**Author details**

Oxana V. Galzitskaya

Address all correspondence to: ogalzit@vega.protres.ru

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia

## **References**


[15] Lobanov MY, Sokolovskiy IV, Galzitskaya OV. IsUnstruct: prediction of the residue status to be ordered or disordered in the protein chain by a method based on the Ising model. J. Biomol. Struct. Dyn. 2013;31:1034–43.

**References**

34.

A. 2000;97:5129–34.

2002;48:134–40.

Acad. Sci. U. S. A. 2004;101:10584–9.

aggregates. FEBS J. 2005;272:2231–6.

1999;24:329–32.

114 Update on Amyotrophic Lateral Sclerosis

Struct. Biol. 2000;10:60–8.

[1] Söderberg L, Dahlqvist C, Kakuyama H, Thyberg J, Ito A, Winblad B, et al. Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant

[2] Dobson CM. Protein misfolding, evolution and disease. Trends Biochem. Sci.

[3] Rochet JC, Lansbury PT. Amyloid fibrillogenesis: themes and variations. Curr. Opin.

[4] Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured

[5] Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002;27:527–33.

[6] Linding R, Schymkowitz J, Rousseau F, Diella F, Serrano L. A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsi‐

[7] Rauscher S, Baud S, Miao M, Keeley FW, Pomès R. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure 2006. 14:1667–76.

[8] Kovacs E, Tompa P, Liliom K, Kalmar L. Dual coding in alternative reading frames correlates with intrinsic protein disorder. Proc. Natl. Acad. Sci. U. S. A. 2010;107:5429–

[9] Tenidis K, Waldner M, Bernhagen J, Fischle W, Bergmann M, Weber M, et al. Identifi‐ cation of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloi‐

[10] von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc. Natl. Acad. Sci. U. S.

[11] Ivanova MI, Sawaya MR, Gingery M, Attinger A, Eisenberg D. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc. Natl.

[12] Huntley MA, Golding GB. Simple sequences are rare in the Protein Data Bank. Proteins.

[13] Lobanov MY, Galzitskaya OV. Disordered patterns in clustered Protein Data Bank and

[14] Lobanov MY, Sokolovskiy IV, Galzitskaya OV. HRaP: database of occurrence of HomoRepeats and patterns in proteomes. Nucleic Acids Res. 2014;42:D273–8.

dogenic and cytotoxic properties. J. Mol. Biol. 2000;295:1055–71.

in eukaryotic and bacterial proteomes. PLoS One. 2011;6:e27142.

under physiologic conditions? Proteins. 2000;41:415–27.

cally disordered proteins. J. Mol. Biol. 2004;342:345–53.


[42] Kino Y, Washizu C, Aquilanti E, Okuno M, Kurosawa M, Yamada M, et al. Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations. Nucleic Acids Res. 2011;39:2781–98.

[28] Liu-Yesucevitz L, Bassell GJ, Gitler AD, Hart AC, Klann E, Richter JD, et al. Local RNA translation at the synapse and in disease. J. Neurosci. Off. J. Soc. Neurosci.

[29] Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell.

[30] Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions andilluminates sequence features ofprionogenicproteins. Cell. 2009;137:146–58.

[31] King OD, Gitler AD, Shorter J. The tip of the iceberg: RNA-binding proteins with prion-

[32] Aguzzi A, Rajendran L. The transcellular spread of cytosolic amyloids, prions, and

[33] Couthouis J, Hart MP, Shorter J, DeJesus-Hernandez M, Erion R, Oristano R, et al. A yeast functional screen predicts new candidate ALS disease genes. Proc. Natl. Acad.

[34] King OD, Gitler AD, Shorter J. The tip of the iceberg: RNA-binding proteins with prion-

[35] Tan AY, Manley JL. The TET family of proteins: functions and roles in disease. J. Mol.

[36] Zinszner H, Albalat R, Ron D. A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP. Genes Dev.

[37] Bentmann E, Neumann M, Tahirovic S, Rodde R, Dormann D, Haass C. Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein

[38] Lerga A, Hallier M, Delva L, Orvain C, Gallais I, Marie J, et al. Identification of an RNA binding specificity for the potential splicing factor TLS. J. Biol. Chem. 2001;276:6807–16.

[39] Iko Y, Kodama TS, Kasai N, Oyama T, Morita EH, Muto T, et al. Domain architectures and characterization of an RNA-binding protein, TLS. J. Biol. Chem. 2004;279:44834–40.

[40] GalJ,Zhang J, KwinterDM,ZhaiJ,Jia H,Jia J, et al. Nuclearlocalization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol. Aging. 2011;32:27–40. [41] Ito D, Seki M, Tsunoda Y, Uchiyama H, Suzuki N. Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS. Ann. Neurol. 2011;69:152–

of 43 kDa (TDP-43). J. Biol. Chem. 2012;287:23079–94.

like domains in neurodegenerative disease. Brain Res. 2012;1462:61–80.

like domains in neurodegenerative disease. Brain Res. 2012;1462:61–80.

2011;31:16086–93.

116 Update on Amyotrophic Lateral Sclerosis

2012;149:753–67.

prionoids. Neuron. 2009;64:783–90.

Sci. 2011;108:20881–90.

Cell Biol. 2009;1:82–92.

1994;8:2513–26.

62.


[67] Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, et al. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol. 2011;9:e1000614.

[54] Shelkovnikova TA, Robinson HK, Connor-Robson N, Buchman VL. Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the

[55] Bossy-Wetzel E, Schwarzenbacher R, Lipton SA. Molecular pathways to neurodegen‐

[56] Rabin SJ, Kim JMH, Baughn M, Libby RT, Kim YJ, Fan Y, et al. Sporadic ALS has compartment-specific aberrant exon splicing and altered cell-matrix adhesion biology.

[57] Orozco D, Edbauer D. FUS-mediated alternative splicing in the nervous system:

[58] Xia R, Liu Y, Yang L, Gal J, Zhu H, Jia J. Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fus-mediated

[59] Vaccaro A, Tauffenberger A, Aggad D, Rouleau G, Drapeau P, Parker JA. Mutant TDP-43 and FUS cause age-dependent paralysis and neurodegeneration in *C. elegans*.

[60] Belzil VV, Valdmanis PN, Dion PA, Daoud H, Kabashi E, Noreau A, et al. Mutations in FUS cause FALS and SALS in French and French Canadian populations. Neurology.

[61] Ju S, Tardiff DF, Han H, Divya K, Zhong Q, Maquat LE, et al. A yeast model of FUS/

[62] Murakami T, Yang S-P, Xie L, Kawano T, Fu D, Mukai A, et al. ALS mutations in FUS cause neuronal dysfunction and death in *Caenorhabditis elegans* by a dominant gain-of-

[63] Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell. 2009;137:146–

[64] Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating

[65] Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, et al. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS.

[66] Shelkovnikova TA, Robinson HK, Connor-Robson N, Buchman VL. Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the

TLS-dependent cytotoxicity. PLoS Biol. 2011;9:e1001052.

function mechanism. Hum. Mol. Genet. 2012;21:1–9.

Sup35 prion conformers. Science. 2004;304:1793–7.

cytoplasm. Cell Cycle Georget. Tex. 2013;12:3194–202.

consequences for ALS and FTLD. J. Mol. Med (Berl.) 2013;91:1343–54.

cytoplasm. Cell Cycle Georget. Tex. 2013;12:3194–202.

eration. Nat. Med. 2004;10 Suppl:S2–9.

Hum. Mol. Genet. 2010;19:313–28.

ALS. Mol. Neurodegener. 2012;7:10.

PLoS One. 2012;7:e31321.

PLoS Biol. 2011;9:e1000614.

2009;73:1176–9.

118 Update on Amyotrophic Lateral Sclerosis

58.

