Gruijs da Silva LA, Simonetti F, Hutten S, Riemenschneider H, Sternburg EL, Pietrek LM, Gebel J, Dötsch V, Edbauer D, Hummer G, Stelzl LS and Dormann D (2022) Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation. EMBO J, 41:e108443 Link

Hutten S and Dormann D (2022) Hormone-inducible transport reporter assay to study nuclear import defects in neurodegenerative diseases. Methods in Molecular Biology (ed. Goldberg MW), pages 81–90, Springer US, New York, NY Link


Baade I*, Hutten S*, Sternburg EL, Pörschke M, Hofweber M, Dormann D# and Kehlenbach RH# (2021) The RNA-binding protein FUS is chaperoned and imported into the nucleus by a network of import receptors. J Biol Chem, 296:100659 (*indicates joint contribution, #indicates joint correspondence)  Link

Dormann D (2021) The chains of stress recovery. Science, 372:1393–1395 Link

Lenard AJ, Hutten S, Zhou Q, Usluer S, Zhang F, Bourgeois BMR, Dormann D and Madl T (2021) Phosphorylation regulates CIRBP arginine methylation, Transportin-1 binding and liquid-liquid phase separation. Front Mol Biosci, 8:1004 Link

Reber S, Jutzi D, Lindsay H, Devoy A, Mechtersheimer J, Levone BR, Domanski M, Bentmann E, Dormann D, Mühlemann O, Barabino SML and Ruepp MD (2021) The phase separation-dependent FUS interactome reveals nuclear and cytoplasmic function of liquid–liquid phase separation. Nucleic Acids Res, 49:7713–7731 Link

Sternburg EL, Gruijs da Silva LA and Dormann D (2021) Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration? Trends Biochem Sci, 47:6–22 Link


Bourgeois B, Hutten S, Gottschalk B, Hofweber M, Richter G, Sternat J, Abou-Ajram C, Göbl C, Leitinger G, Graier WF, Dormann D and Madl T (2020) Nonclassical nuclear localization signals mediate nuclear import of CIRBP. Proc Natl Acad Sci USA, 117:8503–8514 Link

Dormann D (2020) Molecular mechanisms of neurodegeneration. Semin Cell Dev Biol, 99:131–132 Link

Dormann D (2020) FG-nucleoporins caught in the act of liquid–liquid phase separation. J Cell Biol, doi: 10.1083/jcb.201910211 Link

Hutten S and Dormann D (2020) Nucleocytoplasmic transport defects in neurodegeneration - Cause or consequence?Semin Cell Dev Biol, 99:151–162 Link

Hutten S and Dormann D (2020) A quantitative assay to measure stress granule association of proteins and peptidesin semi-permeabilized human cells. Bio-protocol, 10:e3846 Link

Hutten S, Usluer S, Bourgeois B, Simonetti F, Odeh HM, Fare CM, Czuppa M, Hruska-Plochan M, Hofweber M, Polymenidou M, Shorter J, Edbauer D, Madl T and Dormann D (2020) Nuclear import receptors directly bind to arginine-rich dipeptide repeat proteins and suppress their pathological interactions. Cell Rep, 33:108538 Link


Alberti S and Dormann D (2019) Liquid-liquid phase separation in disease. Annu Rev Genet, 53:171–194 Link

Hofweber M and Dormann D (2019) Friend or foe-post-translational modifications as regulators of phase separation and RNP granule dynamics. J Biol Chem, 294:7137–7150 Link

Hutten S and Dormann D (2019) RAN translation down. Nat Neurosci, 22:1379–1380 Link

Ukmar-Godec T, Hutten S, Grieshop MP, Rezaei-Ghaleh N, Cima-Omori MS, Biernat J, Mandelkow E, Söding J, Dormann D and Zweckstetter M (2019) Lysine/RNA-interactions drive and regulate biomolecular condensation. Nat Commun, 10:2909 Link


Ederle H, Funk C, Abou-Ajram C, Hutten S, Funk EBE, Kehlenbach RH, Bailer SM and Dormann D (2018) Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1. Sci Rep, 8:7084 Link

Hock EM, Maniecka Z, Hruska-Plochan M, Reber S, Laferrière F, Sahadevan MK S, Ederle H, Gittings L, Pelkmans L, Dupuis L, Lashley T, Ruepp MD, Dormann D and Polymenidou M (2018) Hypertonic stress causes cytoplasmic translocation of neuronal, but not astrocytic, FUS due to impaired transportin function. Cell Rep, 24:987-1000.e7 Link

Hofweber M, Hutten S, Bourgeois B, Spreitzer E, Niedner-Boblenz A, Schifferer M, Ruepp MD, Simons M, Niessing D, Madl T and Dormann D (2018) Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylation. Cell, 173:706-719.e13 Link

Simandi Z, Pajer K, Karolyi K, Sieler T, Jiang LL, Kolostyak Z, Sari Z, Fekecs Z, Pap A, Patsalos A, Contreras GA, Reho B, Papp Z, Guo X, Horvath A, Kiss G, Keresztessy Z, Vámosi G, Hickman J, Xu H, Dormann D, Hortobagyi T, Antal M, Nógrádi A and Nagy L (2018) Arginine methyltransferase PRMT8 provides cellular stress tolerance in aging motoneurons. J Neurosci, 38:7683–7700 Link

Woodsmith J, Casado-Medrano V, Benlasfer N, Eccles RL, Hutten S, Heine CL, Thormann V, Abou-Ajram C, Rocks O, Dormann D and Stelzl U (2018) Interaction modulation through arrays of clustered methyl-arginine protein modifications. Life Sci Alliance, 1:e201800178 Link


Ederle H and Dormann D (2017) TDP-43 and FUS en route from the nucleus to the cytoplasm. FEBS Lett, 591:1489–1507 Link

Khosravi B, Hartmann H, May S, Möhl C, Ederle H, Michaelsen M, Schludi MH, Dormann D and Edbauer D (2017) Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD. Hum Mol Genet, 26:790–800 Link

Scekic-Zahirovic J, Oussini H El, Mersmann S, Drenner K, Wagner M, Sun Y, Allmeroth K, Dieterlé S, Sinniger J, Dirrig-Grosch S, René F, Dormann D, Haass C, Ludolph AC, Lagier-Tourenne C, Storkebaum E and Dupuis L (2017) Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis. Acta Neuropathol, 133:887–906 Link


Bowden HA and Dormann D (2016) Altered mRNP granule dynamics in FTLD pathogenesis. J Neurochem, 138 Suppl:112–133 Link

Dormann D (2016) FUScinating insights into motor neuron degeneration. EMBO J, 35:1015–1017 Link

Hutten S and Dormann D (2016) hnRNPA2/B1 function in neurodegeneration: it’s a gain, not a loss. Neuron, 92:672–674 Link

Suárez-Calvet M, Neumann M, Arzberger T, Abou-Ajram C, Funk E, Hartmann H, Edbauer D, Kremmer E, Göbl C, Resch M, Bourgeois B, Madl T, Reber S, Jutzi D, Ruepp MD, Mackenzie IRA, Ansorge O, Dormann D and Haass C (2016) Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS. Acta Neuropathol, 131:587–604 Link


Jäckel S, Summerer AK, Thömmes CM, Pan X, Voigt A, Schulz JB, Rasse TM, Dormann D, Haass C and Kahle PJ (2015) Nuclear import factor transportin and arginine methyltransferase 1 modify FUS neurotoxicity in Drosophila. Neurobiol Dis, 74:76–88 Link


Bentmann E, Haass C and Dormann D (2013) Stress granules in neurodegeneration--lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma. FEBS J, 280:4348–4370 Link

Dormann D and Haass C (2013) Fused in sarcoma (FUS): an oncogene goes awry in neurodegeneration. Mol Cell Neurosci, 56:475–486 Link


Dormann D, Madl T, Valori CF, Bentmann E, Tahirovic S, Abou-Ajram C, Kremmer E, Ansorge O, Mackenzie IRA, Neumann M and Haass C (2012) Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. EMBO J, 31:4258–4275 Link


Capell A, Liebscher S, Fellerer K, Brouwers N, Willem M, Lammich S, Gijselinck I, Bittner T, Carlson AM, Sasse F, Kunze B, Steinmetz H, Jansen R, Dormann D, Sleegers K, Cruts M, Herms J, Van Broeckhoven C and Haass C (2011) Rescue of progranulin deficiency associated with frontotemporal lobar degeneration by alkalizing reagents and inhibition of vacuolar ATPase. J Neurosci, 31:1885–1894 Link

Dormann D and Haass C (2011) TDP-43 and FUS: a nuclear affair. Trends Neurosci, 34:339–348 Link


Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, Hruscha A, Than ME, Mackenzie IRA, Capell A, Schmid B, Neumann M and Haass C (2010) ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J, 29:2841–2857 Link


Dormann D, Capell A, Carlson AM, Shankaran SS, Rodde R, Neumann M, Kremmer E, Matsuwaki T, Yamanouchi K, Nishihara M and Haass C (2009) Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J Neurochem, 110:1082–1094 Link


Schmid D and Münz C (2008) Localization and MHC class II presentation of antigens targeted for macroautophagy. Methods Mol Biol, 445:213–225 Link

Note: Dormann D = Schmid D before 2007


Lünemann JD, Schmidt J, Schmid D, Barthel K, Wrede A, Dalakas MC and Münz C (2007) Beta-amyloid is a substrate of autophagy in sporadic inclusion body myositis. Ann Neurol, 61:476–483 Link

Schmid D and Münz C (2007) Innate and adaptive immunity through autophagy. Immunity, 27:11–21 Link

Schmid D and Münz C (2007) Immune surveillance via self digestion. Autophagy, 3:133–135 Link

Schmid D, Pypaert M and Münz C (2007) Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes. Immunity, 26:79–92 Link


Schmid D, Dengjel J, Schoor O, Stevanovic S and Münz C (2006) Autophagy in innate and adaptive immunity against intracellular pathogens. J Mol Med (Berl), 84:194–202 Link


Paludan C, Schmid D, Landthaler M, Vockerodt M, Kube D, Tuschl T and Münz C (2005) Endogenous MHC class II processing of a viral nuclear antigen after autophagy. Science, 307:593–596 Link

Schmid D and Münz C (2005) Immune surveillance of intracellular pathogens via autophagy. Cell Death Differ, 12 Suppl 2:1519–1527 Link


Ferlazzo G, Pack M, Thomas D, Paludan C, Schmid D, Strowig T, Bougras G, Muller WA, Moretta L and Münz C (2004) Distinct roles of IL-12 and IL-15 in human natural killer cell activation by dendritic cells from secondary lymphoid organs. Proc Natl Acad Sci USA, 101:16606–16611 Link