HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells

Enzymatic assembly of DNA molecules up to several hundred kilobases

Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009) · Nature Methods · doi:10.1038/nmeth.1318 · Cited by 9,996

MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,777

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

Biomolecular condensates: organizers of cellular biochemistry

Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,100

Automated electron microscope tomography using robust prediction of specimen movements

Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,336

Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling

Chambers, S. M., Fasano, C. A., Papapetrou, E. P., Tomishima, M., Sadelain, M., & Studer, L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1529 · Cited by 3,620

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

Patel, A., Lee, H. O., Jawerth, L., 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 3,282

Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation

Brangwynne, C. P., Eckmann, C. R., Courson, D. S., Rybarska, A., Hoege, C., Gharakhani, J., Jülicher, F., & Hyman, A. A. (2009) · Science · doi:10.1126/science.1172046 · Cited by 3,202

A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins

Wang, J., Choi, J.-M., Holehouse, A. S., Lee, H. O., Zhang, X., Jahnel, M., Maharana, S., Lemaitre, R., Pozniakovsky, A., Drechsel, D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.006 · Cited by 2,076

Decoding ALS: from genes to mechanism

Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,066

Coexisting Liquid Phases Underlie Nucleolar Subcompartments

Feric, M., Vaidya, N., Harmon, T. S., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R. W., Pappu, R. V., & Brangwynne, C. P. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,945

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

A Phase Separation Model for Transcriptional Control

Hnisz, D., Shrinivas, K., Young, R. A., Chakraborty, A. K., & Sharp, P. A. (2017) · Cell · doi:10.1016/j.cell.2017.02.007 · Cited by 1,753

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616

Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report

Nelson, P. T., Dickson, D. W., Trojanowski, J. Q., Jack, C. R., Boyle, P. A., Arfanakis, K., Rademakers, R., Alafuzoff, I., Attems, J., Brayne, C., et al. (2019) · Brain · doi:10.1093/brain/awz099 · Cited by 1,547

Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335

Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Elden, A. C., Kim, H.-J., Hart, M. P., Chen-Plotkin, A. S., Johnson, B. S., Fang, X., Armakola, M., Geser, F., Greene, R., Lu, M. M., et al. (2010) · Nature · doi:10.1038/nature09320 · Cited by 1,325

The Hsp70 chaperone network

Rosenzweig, R., Nillegoda, N. B., Mayer, M. P., & Bukau, B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0133-3 · Cited by 1,285

Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes

Brangwynne, C. P., Mitchison, T. J., & Hyman, A. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017150108 · Cited by 1,263

Organization of Chromatin by Intrinsic and Regulated Phase Separation

Gibson, B. A., Doolittle, L. K., Schneider, M. W. G., Jensen, L. E., Gamarra, N., Henry, L., Gerlich, D. W., Redding, S., & Rosen, M. K. (2019) · Cell · doi:10.1016/j.cell.2019.08.037 · Cited by 1,072

A harmonized classification system for FTLD-TDP pathology

Mackenzie, I. R. A., Neumann, M., Baborie, A., Sampathu, D. M., Du Plessis, D., Jaros, E., Perry, R. H., Trojanowski, J. Q., Mann, D. M. A., & Lee, V. M. Y. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0845-8 · Cited by 1,017

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

RNA phase transitions in repeat expansion disorders

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

CREB-binding Protein and p300 in Transcriptional Regulation

Vo, N., & Goodman, R. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r000025200 · Cited by 866

Automated tilt series alignment and tomographic reconstruction in IMOD

Mastronarde, D. N., & Held, S. R. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.07.011 · Cited by 825

Immunochemistry on ultrathin frozen sections

Tokuyasu, K. T. (1980) · The Histochemical Journal · doi:10.1007/bf01011956 · Cited by 751

Neurodegenerative disease concomitant proteinopathies are prevalent, age-related and APOE4-associated

Robinson, J. L., Lee, E. B., Xie, S. X., Rennert, L., Suh, E., Bredenberg, C., Caswell, C., Van Deerlin, V. M., Yan, N., Yousef, A., et al. (2018) · Brain · doi:10.1093/brain/awy146 · Cited by 729

TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD

Ling, J. P., Pletnikova, O., Troncoso, J. C., & Wong, P. C. (2015) · Science · doi:10.1126/science.aab0983 · Cited by 688

The Centrosome Is a Selective Condensate that Nucleates Microtubules by Concentrating Tubulin

Woodruff, J. B., Ferreira Gomes, B., Widlund, P. O., Mahamid, J., Honigmann, A., & Hyman, A. A. (2017) · Cell · doi:10.1016/j.cell.2017.05.028 · Cited by 681

ALS-implicated protein TDP-43 sustains levels of STMN2, a mediator of motor neuron growth and repair

Klim, J. R., Williams, L. A., Limone, F., Guerra San Juan, I., Davis-Dusenbery, B. N., Mordes, D. A., Burberry, A., Steinbaugh, M. J., Gamage, K. K., Kirchner, R., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0300-4 · Cited by 653

TDP‐43 regulates its mRNA levels through a negative feedback loop

Ayala, Y. M., De Conti, L., Avendaño‐Vázquez, S. E., Dhir, A., Romano, M., D'Ambrogio, A., Tollervey, J., Ule, J., Baralle, M., Buratti, E., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.310 · Cited by 637

Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration

Melamed, Z., López-Erauskin, J., Baughn, M. W., Zhang, O., Drenner, K., Sun, Y., Freyermuth, F., McMahon, M. A., Beccari, M. S., Artates, J. W., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0293-z · Cited by 635

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

Improving structural integrity of cryosections for immunogold labeling

Liou, W., Geuze, H. J., & Slot, J. W. (1996) · Histochemistry and Cell Biology · doi:10.1007/bf02473201 · Cited by 514

Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death

Gasset-Rosa, F., Lu, S., Yu, H., Chen, C., Melamed, Z., Guo, L., Shorter, J., Da Cruz, S., & Cleveland, D. W. (2019) · Neuron · doi:10.1016/j.neuron.2019.02.038 · Cited by 509

The nucleolus functions as a phase-separated protein quality control compartment

Frottin, F., Schueder, F., Tiwary, S., Gupta, R., Körner, R., Schlichthaerle, T., Cox, J., Jungmann, R., Hartl, F. U., & Hipp, M. S. (2019) · Science · doi:10.1126/science.aaw9157 · Cited by 502

TDP-43 is a key player in the clinical features associated with Alzheimer’s disease

Josephs, K. A., Whitwell, J. L., Weigand, S. D., Murray, M. E., Tosakulwong, N., Liesinger, A. M., Petrucelli, L., Senjem, M. L., Knopman, D. S., Boeve, B. F., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1269-z · Cited by 481

Mapping Local and Global Liquid Phase Behavior in Living Cells Using Photo-Oligomerizable Seeds

Bracha, D., Walls, M. T., Wei, M.-T., Zhu, L., Kurian, M., Avalos, J. L., Toettcher, J. E., & Brangwynne, C. P. (2018) · Cell · doi:10.1016/j.cell.2018.10.048 · Cited by 462

A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

Wang, A., Conicella, A. E., Schmidt, H. B., Martin, E. W., Rhoads, S. N., Reeb, A. N., Nourse, A., Ramirez Montero, D., Ryan, V. H., Rohatgi, R., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201797452 · Cited by 444

Comprehensive identification of peptides in tandem mass spectra using an efficient open search engine

Chi, H., Liu, C., Yang, H., Zeng, W.-F., Wu, L., Zhou, W.-J., Wang, R.-M., Niu, X.-N., Ding, Y.-H., Zhang, Y., et al. (2018) · Nature Biotechnology · doi:10.1038/nbt.4236 · Cited by 434

Transport Selectivity of Nuclear Pores, Phase Separation, and Membraneless Organelles

Schmidt, H. B., & Görlich, D. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.11.001 · Cited by 424

Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

Lukavsky, P. J., Daujotyte, D., Tollervey, J. R., Ule, J., Stuani, C., Buratti, E., Baralle, F. E., Damberger, F. F., & Allain, F. H.-T. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2698 · Cited by 407

Reentrant Phase Transition Drives Dynamic Substructure Formation in Ribonucleoprotein Droplets

Banerjee, P. R., Milin, A. N., Moosa, M. M., Onuchic, P. L., & Deniz, A. A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201703191 · Cited by 396

TDP-43 α-helical structure tunes liquid–liquid phase separation and function

Conicella, A. E., Dignon, G. L., Zerze, G. H., Schmidt, H. B., D’Ordine, A. M., Kim, Y. C., Rohatgi, R., Ayala, Y. M., Mittal, J., & Fawzi, N. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912055117 · Cited by 375

An acetylation switch controls TDP-43 function and aggregation propensity

Cohen, T. J., Hwang, A. W., Restrepo, C. R., Yuan, C.-X., Trojanowski, J. Q., & Lee, V. M. Y. (2015) · Nature Communications · doi:10.1038/ncomms6845 · Cited by 362

The Control Centers of Biomolecular Phase Separation: How Membrane Surfaces, PTMs, and Active Processes Regulate Condensation

Snead, W. T., & Gladfelter, A. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.016 · Cited by 352

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

Afroz, T., Hock, E.-M., Ernst, P., Foglieni, C., Jambeau, M., Gilhespy, L. A. B., Laferriere, F., Maniecka, Z., Plückthun, A., Mittl, P., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00062-0 · Cited by 349

Polar Positioning of Phase-Separated Liquid Compartments in Cells Regulated by an mRNA Competition Mechanism

Saha, S., Weber, C. A., Nousch, M., Adame-Arana, O., Hoege, C., Hein, M. Y., Osborne-Nishimura, E., Mahamid, J., Jahnel, M., Jawerth, L., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.006 · Cited by 343

TDP-43 in the Ubiquitin Pathology of Frontotemporal Dementia With VCP Gene Mutations

Neumann, M., Mackenzie, I. R., Cairns, N. J., Boyer, P. J., Markesbery, W. R., Smith, C. D., Taylor, J. P., Kretzschmar, H. A., Kimonis, V. E., & Forman, M. S. (2007) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/nen.0b013e31803020b9 · Cited by 334

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.

Palleros, D. R., Welch, W. J., & Fink, A. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5719 · Cited by 333

Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization

West, J. A., Mito, M., Kurosaka, S., Takumi, T., Tanegashima, C., Chujo, T., Yanaka, K., Kingston, R. E., Hirose, T., Bond, C., et al. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201601071 · Cited by 328

The Mechanistic Links Between Proteasome Activity, Aging and Agerelated Diseases

Saez, I., & Vilchez, D. (2014) · Current Genomics · doi:10.2174/138920291501140306113344 · Cited by 325

A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism

Ganassi, M., Mateju, D., Bigi, I., Mediani, L., Poser, I., Lee, H. O., Seguin, S. J., Morelli, F. F., Vinet, J., Leo, G., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.021 · Cited by 311

A cellular model for sporadic ALS using patient-derived induced pluripotent stem cells

Burkhardt, M. F., Martinez, F. J., Wright, S., Ramos, C., Volfson, D., Mason, M., Garnes, J., Dang, V., Lievers, J., Shoukat-Mumtaz, U., et al. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.07.007 · Cited by 300

TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies

Cohen, T. J., Lee, V. M. Y., & Trojanowski, J. Q. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.06.004 · Cited by 269

Transient nuclear envelope rupturing during interphase in human cancer cells

Vargas, J. D., Hatch, E. M., Anderson, D. J., & Hetzer, M. W. (2012) · Nucleus · doi:10.4161/nucl.18954 · Cited by 262

Reduced proteasome activity in the aging brain results in ribosome stoichiometry loss and aggregation

Kelmer Sacramento, E., Kirkpatrick, J. M., Mazzetto, M., Baumgart, M., Bartolome, A., Di Sanzo, S., Caterino, C., Sanguanini, M., Papaevgeniou, N., Lefaki, M., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209596 · Cited by 236

Stress Induces Dynamic, Cytotoxicity-Antagonizing TDP-43 Nuclear Bodies via Paraspeckle LncRNA NEAT1-Mediated Liquid-Liquid Phase Separation

Wang, C., Duan, Y., Duan, G., Wang, Q., Zhang, K., Deng, X., Qian, B., Gu, J., Ma, Z., Zhang, S., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.019 · Cited by 230

Novel Adenosine-Derived Inhibitors of 70 kDa Heat Shock Protein, Discovered Through Structure-Based Design

Williamson, D. S., Borgognoni, J., Clay, A., Daniels, Z., Dokurno, P., Drysdale, M. J., Foloppe, N., Francis, G. L., Graham, C. J., Howes, R., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801627a · Cited by 227

The synaptonemal complex has liquid crystalline properties and spatially regulates meiotic recombination factors

Rog, O., Köhler, S., & Dernburg, A. F. (2017) · eLife · doi:10.7554/elife.21455 · Cited by 220

A gel phase promotes condensation of liquid P granules in Caenorhabditis elegans embryos

Putnam, A., Cassani, M., Smith, J., & Seydoux, G. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0193-2 · Cited by 217

Phase transition of RNA−protein complexes into ordered hollow condensates

Alshareedah, I., Moosa, M. M., Raju, M., Potoyan, D. A., & Banerjee, P. R. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1922365117 · Cited by 208

TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea

Kovacs, G. G., Murrell, J. R., Horvath, S., Haraszti, L., Majtenyi, K., Molnar, M. J., Budka, H., Ghetti, B., & Spina, S. (2009) · Movement Disorders · doi:10.1002/mds.22697 · Cited by 198

Protein-RNA Networks Regulated by Normal and ALS-Associated Mutant HNRNPA2B1 in the Nervous System

Martinez, F. J., Pratt, G. A., Van Nostrand, E. L., Batra, R., Huelga, S. C., Kapeli, K., Freese, P., Chun, S. J., Ling, K., Gelboin-Burkhart, C., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.050 · Cited by 185

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

Phase separation-deficient TDP43 remains functional in splicing

Schmidt, H. B., Barreau, A., & Rohatgi, R. (2019) · Nature Communications · doi:10.1038/s41467-019-12740-2 · Cited by 178

Phase separation directs ubiquitination of gene-body nucleosomes

Gallego, L. D., Schneider, M., Mittal, C., Romanauska, A., Carrillo, R. M. G., Schubert, T., Pugh, B. F., & Köhler, A. (2020) · Nature · doi:10.1038/s41586-020-2097-z · Cited by 158

Evaluation of TDP-43 proteinopathy and hippocampal sclerosis in relation to APOE ε4 haplotype status: a community-based cohort study

Yang, H., Yu, L., White, C. C., Chibnik, L. B., Chhatwal, J. P., Sperling, R. A., Bennett, D., Schneider, J. A., & Jager, P. L. D. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30251-5 · Cited by 151

Liquid-crystalline phases of cholesterol/lipid bilayers as revealed by the fluorescence of trans-parinaric acid

Mateo, C. R., Acuña, A. U., & Brochon, J. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80273-0 · Cited by 144

RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy

Chen, H.-J., Topp, S. D., Hui, H. S., Zacco, E., Katarya, M., McLoughlin, C., King, A., Smith, B. N., Troakes, C., Pastore, A., et al. (2019) · Brain · doi:10.1093/brain/awz313 · Cited by 134

TDP-43 Dimerizes in Human Cells in Culture

Shiina, Y., Arima, K., Tabunoki, H., & Satoh, J. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9489-9 · Cited by 133

The mechanism of inhibition of Ran-dependent nuclear transport by cellular ATP depletion

Schwoebel, E. D., Ho, T. H., & Moore, M. S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200111077 · Cited by 131

Reappraisal of TDP-43 pathology in FTLD-U subtypes

Mackenzie, I. R., & Neumann, M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1716-8 · Cited by 119

Distinct molecular patterns of TDP-43 pathology in Alzheimer’s disease: relationship with clinical phenotypes

Tomé, S. O., Vandenberghe, R. R., Ospitalieri, S., Schoor, E. V., Tousseyn, T., Otto, M., Arnim, C. A. F. V., & Thal, D. R. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00934-5 · Cited by 108

Post-transcriptional Inhibition of Hsc70-4/HSPA8 Expression Leads to Synaptic Vesicle Cycling Defects in Multiple Models of ALS

Coyne, A. N., Lorenzini, I., Chou, C., Torvund, M., Rogers, R. S., Starr, A., Zaepfel, B. L., Levy, J., Johannesmeyer, J., Schwartz, J. C., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.028 · Cited by 106

Phase transitioned nuclear Oskar promotes cell division of Drosophila primordial germ cells

Kistler, K. E., Trcek, T., Hurd, T. R., Chen, R., Liang, F., Sall, J., Kato, M., & Lehmann, R. (2018) · eLife · doi:10.7554/elife.37949 · Cited by 101

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions

Mompeán, M., Romano, V. C., Pantoja‐Uceda, D., Stuani, C., Baralle, F. E., Buratti, E., & Laurents, D. V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.775965 · Cited by 98

An Intramolecular Salt Bridge Linking TDP43 RNA Binding, Protein Stability, and TDP43-Dependent Neurodegeneration

Flores, B. N., Li, X., Malik, A. M., Martinez, J., Beg, A. A., & Barmada, S. J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.093 · Cited by 91

Thermotropic liquid crystals from biomacromolecules

Liu, K., Chen, D., Marcozzi, A., Zheng, L., Su, J., Pesce, D., Zajączkowski, W., Kolbe, A., Pisula, W., Müllen, K., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421257111 · Cited by 87

pQuant Improves Quantitation by Keeping out Interfering Signals and Evaluating the Accuracy of Calculated Ratios

Liu, C., Song, C., Yuan, Z., Fu, Y., Chi, H., Wang, L., Fan, S., Zhang, K., Zeng, W., He, S., et al. (2014) · Analytical Chemistry · doi:10.1021/ac404246w · Cited by 85

A novel mutation P112H in the TARDBP gene associated with frontotemporal lobar degeneration without motor neuron disease and abundant neuritic amyloid plaques

Moreno, F., Rabinovici, G. D., Karydas, A., Miller, Z., Hsu, S. C., Legati, A., Fong, J. C., Schonhaut, D. R., Esselmann, H., Watson, C., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0190-6 · Cited by 72

pParse: A method for accurate determination of monoisotopic peaks in high‐resolution mass spectra

Yuan, Z., Liu, C., Wang, H., Sun, R., Fu, Y., Zhang, J., Wang, L., Chi, H., Li, Y., Xiu, L., et al. (2011) · PROTEOMICS · doi:10.1002/pmic.201100081 · Cited by 69

Inhibition of histone deacetylase 6 (HDAC6) protects against vincristine-induced peripheral neuropathies and inhibits tumor growth

Helleputte, L. V., Kater, M. S. J., Cook, D. P., Eykens, C., Rossaert, E., Haeck, W., Jaspers, T., Geens, N., Berghe, P. V., Gysemans, C. A., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.11.011 · Cited by 69

Regulation of Epidermal Growth Factor Receptor Degradation by Heterotrimeric Gαs Protein

Zheng, B., Lavoie, C. L., Tang, T., Ma, P., Meerloo, T., Beas, A. O., & Farquhar, M. G. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0446 · Cited by 57

HDAC6 Is a Bruchpilot Deacetylase that Facilitates Neurotransmitter Release

Miśkiewicz, K., Jose, L. E., Yeshaw, W. M., Valadas, J. S., Swerts, J., Munck, S., Feiguin, F. M., Dermaut, B., & Verstreken, P. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.051 · Cited by 43

Reactive nucleolar and Cajal body responses to proteasome inhibition in sensory ganglion neurons

Palanca, A., Casafont, Í., Berciano, M. T., & Lafarga, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.016 · Cited by 37

Partial demixing of RNA-protein complexes leads to intradroplet patterning in phase-separated biological condensates

Gasior, K. I., Zhao, J., McLaughlin, G. A., Forest, M. G., Gladfelter, A. S., & Newby, J. (2019) · Physical review. E · doi:10.1103/physreve.99.012411 · Cited by 32

N-terminal sequences in matrin 3 mediate phase separation into droplet-like structures that recruit TDP43 variants lacking RNA binding elements

Iradi, M. C. G., Strunk, H., Crown, A. M., Davila, R., Brown, H. H., Rodríguez-Lebrón, E., & Borchelt, D. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0260-7 · Cited by 30

A case of peripheral nerve microvasculitis associated with multiple myeloma and bortezomib treatment

Mauermann, M. L., Blumenreich, M. S., Dispenzieri, A. A., & Staff, N. P. (2012) · Muscle & Nerve · doi:10.1002/mus.23493 · Cited by 27

Accumulation of poly(A) RNA in nuclear granules enriched in Sam68 in motor neurons from the SMNΔ7 mouse model of SMA

Narcís, J. O., Tapia, O., Tarabal, O., Piedrafita, L., Calderó, J., Berciano, M. T., & Lafarga, M. (2018) · Scientific Reports · doi:10.1038/s41598-018-27821-3 · Cited by 18

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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

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