginine Methylation in Mammals: Who, What, and Why

Bedford, M. T., & Clarke, S. G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.013 · Cited by 1,810 · see citing works

Culturing hippocampal neurons

Kaech, S., & Banker, G. A. (2006) · Nature Protocols · doi:10.1038/nprot.2006.356 · Cited by 1,705 · see citing works

Culturing hippocampal neurons.

Tanaka, H. (2002) · Folia Pharmacologica Japonica · doi:10.1254/fpj.119.163 · Cited by 1,141 · see citing works

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021 · see citing works

Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update

Mackenzie, I. R. A., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I., Kril, J., Kovacs, G. G., Ghetti, B., Halliday, G., Holm, I. E., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0612-2 · Cited by 1,012 · see citing works

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 977 · see citing works

ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import

Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., Hruscha, A., Than, M. E., Mackenzie, I. R. A., Capell, A., Schmid, B., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.143 · Cited by 836 · see citing works

A new subtype of frontotemporal lobar degeneration with FUS pathology

Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722 · see citing works

The overlap of amyotrophic lateral sclerosis and frontotemporal dementia

Lomen, C. E., Anderson, T. T., & Miller, B. L. (2002) · Neurology · doi:10.1212/wnl.59.7.1077 · Cited by 699 · see citing works

ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons

Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621 · cited 1× · see citing works

Rules for Nuclear Localization Sequence Recognition by Karyopherinβ2

Lee, B. J., Cansizoglu, A. E., Süel, K. E., Louis, T. H., Zhang, Z., & Chook, Y. M. (2006) · Cell · doi:10.1016/j.cell.2006.05.049 · Cited by 555 · see citing works

Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport

Terry, L. J., Shows, E. B., & Wente, S. R. (2007) · Science · doi:10.1126/science.1142204 · Cited by 543 · see citing works

Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules

Bosco, D. A., Lemay, N., Ko, H. K., Zhou, H., Burke, C., Kwiatkowski, T. J., Sapp, P. C., McKenna-Yasek, D. M., Brown, R. H., & Hayward, L. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq335 · Cited by 520 · see citing works

PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells

Tang, J., Frankel, A., Cook, R. J., Kim, S., Paik, W. K., Williams, K. R., Clarke, S. G., & Herschman, H. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7723 · Cited by 492 · see citing works

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

Ong, S., Mittler, G., & Mann, M. (2004) · Nature Methods · doi:10.1038/nmeth715 · Cited by 458 · see citing works

Advances in understanding the molecular basis of frontotemporal dementia

Rademakers, R., Neumann, M., & Mackenzie, I. R. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.117 · Cited by 414 · see citing works

Nuclear import by Karyopherin-βs: recognition and inhibition

Chook, Y., & Süel, K. E. (2010) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2010.10.014 · Cited by 402 · see citing works

Arginine N -Methyltransferase 1 Is Required for Early Postimplantation Mouse Development, but Cells Deficient in the Enzyme Are Viable

Pawlak, M. R., Scherer, C., Chen, J., Roshon, M. J., & Ruley, H. E. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.13.4859-4869.2000 · Cited by 355 · see citing works

Understanding the role of TDP-43 and FUS/TLS in ALS and beyond

Da Cruz, S., & Cleveland, D. W. (2011) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.05.029 · Cited by 351 · see citing works

The RNA Binding Protein TLS Is Translocated to Dendritic Spines by mGluR5 Activation and Regulates Spine Morphology

Fujii, R., Okabe, S., Urushido, T., Inoue, K., Yoshimura, A., Tachibana, T., Nishikawa, T., Hicks, G. G., & Takumi, T. (2005) · Current Biology · doi:10.1016/j.cub.2005.01.058 · Cited by 322 · see citing works

FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations

Neumann, M., Bentmann, E., Dormann, D., Jawaid, A., DeJesus‐Hernandez, M., Ansorge, O., Roeber, S., Kretzschmar, H. A., Muñoz, D. G., Kusaka, H., et al. (2011) · Brain · doi:10.1093/brain/awr201 · Cited by 302 · see citing works

Local RNA Translation at the Synapse and in Disease: Figure 1.

Liu‐Yesucevitz, L., Bassell, G. J., Gitler, A. D., Hart, A. C., Klann, E., Richter, J. D., Warren, S. T., & Wolozin, B. L. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4105-11.2011 · Cited by 289 · see citing works

Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)

Bentmann, E., Neumann, M., Tahirović, S., Rodde, R., Dormann, D., & Haass, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328757 · Cited by 277 · see citing works

RNA and RNA Binding Proteins Participate in Early Stages of Cell Spreading through Spreading Initiation Centers

de Hoog, C. L., Foster, L. J., & Mann, M. (2004) · Cell · doi:10.1016/s0092-8674(04)00456-8 · Cited by 262 · see citing works

Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease

Neumann, M., Roeber, S., Kretzschmar, H. A., Rademakers, R., Baker, M. C., & Mackenzie, I. R. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0581-5 · Cited by 257 · see citing works

FUS mutations in amyotrophic lateral sclerosis: clinical, pathological, neurophysiological and genetic analysis

Blair, I. P., Williams, K. L., Warraich, S. T., Durnall, J. C., Thoeng, A., Manavis, J., Blumbergs, P. C., Vucic, S., Kiernan, M. C., & Nicholson, G. A. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2009.194399 · Cited by 250 · see citing works

TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines

Fujii, R., & Takumi, T. (2005) · Journal of Cell Science · doi:10.1242/jcs.02692 · Cited by 245 · see citing works

FUS pathology defines the majority of tau- and TDP-43-negative frontotemporal lobar degeneration

Urwin, H., Josephs, K. A., Rohrer, J. D., Mackenzie, I. R., Neumann, M., Authier, A., Seelaar, H., Swieten, J. C. V., Brown, J. M., Johannsen, P., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0698-6 · Cited by 244 · see citing works

Design of Peptide Inhibitors for the Importin α/β Nuclear Import Pathway by Activity-Based Profiling

Kosugi, S., Hasebe, M., Entani, T., Takayama, S., Tomita, M., & Yanagawa, H. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.07.019 · Cited by 237 · see citing works

Protein arginine methylation: Cellular functions and methods of analysis

Pahlich, S., Zakaryan, R. P., & Gehring, H. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.08.008 · Cited by 237 · see citing works

PABP1 identified as an arginine methyltransferase substrate using high‐density protein arrays

Lee, J. H., & Bedford, M. T. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf052 · Cited by 232 · see citing works

Nuclear localization sequence of FUS and induction of stress granules by ALS mutants

Gál, J., Zhang, J. Y., Kwinter, D. M., Zhai, J., Jia, H., Jia, J., & Zhu, H. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.06.010 · Cited by 215 · see citing works

Continuum of Frontal Lobe Impairment in Amyotrophic Lateral Sclerosis

Murphy, J. M., Henry, R. G., Langmore, S. E., Kramer, J. H., Miller, B. L., & Lomen, C. E. (2007) · Archives of Neurology · doi:10.1001/archneur.64.4.530 · Cited by 214 · see citing works

TDP-43 and FUS: a nuclear affair

Dormann, D., & Haass, C. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.05.002 · Cited by 214 · see citing works

Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations

Tradewell, M. L., Yu, Z., Tibshirani, M., Boulanger, M., Durham, H. D., & Richard, S. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr448 · Cited by 213 · see citing works

Frameshift and novel mutations in FUS in familial amyotrophic lateral sclerosis and ALS/dementia

Yan, J., Deng, H., Siddique, N. A., Fecto, F., Chen, W., Yang, Y., Liu, E., Donkervoort, S. C., Zheng, J. G., Shi, Y., et al. (2010) · Neurology · doi:10.1212/wnl.0b013e3181f07e0c · Cited by 208 · see citing works

Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations

Bäumer, D., Hilton, D. A., Paine, S., Turner, M. R., Lowe, J. S., Talbot, K., & Ansorge, O. (2010) · Neurology · doi:10.1212/wnl.0b013e3181ed9cde · Cited by 202 · see citing works

Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation

Mackenzie, I. R. A., Ansorge, O., Strong, M., Bilbao, J., Zinman, L., Ang, L.-C., Baker, M., Stewart, H., Eisen, A., Rademakers, R., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0838-7 · Cited by 183 · see citing works

Klotho as a potential biomarker and therapy for acute kidney injury

Hu, M. C., & Moe, O. W. (2012) · Nature Reviews Nephrology · doi:10.1038/nrneph.2012.92 · Cited by 180 · see citing works

Structure-based design of a pathway-specific nuclear import inhibitor

Cansizoglu, A. E., Lee, B. J., Zhang, Z. C., Fontoura, B. M. A., & Chook, Y. M. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1229 · Cited by 179 · see citing works

Nuclear transport impairment of amyotrophic lateral sclerosis‐linked mutations in FUS/TLS

Ito, D., Seki, M., Tsunoda, Y., Uchiyama, H., & Suzuki, N. (2010) · Annals of Neurology · doi:10.1002/ana.22246 · Cited by 168 · see citing works

Detection of Arginine Dimethylated Peptides by Parallel Precursor Ion Scanning Mass Spectrometry in Positive Ion Mode

Rappsilber, J., Friesen, W. J., Paushkin, S. V., Dreyfuss, G., & Mann, M. (2003) · Analytical Chemistry · doi:10.1021/ac026283q · Cited by 153 · see citing works

Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)

Zhang, Z. C., & Chook, Y. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207247109 · Cited by 151 · see citing works

De novo truncating FUS gene mutation as a cause of sporadic amyotrophic lateral sclerosis

DeJesus‐Hernandez, M., Kocerha, J., Finch, N. A., Crook, R., Baker, M. C., Desaro, P., Johnston, A., Rutherford, N. J., Wojtas, A., Kennelly, K. D., et al. (2010) · Human Mutation · doi:10.1002/humu.21241 · Cited by 150 · see citing works

Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations

Kino, Y., Washizu, C., Aquilanti, E., Okuno, M., Kurosawa, M., Yamada, M., Doi, H., & Nukina, N. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1162 · Cited by 147 · see citing works

Unusual Sites of Arginine Methylation in Poly(A)-binding Protein II and in Vitro Methylation by Protein Arginine Methyltransferases PRMT1 and PRMT3

Smith, J. J., Rücknagel, K. P., Schierhorn, A., Tang, J., Németh, A., Linder, M., Herschman, H. R., & Wahle, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13229 · Cited by 146 · see citing works

Novel FUS/TLS Mutations and Pathology in Familial and Sporadic Amyotrophic Lateral Sclerosis

Hewitt, C., Kirby, J., Highley, J. R., Hartley, J. A., Hibberd, R., Hollinger, H. C., Williams, T. L., Ince, P. G., McDermott, C. J., & Shaw, P. J. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.52 · Cited by 139 · see citing works

Two Italian kindreds with familial amyotrophic lateral sclerosis due to FUS mutation

Chiò, A., Restagno, G., Brunetti, M., Ossola, I., Calvo, A., Mora, G., Sabatelli, M., Monsurrò, M. R., Battistini, S., Mandrioli, J., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.001 · Cited by 135 · see citing works

Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factorsPreprint

Yu, M. C., Bachand, F., McBride, A. E., Komili, S., Casolari, J. M., & Silver, P. A. (2004) · Genes & Development · doi:10.1101/gad.1223204 · Cited by 133 · see citing works

The most common type of FTLD-FUS (aFTLD-U) is associated with a distinct clinical form of frontotemporal dementia but is not related to mutations in the FUS gene

Snowden, J. S., Hu, Q., Rollinson, S. J., Halliwell, N. A., Robinson, A., Davidson, Y. S., Momeni, P., Baborie, A., Griffiths, T. D., Jaros, E., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0816-0 · Cited by 131 · see citing works

Fus gene mutations in familial and sporadic amyotrophic lateral sclerosis

Rademakers, R., Stewart, H. G., DeJesus‐Hernandez, M., Krieger, C., Graff‐Radford, N. R., Fabros, M., Briemberg, H., Cashman, N. R., Eisen, A., & Mackenzie, I. R. (2010) · Muscle & Nerve · doi:10.1002/mus.21665 · Cited by 126 · see citing works

Asymmetric Arginine Dimethylation of Heterogeneous Nuclear Ribonucleoprotein K by Protein-arginine Methyltransferase 1 Inhibits Its Interaction with c-Src

Ostareck‐Lederer, A., Ostareck, D. H., Rücknagel, K. P., Schierhorn, A., Moritz, B., Hüttelmaier, S., Flach, N., Handoko, L., & Wahle, E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513053200 · Cited by 113 · see citing works

Novel missense and truncating mutations in FUS/TLS in familial ALS

Waibel, S., Neumann, M., Rabe, M., Meyer, T., & Ludolph, A. (2010) · Neurology · doi:10.1212/wnl.0b013e3181f07e26 · Cited by 99 · see citing works

Assembly PCR oligo maker: a tool for designing oligodeoxynucleotides for constructing long DNA molecules for RNA production

Rydzanicz, R., Zhao, X. S., & Johnson, P. E. (2005) · Nucleic Acids Res. · doi:10.1093/nar/gki380 · Cited by 95 · see citing works

FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis

Mackenzie, I. R., & Neumann, M. (2011) · Brain Research · doi:10.1016/j.brainres.2011.12.010 · Cited by 91 · see citing works

PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function

Jobert, L., Argentini, M., & Tora, L. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.12.008 · Cited by 91 · see citing works

Effects of adenosine dialdehyde on S-adenosylhomocysteine hydrolase and S-adenosylmethionine-dependent transmethylations in mouse L929 cells.

Bartel, R. L., & BORCHARDT, R. T. (1984) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)15050-5 · Cited by 89 · see citing works

Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations

Neumann, M., Valori, C. F., Ansorge, O., Kretzschmar, H. A., Muñoz, D. G., Kusaka, H., Yokota, O., Ishihara, K., Ang, L.-C., Bilbao, J. M., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1020-6 · Cited by 88 · see citing works

Exposure on Cell Surface and Extensive Arginine Methylation of Ewing Sarcoma (EWS) Protein

Belyanskaya, L. L., Gehrig, P. M., & Gehring, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011446200 · Cited by 86 · see citing works

Modular Organization and Combinatorial Energetics of Proline–Tyrosine Nuclear Localization Signals

Süel, K. E., Gu, H., & Chook, Y. M. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060137 · Cited by 85 · see citing works

Transportin1: a marker of FTLD-FUS

Brelstaff, J., Lashley, T., Holton, J. L., Lees, A. J., Rossor, M. N., Bandopadhyay, R., & Révész, T. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0863-6 · Cited by 73 · see citing works

FUS Mutations in Familial Amyotrophic Lateral Sclerosis in the Netherlands

Groen, E. J. N., van Es, M. A., van Vught, P. W. J., Spliet, W. G. M., Engelen-Lee, J.-Y., de Visser, M., Wokke, J. H. J., Schelhaas, H. J., Ophoff, R. A., Fumoto, K., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2009.329 · Cited by 73 · see citing works

Immunohistochemical identification of messenger RNA-related proteins in basophilic inclusions of adult-onset atypical motor neuron disease

Fujita, K., Ito, H., Nakano, S., Kinoshita, Y., Wate, R., & Kusaka, H. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0415-x · Cited by 63 · see citing works

Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich region-mediated nucleocytoplasmic distribution

Aoki, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf638 · Cited by 63 · see citing works

Regulation of the Nuclear Poly(A)-binding Protein by Arginine Methylation in Fission Yeast

Perreault, A., Lemieux, C., & Bachand, F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610512200 · Cited by 62 · see citing works

Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1

Araya, N., Hiraga, H., Kako, K., Arao, Y., Kato, S., & Fukamizu, A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.018 · Cited by 61 · see citing works

Effects of Adenosine Dialdehyde Treatment on In Vitro and In Vivo Stable Protein Methylation in HeLa Cells

Chen, D. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh131 · Cited by 57 · see citing works

TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation

Du, K., Arai, S., Kawamura, T., Matsushita, A., & Kurokawa, R. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.12.097 · Cited by 48 · see citing works

Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide

Pahlich, S., Bschir, K., Chiavi, C., Belyanskaya, L. L., & Gehring, H. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20579 · Cited by 40 · see citing works

Localization of fused in sarcoma (FUS) protein to the post-synaptic density in the brain

Aoki, N., Higashi, S., Kawakami, I., Kobayashi, Z., Hosokawa, M., Katsuse, O., Togo, T., Hirayasu, Y., & Akiyama, H. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0984-6 · Cited by 40 · see citing works

Arginine Methylation of the Nuclear Poly(A) Binding Protein Weakens the Interaction with Its Nuclear Import Receptor, Transportin

Fronz, K., Güttinger, S., Burkert, K., Kühn, U., Stöhr, N., Schierhorn, A., & Wahle, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.273912 · Cited by 35 · see citing works

Protein-arginine Methyltransferase 1 (PRMT1) Methylates Ash2L, a Shared Component of Mammalian Histone H3K4 Methyltransferase Complexes

Napierala, J. S., Zurita‐Lopez, C. I., Clarke, S. G., Bedford, M. T., & Dent, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202416 · Cited by 35 · see citing works

Nuclear carrier and RNA‐binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes

Davidson, Y. S., Robinson, A., Hu, Q., Mishra, M., Baborie, A., Jaros, E., Perry, R. H., Cairns, N. J., Richardson, A. M. T., Gerhard, A., et al. (2012) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2012.01274.x · Cited by 35 · see citing works

Proteomic Analysis of Methylarginine-Containing Proteins in HeLa Cells by Two-Dimensional Gel Electrophoresis and Immunoblotting with a Methylarginine-Specific Antibody

Hung, C., Lee, Y., Chen, D., & Li, C. (2009) · The Protein Journal · doi:10.1007/s10930-009-9174-3 · Cited by 25 · see citing works

Periodate-oxidized adenosine induction of murine thymidine kinase: role of DNA methylation in the generation of tumor cell heterogeneity.

Liteplo, R. G., & Kerbel, R. S. (1986) · PubMed · Cited by 14 · 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

FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions

Qamar, S., Wang, G., Randle, S. J., Ruggeri, F. S., Varela, J. A., Lin, J. Q., Phillips, E. C., Miyashita, A., Williams, D., Ströhl, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.056 · Cited by 907 · see citing works

The changing scene of amyotrophic lateral sclerosis

Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957 · see citing works

Liquid-Liquid Phase Separation in Disease.

Alberti, S., & Dormann, D. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043527 · Cited by 782 · see citing works

Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation

Hofweber, M., Hutten, S., Bourgeois, B. M. R., Spreitzer, E., Niedner, A., Schifferer, M., Ruepp, M., Simons, M., Niessing, D., Madl, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.004 · Cited by 654 · see citing works

Phase separation and neurodegenerative diseases: a disturbance in the force

Zbinden, A., Pérez-Berlanga, M., De Rossi, P., & Polymenidou, M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.09.014 · Cited by 500 · see citing works

Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics

Boeynaems, S., Bogaert, E., Kovács, D., Konijnenberg, A., Timmerman, E., Volkov, A. N., Guharoy, M., Decker, M. D., Jaspers, T., Ryan, V. H., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.013 · Cited by 502 · see citing works

RGG/RG Motif Regions in RNA Binding and Phase Separation

Chong, P. A., Vernon, R. M., & Forman-Kay, J. D. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.06.014 · Cited by 408 · see citing works

Friend or foe—Post-translational modifications as regulators of phase separation and RNP granule dynamics

Hofweber, M., & Dormann, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001189 · Cited by 382 · see citing works

Physiological functions and pathobiology of TDP ‐43 and FUS / TLS proteins

Ratti, A., & Buratti, E. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13625 · Cited by 384 · see citing works

Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies

Mackenzie, I. R., & Neumann, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13588 · Cited by 374 · see citing works

The role of FUS gene variants in neurodegenerative diseases

Deng, H., Gao, K., & Jankovic, J. J. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.78 · Cited by 357 · see citing works

hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations

Mori, K., Lammich, S., Mackenzie, I. R., Forné, I., Zilow, S., Kretzschmar, H. A., Edbauer, D., Janssens, J., Kleinberger, G., Cruts, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1088-7 · Cited by 339 · see citing works

Chemical Biology of Protein Arginine Modifications in Epigenetic Regulation

Fuhrmann, J., Clancy, K. W., & Thompson, P. R. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00003 · Cited by 325 · see citing works

Are aberrant phase transitions a driver of cellular aging?

Alberti, S., & Hyman, A. A. (2016) · BioEssays · doi:10.1002/bies.201600042 · Cited by 273 · see citing works

Impaired DNA damage response signaling by FUS-NLS mutations leads to neurodegeneration and FUS aggregate formation

Naumann, M., Pal, A., Goswami, A., Lojewski, X., Japtok, J., Vehlow, A., Naujock, M., Günther, R., Jin, M., Stanslowsky, N., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02299-1 · Cited by 275 · see citing works

Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD

Boeynaems, S., Bogaert, E., Michiels, E., Gijselinck, I., Sieben, A., Jovičić, A., De Baets, G., Scheveneels, W., Steyaert, J., Cuijt, I., et al. (2016) · Scientific Reports · doi:10.1038/srep20877 · Cited by 262 · see citing works

Structural Biology and Regulation of Protein Import into the Nucleus

Christie, M., Chang, C.-W. M., Róna, G., Smith, K. M. L., Stewart, A. G., Takeda, A. A. S., Fontes, M. R. M., Stewart, M., Vértessy, B. G., Forwood, J. K., et al. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.10.023 · Cited by 247 · see citing works

ALS/FTD-Linked Mutation in FUS Suppresses Intra-axonal Protein Synthesis and Drives Disease Without Nuclear Loss-of-Function of FUS

López‐Erauskin, J., Tadokoro, T., Baughn, M. W., Myers, B., McAlonis‐Downes, M., Chillón-Marinas, C., Asiaban, J. N., Artates, J. W., Bui, A. T., Vetto, A. P., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.044 · Cited by 233 · see citing works

Biochemical Properties and Biological Functions of FET Proteins

Schwartz, J. C., Cech, T. R., & Parker, R. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034325 · Cited by 230 · see citing works

PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA

Singatulina, A. S., Hamon, L., Sukhanova, M. V., Desforges, B., Joshi, V., Bouhss, A., Lavrik, O. I., & Pastré, D. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.031 · Cited by 228 · see citing works

The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity

Loughlin, F. E., Lukavsky, P. J., Kazeeva, T., Reber, S., Hock, E., Colombo, M., von Schroetter, C., Pauli, P., Cléry, A., Mühlemann, O., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.11.012 · Cited by 214 · see citing works

Autophagy and ALS: mechanistic insights and therapeutic implications

Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works

An update on blood-based biomarkers for non-Alzheimer neurodegenerative disorders

Ashton, N. J., Hye, A., Rajkumar, A. P., Leuzy, A., Snowden, S. G., Suárez‐Calvet, M., Karikari, T. K., Schöll, M., Joie, R. L., Rabinovici, G. D., et al. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0348-0 · Cited by 182 · see citing works

A complex of C9ORF72 and p62 uses arginine methylation to eliminate stress granules by autophagy

Chitiprolu, M., Jagow, C., Tremblay, V., Bondy‐Chorney, E., Paris, G., Savard, A., Palidwor, G., Barry, F. A., Zinman, L. H., Keith, J. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05273-7 · Cited by 179 · see citing works

Stress granules in neurodegeneration – lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma

Bentmann, E., Haass, C., & Dormann, D. (2013) · FEBS Journal · doi:10.1111/febs.12287 · Cited by 173 · see citing works

Post-translational modifications in liquid-liquid phase separation: a comprehensive review

Li, J., Zhang, M., Ma, W., Yang, B., Lu, H., Zhou, F., & Zhang, L. (2022) · Molecular Biomedicine · doi:10.1186/s43556-022-00075-2 · Cited by 168 · see citing works

TDP ‐43 and FUS en route from the nucleus to the cytoplasm

Ederle, H., & Dormann, D. (2017) · FEBS Letters · doi:10.1002/1873-3468.12646 · Cited by 169 · see citing works

Nuclear localization signals for four distinct karyopherin-β nuclear import systems

Soniat, M. M., & Chook, Y. M. (2015) · Biochemical Journal · doi:10.1042/bj20150368 · Cited by 165 · see citing works

Cellular consequences of arginine methylation

Lorton, B. M., & Shechter, D. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03140-2 · Cited by 164 · see citing works

FUS is Phosphorylated by DNA-PK and Accumulates in the Cytoplasm after DNA Damage

Deng, Q., Holler, C. J., Taylor, G., Hudson, K. F., Watkins, W., Gearing, M., Ito, D., Murray, M. E., Dickson, D. W., Seyfried, N. T., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0172-14.2014 · Cited by 161 · see citing works

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

Ederle, H., Funk, C., Abou‐Ajram, C., Hutten, S., Funk, E. B. E., Kehlenbach, R. H., Bailer, S. M., & Dormann, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-25007-5 · Cited by 159 · see citing works

Genetics of <scp>FTLD</scp> : overview and what else we can expect from genetic studies

Pottier, C., Ravenscroft, T. A., Sanchez‐Contreras, M., & Rademakers, R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13622 · Cited by 148 · see citing works

Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics

Baron, D. M., Kaushansky, L. J., Ward, C. L., Sama, R. R. K., Chian, R.-J., Boggio, K. J., Quaresma, A. J. C., Nickerson, J. A., & Bosco, D. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-30 · Cited by 154 · see citing works

Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis

Shang, Y., & Huang, E. J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.036 · Cited by 154 · see citing works

Activity-dependent FUS dysregulation disrupts synaptic homeostasis

Sephton, C. F., Tang, A. A., Kulkarni, A., West, J. D., Brooks, M., Stubblefield, J. J., Liu, Y., Zhang, M. Q., Green, C. B., Huber, K. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406162111 · Cited by 145 · see citing works

Review: neuropathology of non-tau frontotemporal lobar degeneration

Neumann, M., & Mackenzie, I. R. A. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12526 · Cited by 144 · see citing works

TDP-43/FUS in motor neuron disease: Complexity and challenges

Guerrero, E. N., Wang, H., Mitra, J., Hegde, P. M., Stowell, S. E., Liachko, N. F., Kraemer, B. C., Garruto, R. M., Rao, K. S. J., & Hegde, M. L. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.09.004 · Cited by 144 · see citing works

ALS mutant FUS proteins are recruited into stress granules in induced Pluripotent Stem Cells (iPSCs) derived motoneurons

Lenzi, J., Santis, R. D., de Turris, V., Morlando, M., Laneve, P., Calvo, A., Caliendo, V., Chiò, A., Rosa, A., & Bozzoni, I. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.020099 · Cited by 140 · see citing works

Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis

Scekic‐Zahirovic, J., Oussini, H. E., Mersmann, S., Drenner, K., Wagner, M., Sun, Y., Allmeroth, K., Dieterle, S., Sinniger, J., Dirrig‐Grosch, S., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1687-9 · Cited by 135 · see citing works

Pathogenesis of FUS-associated ALS and FTD: insights from rodent models

Nolan, M., Talbot, K., & Ansorge, O. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0358-8 · Cited by 139 · see citing works

Fused in sarcoma (FUS): An oncogene goes awry in neurodegeneration

Dormann, D., & Haass, C. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.03.006 · Cited by 134 · see citing works

Compromised paraspeckle formation as a pathogenic factor in FUSopathies

Shelkovnikova, T. A., Robinson, H. K., Troakes, C., Ninkina, N. N., & Buchman, V. L. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt622 · Cited by 134 · see citing works

Common Molecular Pathways in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Weishaupt, J. H., Hyman, T., & Đikić, I. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.07.005 · Cited by 128 · see citing works

Nucleic acid-binding specificity of human FUS protein

Wang, X., Schwartz, J. C., & Cech, T. R. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv679 · Cited by 130 · see citing works

Functions of FUS/TLS From DNA Repair to Stress Response: Implications for ALS

Sama, R. R. K., Ward, C. L., & Bosco, D. A. (2014) · ASN NEURO · doi:10.1177/1759091414544472 · Cited by 128 · see citing works

Inside out: the role of nucleocytoplasmic transport in ALS and FTLD

Boeynaems, S., Bogaert, E., Damme, P. V., & Bosch, L. V. D. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1586-5 · Cited by 128 · see citing works

Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons

Ryu, H.-H., Jun, M.-H., Min, K.-J., Jang, D.-J., Lee, Y.-S., Kim, H. K., & Lee, J.-A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.026 · Cited by 125 · see citing works

Modeling Neurodegenerative Disorders in Drosophila melanogaster

Bolus, H., Crocker, K. L., Boekhoff‐Falk, G., & Chtarbanova, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093055 · Cited by 121 · see citing works

The nexus between RNA-binding proteins and their effectors

He, S., Valkov, E., Cheloufi, S., & Murn, J. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00550-0 · Cited by 119 · see citing works

Linking hnRNP Function to ALS and FTD Pathology

Purice, M. D., & Taylor, J. P. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00326 · Cited by 121 · see citing works

Regulation of liquid–liquid phase separation with focus on post-translational modifications

Luo, Y.-Y., Wu, J., & Li, Y. (2021) · Chemical Communications · doi:10.1039/d1cc05266g · Cited by 117 · see citing works

Biomolecular condensates in neurodegeneration and cancer

Spannl, S., Tereshchenko, M., Mastromarco, G. J., Ihn, S. J., & Lee, H. O. (2019) · Traffic · doi:10.1111/tra.12704 · Cited by 112 · see citing works

The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS

Rhoads, S. N., Monahan, Z. T., Yee, D. S., & Shewmaker, F. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030886 · Cited by 115 · see citing works

Protein Arginine Methyltransferase 1 and 8 Interact with FUS to Modify Its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo

Scaramuzzino, C., Monaghan, J., Milioto, C., Lanson, N. A., Maltare, A., Aggarwal, T., Casci, I., Fackelmayer, F. O., Pennuto, M., & Pandey, U. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061576 · Cited by 106 · see citing works

Role of FET proteins in neurodegenerative disorders

Svetoni, F., Frisone, P., & Paronetto, M. P. (2016) · RNA Biology · doi:10.1080/15476286.2016.1211225 · Cited by 107 · see citing works

Protein Arginine Methyltransferase 6 Enhances Polyglutamine-Expanded Androgen Receptor Function and Toxicity in Spinal and Bulbar Muscular Atrophy

Scaramuzzino, C., Casci, I., Parodi, S., Lievens, P., Polanco, M. J., Milioto, C., Chivet, M., Monaghan, J., Mishra, A., Badders, N. M., et al. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.031 · Cited by 107 · see citing works

Transportin‐1 and Transportin‐2: Protein nuclear import and beyond

Twyffels, L., Gueydan, C., & Kruys, V. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.023 · Cited by 107 · see citing works

A fruitful endeavor: Modeling ALS in the fruit fly

Casci, I., & Pandey, U. B. (2014) · Brain Research · doi:10.1016/j.brainres.2014.09.064 · Cited by 98 · see citing works

The Effect of PRMT1-Mediated Arginine Methylation on the Subcellular Localization, Stress Granules, and Detergent-Insoluble Aggregates of FUS/TLS

Yamaguchi, A., & Kitajo, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049267 · Cited by 101 · see citing works

Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases

Chen, C., Ding, X., Akram, N., Xue, S., & Luo, S. (2019) · Molecules · doi:10.3390/molecules24081622 · Cited by 96 · see citing works

Molecular Dissection of FUS Points at Synergistic Effect of Low-Complexity Domains in Toxicity

Bogaert, E., Boeynaems, S., Kato, M., Guo, L. E., Caulfield, T. R., Steyaert, J., Scheveneels, W., Wilmans, N., Haeck, W., Hersmus, N., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.070 · Cited by 95 · see citing works

Genotype-phenotype relationship in hereditary amyotrophic lateral sclerosis

Yamashita, S., & Ando, Y. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0036-y · Cited by 94 · see citing works

Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS

Suárez‐Calvet, M., Neumann, M., Arzberger, T., Abou‐Ajram, C., Funk, E. B. E., Hartmann, H., Edbauer, D., Kremmer, E., Göbl, C., Moritz, R., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1544-2 · Cited by 92 · see citing works

Small molecule modulation of a redox-sensitive stress granule protein dissolves stress granules with beneficial outcomes for familial amyotrophic lateral sclerosis modelsPreprint

Uechi, H., Sridharan, S., Nijssen, J., Bilstein, J., Iglesias‐Artola, J. M., Kishigami, S., Casablancas-Antràs, V., Poser, I., Martinez, E. J., Boczek, E. E., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/721001 · Cited by 82 · see citing works

A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1

Barraud, P., Banerjee, S., Mohamed, W. I., Jantsch, M. F., & Allain, F. H. ‐. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323698111 · Cited by 78 · see citing works

Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?

Sternburg, E. L., da Silva, L. A. G., & Dormann, D. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.07.004 · Cited by 78 · see citing works

RNA dysfunction and aggrephagy at the centre of an amyotrophic lateral sclerosis/frontotemporal dementia disease continuum

Thomas, M., Alegre‐Abarrategui, J., & Wade‐Martins, R. (2013) · Brain · doi:10.1093/brain/awt030 · Cited by 74 · see citing works

The roles of intrinsic disorder-based liquid-liquid phase transitions in the “Dr. Jekyll–Mr. Hyde” behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Uversky, V. N. (2017) · Autophagy · doi:10.1080/15548627.2017.1384889 · Cited by 76 · see citing works

The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration

George‐Hyslop, P. S., Lin, J. Q., Miyashita, A., Phillips, E. C., Qamar, S., Randle, S. J., & Wang, G. (2018) · Brain Research · doi:10.1016/j.brainres.2018.04.036 · Cited by 76 · see citing works

Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cells

Appocher, C., Mohagheghi, F., Cappelli, S., Stuani, C., Romano, M., Feiguin, F. M., & Buratti, E. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx477 · Cited by 76 · see citing works

The RGG motif proteins: Interactions, functions, and regulations

Chowdhury, M. N., & Jin, H. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1748 · Cited by 68 · see citing works

PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca2+ uptake in immortalized cells

Madreiter‐Sokolowski, C. T., Klec, C., Parichatikanond, W., Stryeck, S., Gottschalk, B., Pulido, S., Rost, R., Eroğlu, E., Hofmann, N., Bondarenko, A. I., et al. (2016) · Nature Communications · doi:10.1038/ncomms12897 · Cited by 75 · see citing works

Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis

Cicardi, M. E., Marrone, L., Azzouz, M., & Trotti, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106389 · Cited by 73 · see citing works

Impaired protein degradation in FTLD and related disorders

Götzl, J. K., Lang, C. M., Haass, C., & Capell, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.008 · Cited by 70 · see citing works

Nonclassical nuclear localization signals mediate nuclear import of CIRBP

Bourgeois, B. M. R., Hutten, S., Gottschalk, B., Hofweber, M., Richter, G., Sternat, J., Abou‐Ajram, C., Göbl, C., Leitinger, G., Graier, W. F., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1918944117 · Cited by 72 · see citing works

Traffic jam at the nuclear pore: All roads lead to nucleocytoplasmic transport defects in ALS/FTD

Fallini, C., Khalil, B., Smith, C. L., & Rossoll, W. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104835 · Cited by 68 · see citing works

ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1

Soo, K. Y., Sultana, J. M., King, A. E., Atkinson, R., Warraich, S. T., Sundaramoorthy, V., Blair, I. P., Farg, M. A., & Atkin, J. D. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.30 · Cited by 71 · see citing works

Nucleic acid binding proteins affect the subcellular distribution of phosphorothioate antisense oligonucleotides

Bailey, J., Shen, W., Liang, X., & Crooke, S. T. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx709 · Cited by 69 · see citing works

Posttranslational Modifications of the Retinoblastoma Tumor Suppressor Protein as Determinants of Function

MacDonald, J. I., & Dick, F. A. (2012) · Genes & Cancer · doi:10.1177/1947601912473305 · Cited by 69 · see citing works

Therapeutic Dissolution of Aberrant Phases by Nuclear-Import Receptors

Guo, L. E., Fare, C. M., & Shorter, J. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.12.004 · Cited by 66 · see citing works

Stepwise acquirement of hallmark neuropathology in FUS-ALS iPSC models depends on mutation type and neuronal aging

Japtok, J., Lojewski, X., Naumann, M., Klingenstein, M., Reinhardt, P., Sterneckert, J. L., Putz, S., Demestre, M., Boeckers, T. M., Ludolph, A. C., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.07.017 · Cited by 68 · see citing works

Mislocalised FUS mutants stall spliceosomal snRNPs in the cytoplasm

Gerbino, V., Carrı̀, M. T., Cozzolino, M., & Achsel, T. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.03.003 · Cited by 68 · see citing works

FUS Recognizes G Quadruplex Structures Within Neuronal mRNAs

Imperatore, J. A., McAninch, D. S., Valdez‐Sinon, A. N., Bassell, G. J., & Mihailescu, M. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00006 · Cited by 66 · see citing works

Cytoplasmic FUS triggers early behavioral alterations linked to cortical neuronal hyperactivity and inhibitory synaptic defects

Scekic‐Zahirovic, J., Sanjuan-Ruiz, I., Kan, V. W. Y., Megat, S., Rossi, P. D., Dieterle, S., Cassel, R., Jamet, M., Kessler, P., Wiesner, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23187-9 · Cited by 61 · see citing works

Nuclear trafficking in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Mihevc, S. P., Darovic, S., Kovanda, A., Česnik, A. B., Župunski, V., & Rogelj, B. (2016) · Brain · doi:10.1093/brain/aww197 · Cited by 59 · see citing works

Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasm

Shelkovnikova, T. A., Robinson, H. K., Connor‐Robson, N., & Buchman, V. L. (2013) · Cell Cycle · doi:10.4161/cc.26241 · Cited by 64 · see citing works

RNA ‐protein interactions in an unstructured context

Žagrović, B., Bartonek, L., & Polyansky, A. A. (2018) · FEBS Letters · doi:10.1002/1873-3468.13116 · Cited by 61 · see citing works

Nucleo–cytoplasmic transport defects and protein aggregates in neurodegeneration

Bitetto, G., & Fonzo, A. D. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00205-2 · Cited by 66 · see citing works

Amyotrophic lateral sclerosis caused by FUS mutations: advances with broad implications

Moens, T. G., Cruz, S. D., Neumann, M., Shelkovnikova, T. A., Shneider, N. A., & Bosch, L. V. D. (2025) · The Lancet Neurology · doi:10.1016/s1474-4422(24)00517-9 · Cited by 63 · see citing works

RNA metabolism in ALS: When normal processes become pathological

Droppelmann, C. A., Campos‐Melo, D., Ishtiaq, M., Volkening, K., & Strong, M. J. (2014) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2014.881377 · Cited by 61 · see citing works

Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1

Tibshirani, M., Tradewell, M. L., Mattina, K. R., Minotti, S., Yang, W., Zhou, H., Strong, M. J., Hayward, L. J., & Durham, H. D. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu494 · Cited by 63 · see citing works

Localization of SERBP 1 in stress granules and nucleoli

Lee, Y., Wei, H., Chen, L., & Li, C. (2013) · FEBS Journal · doi:10.1111/febs.12606 · Cited by 60 · see citing works

TDP-43 and FUS–structural insights into RNA recognition and self-association

Loughlin, F. E., & Wilce, J. A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.07.012 · Cited by 60 · see citing works

Oxr1 improves pathogenic cellular features of ALS-associated FUS and TDP-43 mutations

Finelli, M. J., Liu, K. X., Wu, Y., Oliver, P. L., & Davies, K. E. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv104 · Cited by 59 · see citing works

Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U

Lee, E. B., Russ, J., Jung, H., Elman, L. B., Chahine, L. M., Kremens, D. E., Miller, B. L., Coslett, H. B., Trojanowski, J. Q., Deerlin, V. M. V., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-9 · Cited by 58 · see citing works

Global Analysis of Protein Arginine Methylation

Zhang, F., Kerbl-Knapp, J., Colman, M. J. R., Meinitzer, A., Macher, T., Vujić, N., Fasching, S., Jany-Luig, E., Korbelius, M., Kuentzel, K. B., et al. (2021) · Cell Reports Methods · doi:10.1016/j.crmeth.2021.100016 · Cited by 56 · see citing works

Role of RNA Binding Proteins with prion-like domains in muscle and neuromuscular diseases

Picchiarelli, G., & Dupuis, L. (2020) · Cell Stress · doi:10.15698/cst2020.04.217 · Cited by 56 · see citing works

TAF15 amyloid filaments in frontotemporal lobar degeneration

Tetter, S., Arseni, D., Murzin, A. G., Buhidma, Y., Peak‐Chew, S., Garringer, H. J., Newell, K. L., Vidal, R., Apostolova, L. G., Lashley, T., et al. (2023) · Nature · doi:10.1038/s41586-023-06801-2 · Cited by 55 · see citing works

Nuclear transport dysfunction: a common theme in amyotrophic lateral sclerosis and frontotemporal dementia

Jovičić, A., Paul, J. W., & Gitler, A. D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13642 · Cited by 53 · see citing works

Nuclear import factor transportin and arginine methyltransferase 1 modify FUS neurotoxicity in Drosophila

Jäckel, S., Summerer, A. K., Thömmes, C. M., Pan, X., Voigt, A., Schulz, J. B., Rasse, T. M., Dormann, D., Haass, C., & Kahle, P. J. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.11.003 · Cited by 42 · see citing works

Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation

Hofweber, M., Hutten, S., Bourgeois, B. M. R., Spreitzer, E., Niedner, A., Schifferer, M., Ruepp, M., Simons, M., Niessing, D., Madl, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.004 · Cited by 654 · see citing works

Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations

Tradewell, M. L., Yu, Z., Tibshirani, M., Boulanger, M., Durham, H. D., & Richard, S. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr448 · Cited by 213 · see citing works

The FUS about arginine methylation in ALS and FTLD

Kaneb, H., Dion, P. A., & Rouleau, G. A. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.291 · Cited by 18 · see citing works

Handbook of aqueous electrolyte solutions

Dawber, J. G. (1986) · Endeavour · doi:10.1016/0160-9327(86)90025-6 · Cited by 168 · see citing works