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Department of Chemistry and Biochemistry, United States; email: gdebelouchina@ucsd.edu \n Chemicals/CAS: amyloid, 11061-24-8; Amyloid; RNA-Binding Protein FUS \n Funding details: National Institutes of Health, NIH, P30 AG062429, P41 EB002031, R21 AG069064, T32 GM112584 \n Funding details: National Institute of Neurological Disorders and Stroke, NINDS, NS047101 \n Funding text 1: This work was supported by a Research Education Component associated with NIH Grant P30 AG062429 , an R21 AG069064 award to G.T.D., a T32 GM112584 fellowship to R.F.B., the BRC for NMR Molecular Imaging of Proteins at UCSD ( P41 EB002031 ), and the UCSD Microscopy Core ( NINDS NS047101 ).\nCited By :5 \n Export Date: 6 September 2021 \n CODEN: BIOJA \n Correspondence Address: Debelouchina, G.T.; Department of Chemistry and Biochemistry, United States; email: gdebelouchina@ucsd.edu \n Chemicals/CAS: amyloid, 11061-24-8; Amyloid; RNA-Binding Protein FUS \n Funding details: National Institutes of Health, NIH, P30 AG062429, P41 EB002031, R21 AG069064, T32 GM112584 \n Funding details: National Institute of Neurological Disorders and Stroke, NINDS, NS047101 \n Funding text 1: This work was supported by a Research Education Component associated with NIH Grant P30 AG062429 , an R21 AG069064 award to G.T.D., a T32 GM112584 fellowship to R.F.B., the BRC for NMR Molecular Imaging of Proteins at UCSD ( P41 EB002031 ), and the UCSD Microscopy Core ( NINDS NS047101 ).", "unhandledTickets" : 0, "deleted" : false, "lastRefresh" : "2023-03-11T16:16:45.516+0000", "lastModified" : "2023-03-11T16:15:02.076+0000", "created" : "2021-03-25T09:30:59.327+0000", "creator" : { "otype" : "Author", "mtid" : 10001424, "link" : "/api/author/10001424", "label" : "Tompa Péter (Enzimológia)", "familyName" : "Tompa", "givenName" : "Péter", "published" : true, "oldId" : 10001424, "snippet" : true }, "lastDuplumOK" : "2023-03-11T16:15:02.436+0000", "lastDuplumSearch" : "2023-03-11T16:15:02.436+0000", "core" : false, "citation" 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The mechanisms underlying the connection between these phase transitions have been challenging to study due to the heterogeneous and dynamic nature of the states formed during the maturation of LLPS protein droplets into gels and solid aggregates. Here, we interrogate the liquid-to-solid transition of the low-complexity domain of the RNA-binding protein FUS (FUS LC), which has been shown to adopt LLPS, gel-like, and amyloid states. We employ magic-angle-spinning NMR spectroscopy, which has allowed us to follow these transitions in real time and with residue-specific resolution. We observe the development of β-sheet structure through the maturation process and show that the final state of FUS LC fibrils produced after LLPS is distinct from that grown from fibrillar seeds. We also apply our methodology to FUS LC G156E, a clinically relevant FUS mutant that exhibits accelerated fibrillization rates. We observe significant changes in dynamics during the transformation of the FUS LC G156E construct and begin to unravel the sequence specific contributions to this phenomenon with computational studies of the phase-separated state of FUS LC and FUS LC G156E. © 2021 Biophysical Society", "digital" : null, "printed" : null, "sourceYear" : 2021, "foreignEdition" : true, "foreignLanguage" : true, "fullPublication" : true, "conferencePublication" : false, "nationalOrigin" : null, "missingAuthor" : false, "oaType" : "NONE", "oaCheckDate" : "2023-03-11", "oaFree" : false, "citationCount" : 0, "citationCountUnpublished" : 0, "citationCountWoOther" : 0, "independentCitCountWoOther" : 0, "doiCitationCount" : 0, "wosCitationCount" : 0, "scopusCitationCount" : 0, "independentCitationCount" : 0, "unhandledCitationCount" : 0, "citingPubCount" : 0, "independentCitingPubCount" : 0, "unhandledCitingPubCount" : 0, "citedPubCount" : 2, "citedCount" : 2, "ratings" : [ { "otype" : "SjrRating", "mtid" : 11196568, "link" : "/api/sjrrating/11196568", "label" : "sjr:Q1 (2021) Scopus - Biophysics BIOPHYSICAL JOURNAL 0006-3495 1542-0086", "listPos" : 15, "rankValue" : 0.24, "type" : "journal", "ratingType" : { "otype" : "RatingType", "mtid" : 10002, "link" : "/api/ratingtype/10002", "label" : "sjr", "code" : "sjr", "published" : true, "snippet" : true }, "subject" : { "otype" : "ClassificationExternal", "mtid" : 1304, "link" : "/api/classificationexternal/1304", "label" : "Scopus - Biophysics", "published" : true, "oldId" : 1304, "snippet" : true }, "ranking" : "Q1", "calculation" : "DIRECT", "published" : true, "snippet" : true } ], "ratingsForSort" : "Q1", "references" : [ { "otype" : "Reference", "mtid" : 19269537, "link" : "/api/reference/19269537", "label" : "1. Wolozin, B., Ivanov, P., Stress granules and neurodegeneration (2019) Nat. Rev. Neurosci, 20, pp. 649-666", "listPosition" : 1, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269536, "link" : "/api/reference/19269536", "label" : "2. Wheeler, J.R., Matheny, T., Parker, R., Distinct stages in stress granule assembly and disassembly (2016) eLife, 5, p. e18413", "listPosition" : 2, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269535, "link" : "/api/reference/19269535", "label" : "3. Sawaya, M.R., Sambashivan, S., Eisenberg, D., Atomic structures of amyloid cross-beta spines reveal varied steric zippers (2007) Nature, 447, pp. 453-457", "listPosition" : 3, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269534, "link" : "/api/reference/19269534", "label" : "4. Takegoshi, K., Nakamura, S., Terao, T., 13C–1H dipolar-driven 13C–13C recoupling without 13C rf irradiation in nuclear magnetic resonance of rotating solids (2003) J. Chem. Phys, 118, pp. 2325-2341", "listPosition" : 4, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269533, "link" : "/api/reference/19269533", "label" : "5. Kato, M., Han, T.W., McKnight, S.L., Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels (2012) Cell, 149, pp. 753-767", "listPosition" : 5, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269532, "link" : "/api/reference/19269532", "label" : "6. Pines, A., Gibby, M.G., Waugh, J.S., Proton-enhanced nuclear induction spectroscopy. A method for high resolution NMR of dilute spins in solids (1972) J. Chem. Phys, 56, pp. 1776-1777", "listPosition" : 6, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269531, "link" : "/api/reference/19269531", "label" : "7. Hartmann, S.R., Hahn, E.L., Nuclear double resonance in the rotating frame (1962) Phys. Rev, 128, pp. 2042-2053", "listPosition" : 7, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269530, "link" : "/api/reference/19269530", "label" : "8. Debelouchina, G.T., Platt, G.W., Griffin, R.G., Magic angle spinning NMR analysis of β2-microglobulin amyloid fibrils in two distinct morphologies (2010) J. Am. Chem. Soc, 132, pp. 10414-10423", "listPosition" : 8, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269529, "link" : "/api/reference/19269529", "label" : "9. Andronesi, O.C., Becker, S., Baldus, M., Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy (2005) J. Am. Chem. Soc, 127, pp. 12965-12974", "listPosition" : 9, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269528, "link" : "/api/reference/19269528", "label" : "10. Kroschwald, S., Maharana, S., Simon, A., Hexanediol: a chemical probe to investigate the material properties of membrane-less compartments (2017) Matters (Zur.), 3. , e201702000010", "listPosition" : 10, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269527, "link" : "/api/reference/19269527", "label" : "11. Stsiapura, V.I., Maskevich, A.A., Turoverov, K.K., Thioflavin T as a molecular rotor: fluorescent properties of thioflavin T in solvents with different viscosity (2008) J. Phys. Chem. B, 112, pp. 15893-15902", "listPosition" : 11, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269526, "link" : "/api/reference/19269526", "label" : "12. Naiki, H., Higuchi, K., Takeda, T., Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1 (1989) Anal. Biochem, 177, pp. 244-249", "listPosition" : 12, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269525, "link" : "/api/reference/19269525", "label" : "13. Nomura, T., Watanabe, S., Furukawa, Y., Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis (2014) J. Biol. Chem, 289, pp. 1192-1202", "listPosition" : 13, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269524, "link" : "/api/reference/19269524", "label" : "14. Murakami, T., Qamar, S., St George-Hyslop, P., ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function (2015) Neuron, 88, pp. 678-690", "listPosition" : 14, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269523, "link" : "/api/reference/19269523", "label" : "15. Lee, M., Ghosh, U., Tycko, R., Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS (2020) Nat. Commun, 11, p. 5735", "listPosition" : 15, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269522, "link" : "/api/reference/19269522", "label" : "16. Stukowski, A., Visualization and analysis of atomistic simulation data with OVITO–the Open Visualization Tool (2009) Model. Simul. Mater. Sci. Eng, 18, p. 015012", "listPosition" : 16, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269521, "link" : "/api/reference/19269521", "label" : "17. Martínez, L., Andrade, R., Martínez, J.M., PACKMOL: a package for building initial configurations for molecular dynamics simulations (2009) J. Comput. Chem, 30, pp. 2157-2164", "listPosition" : 17, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269520, "link" : "/api/reference/19269520", "label" : "18. Klein, C., Sallai, J., Cummings, P.T., A hierarchical, component based approach to screening properties of soft matter (2016) Foundations of Molecular Modeling and Simulation: Select Papers from FOMMS 2015, pp. 79-92. , R.Q. Snurr C.S. Adjiman D.A. Kofke R.Q. Snurr C.S. Adjiman D.A. Kofke", "listPosition" : 18, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269519, "link" : "/api/reference/19269519", "label" : "19. Kapcha, L.H., Rossky, P.J., A simple atomic-level hydrophobicity scale reveals protein interfacial structure (2014) J. Mol. Biol, 426, pp. 484-498", "listPosition" : 19, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269518, "link" : "/api/reference/19269518", "label" : "20. (2020), mphowardlab/azplugins mphowardlab", "listPosition" : 20, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269517, "link" : "/api/reference/19269517", "label" : "21. Conicella, A.E., Dignon, G.L., Fawzi, N.L., TDP-43 α-helical structure tunes liquid-liquid phase separation and function (2020) Proc. Natl. Acad. Sci. USA, 117, pp. 5883-5894", "listPosition" : 21, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269516, "link" : "/api/reference/19269516", "label" : "22. Schuster, B.S., Dignon, G.L., Mittal, J., Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior (2020) Proc. Natl. Acad. Sci. USA, 117, pp. 11421-11431", "listPosition" : 22, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269515, "link" : "/api/reference/19269515", "label" : "23. Anderson, J.A., Glaser, J., Glotzer, S.C., HOOMD-blue: a Python package for high-performance molecular dynamics and hard particle Monte Carlo simulations (2020) Comput. Mater. Sci, 173, p. 109363", "listPosition" : 23, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269514, "link" : "/api/reference/19269514", "label" : "24. Fritzsching, K.J., Yang, Y., Hong, M., Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information (2013) J. Biomol. NMR, 56, pp. 155-167", "listPosition" : 24, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269513, "link" : "/api/reference/19269513", "label" : "25. Helmus, J.J., Jaroniec, C.P., Nmrglue: an open source Python package for the analysis of multidimensional NMR data (2013) J. Biomol. NMR, 55, pp. 355-367", "listPosition" : 25, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269512, "link" : "/api/reference/19269512", "label" : "26. Heinig, M., Frishman, D., STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins (2004) Nucleic Acids Res, 32, pp. W500-W502", "listPosition" : 26, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269511, "link" : "/api/reference/19269511", "label" : "27. Lee, W., Yu, W., Markley, J.L., PACSY, a relational database management system for protein structure and chemical shift analysis (2012) J. Biomol. NMR, 54, pp. 169-179", "listPosition" : 27, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269510, "link" : "/api/reference/19269510", "label" : "28. Lee, W., Westler, W.M., Markley, J.L., PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy (2009) Bioinformatics, 25, pp. 2085-2087", "listPosition" : 28, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269509, "link" : "/api/reference/19269509", "label" : "29. Harris, C.R., Millman, K.J., Oliphant, T.E., Array programming with NumPy (2020) Nature, 585, pp. 357-362", "listPosition" : 29, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269508, "link" : "/api/reference/19269508", "label" : "30. Hunter, J.D., Matplotlib: a 2D graphics environment (2007) Comput. Sci. Eng, 9, pp. 90-95", "listPosition" : 30, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269507, "link" : "/api/reference/19269507", "label" : "31. McKinney, W., Data structures for statistical computing in Python (2010) Proceedings of the 9th Python in Science Conference, 445, pp. 56-61", "listPosition" : 31, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269506, "link" : "/api/reference/19269506", "label" : "32. Virtanen, P., Gommers, R., van Mulbregt, P., SciPy 1.0: fundamental algorithms for scientific computing in Python (2020) Nat. Methods, 17, pp. 261-272", "listPosition" : 32, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269505, "link" : "/api/reference/19269505", "label" : "33. Rueden, C.T., Schindelin, J., Eliceiri, K.W., ImageJ2: ImageJ for the next generation of scientific image data (2017) BMC Bioinformatics, 18, p. 529", "listPosition" : 33, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269504, "link" : "/api/reference/19269504", "label" : "34. Schindelin, J., Arganda-Carreras, I., Cardona, A., Fiji: an open-source platform for biological-image analysis (2012) Nat. Methods, 9, pp. 676-682", "listPosition" : 34, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269503, "link" : "/api/reference/19269503", "label" : "35. Monahan, Z., Ryan, V.H., Fawzi, N.L., Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity (2017) EMBO J, 36, pp. 2951-2967", "listPosition" : 35, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269502, "link" : "/api/reference/19269502", "label" : "36. Ackermann, B.E., Debelouchina, G.T., Heterochromatin protein HP1α gelation dynamics revealed by solid-state NMR spectroscopy (2019) Angew. Chem. Int.Ed, 58, pp. 6300-6305", "listPosition" : 36, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269501, "link" : "/api/reference/19269501", "label" : "37. Matlahov, I., van der Wel, P.C.A., Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR (2018) Methods, 148, pp. 123-135", "listPosition" : 37, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269500, "link" : "/api/reference/19269500", "label" : "38. Takegoshi, K., Nakamura, S., Terao, T., 13C–1H dipolar-assisted rotational resonance in magic-angle spinning NMR (2001) Chem. Phys. Lett, 344, pp. 631-637", "listPosition" : 38, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269499, "link" : "/api/reference/19269499", "label" : "39. Baldus, M., Meier, B.H., Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the through-bond connectivity (1996) J. Magn. Reson. A, 121, pp. 65-69", "listPosition" : 39, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269498, "link" : "/api/reference/19269498", "label" : "40. Maricq, M.M., Waugh, J.S., NMR in rotating solids (1979) J. Chem. Phys, 70, pp. 3300-3316", "listPosition" : 40, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269497, "link" : "/api/reference/19269497", "label" : "41. Andrew, E.R., Bradbury, A., Eades, R.G., Nuclear magnetic resonance spectra from a crystal rotated at high speed (1958) Nature, 182, p. 1659", "listPosition" : 41, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269496, "link" : "/api/reference/19269496", "label" : "42. Marchanka, A., Simon, B., Carlomagno, T., RNA structure determination by solid-state NMR spectroscopy (2015) Nat. Commun, 6, p. 7024", "listPosition" : 42, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269495, "link" : "/api/reference/19269495", "label" : "43. Mandala, V.S., Hong, M., High-sensitivity protein solid-state NMR spectroscopy (2019) Curr. Opin. Struct. Biol, 58, pp. 183-190", "listPosition" : 43, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269494, "link" : "/api/reference/19269494", "label" : "44. Kennedy, S.B., deAzevedo, E.R., Hong, M., Dynamic structure of a protein hydrogel: a solid-state NMR study (2001) Macromolecules, 34, pp. 8675-8685", "listPosition" : 44, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269493, "link" : "/api/reference/19269493", "label" : "45. Ader, C., Frey, S., Baldus, M., Amyloid-like interactions within nucleoporin FG hydrogels (2010) Proc. Natl. Acad. Sci. USA, 107, pp. 6281-6285", "listPosition" : 45, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269492, "link" : "/api/reference/19269492", "label" : "46. Iadanza, M.G., Silvers, R., Radford, S.E., The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism (2018) Nat. Commun, 9, p. 4517", "listPosition" : 46, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269491, "link" : "/api/reference/19269491", "label" : "47. Ding, X., Sun, F., Luo, S.-Z., Amyloid-forming segment induces aggregation of FUS-LC domain from phase separation modulated by site-specific phosphorylation (2020) J. Mol. Biol, 432, pp. 467-483", "listPosition" : 47, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269490, "link" : "/api/reference/19269490", "label" : "48. Murray, D.T., Tycko, R., Side chain hydrogen-bonding interactions within amyloid-like fibrils formed by the low-complexity domain of FUS: evidence from solid state nuclear magnetic resonance spectroscopy (2020) Biochemistry, 59, pp. 364-378", "listPosition" : 48, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269489, "link" : "/api/reference/19269489", "label" : "49. Banani, S.F., Rice, A.M., Rosen, M.K., Compositional control of phase-separated cellular bodies (2016) Cell, 166, pp. 651-663", "listPosition" : 49, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269488, "link" : "/api/reference/19269488", "label" : "50. Molliex, A., Temirov, J., Taylor, J.P., Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization (2015) Cell, 163, pp. 123-133", "listPosition" : 50, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269487, "link" : "/api/reference/19269487", "label" : "51. Murthy, A.C., Dignon, G.L., Fawzi, N.L., Molecular interactions underlying liquid-liquid phase separation of the FUS low-complexity domain (2019) Nat. Struct. Mol. Biol, 26, pp. 637-648", "listPosition" : 51, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269486, "link" : "/api/reference/19269486", "label" : "52. Burke, K.A., Janke, A.M., Fawzi, N.L., Residue-by-Residue view of in vitro FUS granules that bind the C-terminal domain of RNA polymerase II (2015) Mol. Cell, 60, pp. 231-241", "listPosition" : 52, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269485, "link" : "/api/reference/19269485", "label" : "53. Dignon, G.L., Best, R.B., Mittal, J., Biomolecular phase separation: from molecular driving forces to macroscopic properties (2020) Annu. Rev. Phys. Chem, 71, pp. 53-75", "listPosition" : 53, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269484, "link" : "/api/reference/19269484", "label" : "54. Feric, M., Vaidya, N., Brangwynne, C.P., Coexisting liquid phases underlie nucleolar subcompartments (2016) Cell, 165, pp. 1686-1697", "listPosition" : 54, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269483, "link" : "/api/reference/19269483", "label" : "55. Pak, C.W., Kosno, M., Rosen, M.K., Sequence determinants of intracellular phase separation by complex coacervation of a disordered protein (2016) Mol. Cell, 63, pp. 72-85", "listPosition" : 55, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269482, "link" : "/api/reference/19269482", "label" : "56. Dignon, G.L., Zheng, W., Mittal, J., Sequence determinants of protein phase behavior from a coarse-grained model (2018) PLOS Comput. Biol, 14, p. e1005941", "listPosition" : 56, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269481, "link" : "/api/reference/19269481", "label" : "57. Brangwynne, C.P., Tompa, P., Pappu, R.V., Polymer physics of intracellular phase transitions (2015) Nat. Phys, 11, pp. 899-904", "listPosition" : 57, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269480, "link" : "/api/reference/19269480", "label" : "58. van der Lee, R., Buljan, M., Babu, M.M., Classification of intrinsically disordered regions and proteins (2014) Chem. Rev, 114, pp. 6589-6631", "listPosition" : 58, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269479, "link" : "/api/reference/19269479", "label" : "59. Martin, E.W., Mittag, T., Relationship of sequence and phase separation in protein low-complexity regions (2018) Biochemistry, 57, pp. 2478-2487", "listPosition" : 59, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269478, "link" : "/api/reference/19269478", "label" : "60. Mittag, T., Forman-Kay, J.D., Atomic-level characterization of disordered protein ensembles (2007) Curr. Opin. Struct. Biol, 17, pp. 3-14", "listPosition" : 60, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269477, "link" : "/api/reference/19269477", "label" : "61. Mitrea, D.M., Chandra, B., Kriwacki, R.W., Methods for physical characterization of phase-separated bodies and membrane-less organelles (2018) J. Mol. Biol, 430, pp. 4773-4805", "listPosition" : 61, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269476, "link" : "/api/reference/19269476", "label" : "62. Liu, Z., Zhang, S., Liu, C., Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation (2020) Nat. Struct. Mol. Biol, 27, pp. 363-372", "listPosition" : 62, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269475, "link" : "/api/reference/19269475", "label" : "63. Lin, Y., Protter, D.S., Parker, R., formation and maturation of phase-separated liquid droplets by RNA-binding proteins (2015) Mol. Cell, 60, pp. 208-219", "listPosition" : 63, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269474, "link" : "/api/reference/19269474", "label" : "64. Patel, A., Lee, H.O., Alberti, S., A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation (2015) Cell, 162, pp. 1066-1077", "listPosition" : 64, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269473, "link" : "/api/reference/19269473", "label" : "65. Babinchak, W.M., Haider, R., Surewicz, W.K., The role of liquid-liquid phase separation in aggregation of the TDP-43 low-complexity domain (2019) J. Biol. Chem, 294, pp. 6306-6317", "listPosition" : 65, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269472, "link" : "/api/reference/19269472", "label" : "66. Gui, X., Luo, F., Li, D., Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly (2019) Nat. Commun, 10, p. 2006", "listPosition" : 66, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269471, "link" : "/api/reference/19269471", "label" : "67. Murray, D.T., Kato, M., Tycko, R., Structure of FUS protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains (2017) Cell, 171, pp. 615-627.e16", "listPosition" : 67, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269470, "link" : "/api/reference/19269470", "label" : "68. Li, Y.R., King, O.D., Gitler, A.D., Stress granules as crucibles of ALS pathogenesis (2013) J. Cell Biol, 201, pp. 361-372", "listPosition" : 68, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269469, "link" : "/api/reference/19269469", "label" : "69. Tuttle, M.D., Comellas, G., Rienstra, C.M., Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein (2016) Nat. Struct. Mol. Biol, 23, pp. 409-415", "listPosition" : 69, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269468, "link" : "/api/reference/19269468", "label" : "70. Araki, K., Yagi, N., Mochizuki, H., Parkinson's disease is a type of amyloidosis featuring accumulation of amyloid fibrils of α-synuclein (2019) Proc. Natl. Acad. Sci. USA, 116, pp. 17963-17969", "listPosition" : 70, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269467, "link" : "/api/reference/19269467", "label" : "71. Ray, S., Singh, N., Maji, S.K., α-Synuclein aggregation nucleates through liquid-liquid phase separation (2020) Nat. Chem, 12, pp. 705-716", "listPosition" : 71, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269466, "link" : "/api/reference/19269466", "label" : "72. Schweighauser, M., Shi, Y., Goedert, M., Structures of α-synuclein filaments from multiple system atrophy (2020) Nature, 585, pp. 464-469", "listPosition" : 72, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269465, "link" : "/api/reference/19269465", "label" : "73. Ambadipudi, S., Reddy, J.G., Zweckstetter, M., Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau (2019) Chem. Sci. (Camb.), 10, pp. 6503-6507", "listPosition" : 73, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269464, "link" : "/api/reference/19269464", "label" : "74. Ambadipudi, S., Biernat, J., Zweckstetter, M., Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) Nat. Commun, 8, p. 275", "listPosition" : 74, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269463, "link" : "/api/reference/19269463", "label" : "75. Dregni, A.J., Mandala, V.S., Hong, M., In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments (2019) Proc. Natl. Acad. Sci. USA, 116, pp. 16357-16366", "listPosition" : 75, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269462, "link" : "/api/reference/19269462", "label" : "76. Wegmann, S., Eftekharzadeh, B., Hyman, B.T., Tau protein liquid-liquid phase separation can initiate tau aggregation (2018) EMBO J, 37, p. e98049", "listPosition" : 76, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269461, "link" : "/api/reference/19269461", "label" : "77. Lin, Y., Fichou, Y., Han, S., Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions (2020) ACS Chem. Neurosci, 11, pp. 615-627", "listPosition" : 77, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269460, "link" : "/api/reference/19269460", "label" : "78. Fitzpatrick, A.W.P., Falcon, B., Scheres, S.H.W., Cryo-EM structures of tau filaments from Alzheimer's disease (2017) Nature, 547, pp. 185-190", "listPosition" : 78, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269459, "link" : "/api/reference/19269459", "label" : "79. Martin, E.W., Holehouse, A.S., Mittag, T., Valence and patterning of aromatic residues determine the phase behavior of prion-like domains (2020) Science, 367, pp. 694-699", "listPosition" : 79, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269458, "link" : "/api/reference/19269458", "label" : "80. Wang, J., Choi, J.-M., Hyman, A.A., A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins (2018) Cell, 174, pp. 688-699.e16", "listPosition" : 80, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269457, "link" : "/api/reference/19269457", "label" : "81. Mathieu, C., Pappu, R.V., Taylor, J.P., Beyond aggregation: pathological phase transitions in neurodegenerative disease (2020) Science, 370, pp. 56-60", "listPosition" : 81, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19269456, "link" : "/api/reference/19269456", "label" : "82. Soto, C., Pritzkow, S., Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases (2018) Nat. Neurosci, 21, pp. 1332-1340", "listPosition" : 82, "published" : false, "snippet" : true } ], "hasCitationDuplums" : false, "userChangeableUntil" : "2021-06-23T12:35:20.510+0000", "directInstitutesForSort" : "", "ownerAuthorCount" : 2, "ownerInstituteCount" : 17, "directInstituteCount" : 0, "authorCount" : 3, "contributorCount" : 0, "hasQualityFactor" : true, "link" : "/api/publication/31930727", "label" : "Berkeley R.F. et al. Real-time observation of structure and dynamics during the liquid-to-solid transition of FUS LC. 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