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Volumn 165, Issue 5, 2016, Pages 1055-1066

The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; COP9 SIGNALOSOME; NUCLEOPORIN; PRION PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; RIBONUCLEOPROTEIN; RNA POLYMERASE II; T LYMPHOCYTE RECEPTOR; MULTIPROTEIN COMPLEX; PRION;

EID: 84975159042     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2016.05.004     Document Type: Review
Times cited : (294)

References (97)
  • 2
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • S. Alberti, R. Halfmann, O. King, A. Kapila, and S. Lindquist A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Cell 137 2009 146 158
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 5
    • 84946036190 scopus 로고    scopus 로고
    • The linker for activation of T cells (LAT) signaling hub: From signaling complexes to microclusters
    • L. Balagopalan, R.L. Kortum, N.P. Coussens, V.A. Barr, and L.E. Samelson The linker for activation of T cells (LAT) signaling hub: from signaling complexes to microclusters J. Biol. Chem. 290 2015 26422 26429
    • (2015) J. Biol. Chem. , vol.290 , pp. 26422-26429
    • Balagopalan, L.1    Kortum, R.L.2    Coussens, N.P.3    Barr, V.A.4    Samelson, L.E.5
  • 6
    • 84947985485 scopus 로고    scopus 로고
    • Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck
    • S. Banjade, Q. Wu, A. Mittal, W.B. Peeples, R.V. Pappu, and M.K. Rosen Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck Proc. Natl. Acad. Sci. USA 112 2015 E6426 E6435
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. E6426-E6435
    • Banjade, S.1    Wu, Q.2    Mittal, A.3    Peeples, W.B.4    Pappu, R.V.5    Rosen, M.K.6
  • 8
    • 84975138897 scopus 로고    scopus 로고
    • Mechanisms and consequences of macromolecular phase separation
    • this issue
    • L.-P. Bergeron-Sandoval, N. Safaee, and S.W. Michnick Mechanisms and consequences of macromolecular phase separation Cell 165 2016 1067 1079 this issue
    • (2016) Cell , vol.165 , pp. 1067-1079
    • Bergeron-Sandoval, L.-P.1    Safaee, N.2    Michnick, S.W.3
  • 9
    • 84918528755 scopus 로고    scopus 로고
    • Signalosome assembly by domains undergoing dynamic head-to-tail polymerization
    • M. Bienz Signalosome assembly by domains undergoing dynamic head-to-tail polymerization Trends Biochem. Sci. 39 2014 487 495
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 487-495
    • Bienz, M.1
  • 11
    • 84946554664 scopus 로고    scopus 로고
    • Polymer physics of intracellular phase transitions
    • C.P. Brangwynne, P. Tompa, and R.V. Pappu Polymer physics of intracellular phase transitions Nat. Phys. 11 2015 899 904
    • (2015) Nat. Phys. , vol.11 , pp. 899-904
    • Brangwynne, C.P.1    Tompa, P.2    Pappu, R.V.3
  • 12
    • 84944894243 scopus 로고    scopus 로고
    • Residue-by-Residue View of in Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II
    • K.A. Burke, A.M. Janke, C.L. Rhine, and N.L. Fawzi Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II Mol. Cell 60 2015 231 241
    • (2015) Mol. Cell , vol.60 , pp. 231-241
    • Burke, K.A.1    Janke, A.M.2    Rhine, C.L.3    Fawzi, N.L.4
  • 13
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • X. Cai, J. Chen, H. Xu, S. Liu, Q.X. Jiang, R. Halfmann, and Z.J. Chen Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation Cell 156 2014 1207 1222
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1    Chen, J.2    Xu, H.3    Liu, S.4    Jiang, Q.X.5    Halfmann, R.6    Chen, Z.J.7
  • 14
    • 84919770982 scopus 로고    scopus 로고
    • Theoretical perspectives on nonnative interactions and intrinsic disorder in protein folding and binding
    • T. Chen, J. Song, and H.S. Chan Theoretical perspectives on nonnative interactions and intrinsic disorder in protein folding and binding Curr. Opin. Struct. Biol. 30 2015 32 42
    • (2015) Curr. Opin. Struct. Biol. , vol.30 , pp. 32-42
    • Chen, T.1    Song, J.2    Chan, H.S.3
  • 17
    • 84890288534 scopus 로고    scopus 로고
    • Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation
    • S.L. Crick, K.M. Ruff, K. Garai, C. Frieden, and R.V. Pappu Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation Proc. Natl. Acad. Sci. USA 110 2013 20075 20080
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 20075-20080
    • Crick, S.L.1    Ruff, K.M.2    Garai, K.3    Frieden, C.4    Pappu, R.V.5
  • 18
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • B.C. Cunningham, and J.A. Wells Comparison of a structural and a functional epitope J. Mol. Biol. 234 1993 554 563
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 19
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • D. Eisenberg, and M. Jucker The amyloid state of proteins in human diseases Cell 148 2012 1188 1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 21
    • 84907975948 scopus 로고    scopus 로고
    • IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly
    • R. Ferrao, H. Zhou, Y. Shan, Q. Liu, Q. Li, D.E. Shaw, X. Li, and H. Wu IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly Mol. Cell 55 2014 891 903
    • (2014) Mol. Cell , vol.55 , pp. 891-903
    • Ferrao, R.1    Zhou, H.2    Shan, Y.3    Liu, Q.4    Li, Q.5    Shaw, D.E.6    Li, X.7    Wu, H.8
  • 22
    • 79952148045 scopus 로고    scopus 로고
    • Dishevelled interacts with the DIX domain polymerization interface of Axin to interfere with its function in down-regulating β-catenin
    • M. Fiedler, C. Mendoza-Topaz, T.J. Rutherford, J. Mieszczanek, and M. Bienz Dishevelled interacts with the DIX domain polymerization interface of Axin to interfere with its function in down-regulating β-catenin Proc. Natl. Acad. Sci. USA 108 2011 1937 1942
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1937-1942
    • Fiedler, M.1    Mendoza-Topaz, C.2    Rutherford, T.J.3    Mieszczanek, J.4    Bienz, M.5
  • 23
    • 0000724163 scopus 로고
    • Molecular size distribution in three dimensional polymers I. Gelation
    • P.J. Flory Molecular size distribution in three dimensional polymers I. Gelation J. Am. Chem. Soc. 63 1941 3083
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 3083
    • Flory, P.J.1
  • 27
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • S. Frey, R.P. Richter, and D. Görlich FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties Science 314 2006 815 817
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Görlich, D.3
  • 28
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: Linking regulation to protein dynamics
    • M. Fuxreiter Fuzziness: linking regulation to protein dynamics Mol. Biosyst. 8 2012 168 177
    • (2012) Mol. Biosyst. , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 29
    • 0034624393 scopus 로고    scopus 로고
    • A computational study of cation-p interaction vs salt bridges in aqueous media: Implications for protein engineering
    • J.P. Gallivan, and D.A. Dougherty A computational study of cation-p interaction vs salt bridges in aqueous media: implications for protein engineering J. Am. Chem. Soc. 122 2000 870 874
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 870-874
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 33
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • F. Hou, L. Sun, H. Zheng, B. Skaug, Q.X. Jiang, and Z.J. Chen MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response Cell 146 2011 448 461
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5    Chen, Z.J.6
  • 35
    • 0036643433 scopus 로고    scopus 로고
    • Simple sequences are rare in the Protein Data Bank
    • M.A. Huntley, and G.B. Golding Simple sequences are rare in the Protein Data Bank Proteins 48 2002 134 140
    • (2002) Proteins , vol.48 , pp. 134-140
    • Huntley, M.A.1    Golding, G.B.2
  • 38
    • 84873532024 scopus 로고    scopus 로고
    • The discovery and analysis of P Bodies
    • S. Jain, and R. Parker The discovery and analysis of P Bodies Adv. Exp. Med. Biol. 768 2013 23 43
    • (2013) Adv. Exp. Med. Biol. , vol.768 , pp. 23-43
    • Jain, S.1    Parker, R.2
  • 39
    • 84859986329 scopus 로고    scopus 로고
    • Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor
    • T. Jin, A. Perry, J. Jiang, P. Smith, J.A. Curry, L. Unterholzner, Z. Jiang, G. Horvath, V.A. Rathinam, R.W. Johnstone, and et al. Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor Immunity 36 2012 561 571
    • (2012) Immunity , vol.36 , pp. 561-571
    • Jin, T.1    Perry, A.2    Jiang, J.3    Smith, P.4    Curry, J.A.5    Unterholzner, L.6    Jiang, Z.7    Horvath, G.8    Rathinam, V.A.9    Johnstone, R.W.10
  • 40
    • 84877692253 scopus 로고    scopus 로고
    • Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly
    • T. Jin, A. Perry, P. Smith, J. Jiang, and T.S. Xiao Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly J. Biol. Chem. 288 2013 13225 13235
    • (2013) J. Biol. Chem. , vol.288 , pp. 13225-13235
    • Jin, T.1    Perry, A.2    Smith, P.3    Jiang, J.4    Xiao, T.S.5
  • 41
    • 84922479840 scopus 로고    scopus 로고
    • SMOCs: Supramolecular organizing centres that control innate immunity
    • J.C. Kagan, V.G. Magupalli, and H. Wu SMOCs: supramolecular organizing centres that control innate immunity Nat. Rev. Immunol. 14 2014 821 826
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 821-826
    • Kagan, J.C.1    Magupalli, V.G.2    Wu, H.3
  • 42
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • M. Kato, T.W. Han, S. Xie, K. Shi, X. Du, L.C. Wu, H. Mirzaei, E.J. Goldsmith, J. Longgood, J. Pei, and et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels Cell 149 2012 753 767
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5    Wu, L.C.6    Mirzaei, H.7    Goldsmith, E.J.8    Longgood, J.9    Pei, J.10
  • 43
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • R. Krishnan, and S.L. Lindquist Structural insights into a yeast prion illuminate nucleation and strain diversity Nature 435 2005 765 772
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 47
    • 0037117543 scopus 로고    scopus 로고
    • IRAK-4: A novel member of the IRAK family with the properties of an IRAK-kinase
    • S. Li, A. Strelow, E.J. Fontana, and H. Wesche IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase Proc. Natl. Acad. Sci. USA 99 2002 5567 5572
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5567-5572
    • Li, S.1    Strelow, A.2    Fontana, E.J.3    Wesche, H.4
  • 50
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • S.C. Lin, Y.C. Lo, and H. Wu Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling Nature 465 2010 885 890
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 51
    • 84944884978 scopus 로고    scopus 로고
    • Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
    • Y. Lin, D.S. Protter, M.K. Rosen, and R. Parker Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins Mol. Cell 60 2015 208 219
    • (2015) Mol. Cell , vol.60 , pp. 208-219
    • Lin, Y.1    Protter, D.S.2    Rosen, M.K.3    Parker, R.4
  • 52
    • 84895923768 scopus 로고    scopus 로고
    • Crystal structure of the F27G AIM2 PYD mutant and similarities of its self-association to DED/DED interactions
    • A. Lu, V. Kabaleeswaran, T. Fu, V.G. Magupalli, and H. Wu Crystal structure of the F27G AIM2 PYD mutant and similarities of its self-association to DED/DED interactions J. Mol. Biol. 426 2014 1420 1427
    • (2014) J. Mol. Biol. , vol.426 , pp. 1420-1427
    • Lu, A.1    Kabaleeswaran, V.2    Fu, T.3    Magupalli, V.G.4    Wu, H.5
  • 54
    • 84951838786 scopus 로고    scopus 로고
    • Plasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2
    • A. Lu, Y. Li, Q. Yin, J. Ruan, X. Yu, E. Egelman, and H. Wu Plasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2 Cell Discov 1 2015 15013
    • (2015) Cell Discov , vol.1 , pp. 15013
    • Lu, A.1    Li, Y.2    Yin, Q.3    Ruan, J.4    Yu, X.5    Egelman, E.6    Wu, H.7
  • 55
    • 84876288161 scopus 로고    scopus 로고
    • Protein disorder, prion propensities, and self-organizing macromolecular collectives
    • L. Malinovska, S. Kroschwald, and S. Alberti Protein disorder, prion propensities, and self-organizing macromolecular collectives Biochim. Biophys. Acta 1834 2013 918 931
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 918-931
    • Malinovska, L.1    Kroschwald, S.2    Alberti, S.3
  • 56
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • G. Matsumoto, K. Wada, M. Okuno, M. Kurosawa, and N. Nukina Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins Mol. Cell 44 2011 279 289
    • (2011) Mol. Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3    Kurosawa, M.4    Nukina, N.5
  • 58
    • 84901033525 scopus 로고    scopus 로고
    • Principles and properties of eukaryotic mRNPs
    • S.F. Mitchell, and R. Parker Principles and properties of eukaryotic mRNPs Mol. Cell 54 2014 547 558
    • (2014) Mol. Cell , vol.54 , pp. 547-558
    • Mitchell, S.F.1    Parker, R.2
  • 59
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
    • A. Molliex, J. Temirov, J. Lee, M. Coughlin, A.P. Kanagaraj, H.J. Kim, T. Mittag, and J.P. Taylor Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization Cell 163 2015 123 133
    • (2015) Cell , vol.163 , pp. 123-133
    • Molliex, A.1    Temirov, J.2    Lee, J.3    Coughlin, M.4    Kanagaraj, A.P.5    Kim, H.J.6    Mittag, T.7    Taylor, J.P.8
  • 60
    • 84960129723 scopus 로고    scopus 로고
    • ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function
    • T. Murakami, S. Qamar, J.Q. Lin, G.S. Schierle, E. Rees, A. Miyashita, A.R. Costa, R.B. Dodd, F.T. Chan, C.H. Michel, and et al. ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function Neuron 88 2015 678 690
    • (2015) Neuron , vol.88 , pp. 678-690
    • Murakami, T.1    Qamar, S.2    Lin, J.Q.3    Schierle, G.S.4    Rees, E.5    Miyashita, A.6    Costa, A.R.7    Dodd, R.B.8    Chan, F.T.9    Michel, C.H.10
  • 62
    • 84902160274 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and intrinsically disordered protein regions
    • C.J. Oldfield, and A.K. Dunker Intrinsically disordered proteins and intrinsically disordered protein regions Annu. Rev. Biochem. 83 2014 553 584
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 553-584
    • Oldfield, C.J.1    Dunker, A.K.2
  • 64
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • S.B. Prusiner Molecular biology of prion diseases Science 252 1991 1515 1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 70
    • 85047593740 scopus 로고    scopus 로고
    • Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity
    • H.B. Schmidt, and D. Görlich Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity eLife 4 2015 e04251
    • (2015) ELife , vol.4 , pp. e04251
    • Schmidt, H.B.1    Görlich, D.2
  • 71
    • 84888429488 scopus 로고    scopus 로고
    • RNA seeds higher-order assembly of FUS protein
    • J.C. Schwartz, X. Wang, E.R. Podell, and T.R. Cech RNA seeds higher-order assembly of FUS protein Cell Rep. 5 2013 918 925
    • (2013) Cell Rep. , vol.5 , pp. 918-925
    • Schwartz, J.C.1    Wang, X.2    Podell, E.R.3    Cech, T.R.4
  • 72
    • 29244462476 scopus 로고    scopus 로고
    • The Wnt signalling effector Dishevelled forms dynamic protein assemblies rather than stable associations with cytoplasmic vesicles
    • T. Schwarz-Romond, C. Merrifield, B.J. Nichols, and M. Bienz The Wnt signalling effector Dishevelled forms dynamic protein assemblies rather than stable associations with cytoplasmic vesicles J. Cell Sci. 118 2005 5269 5277
    • (2005) J. Cell Sci. , vol.118 , pp. 5269-5277
    • Schwarz-Romond, T.1    Merrifield, C.2    Nichols, B.J.3    Bienz, M.4
  • 74
    • 0038298868 scopus 로고    scopus 로고
    • Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
    • P. Selenko, G. Gregorovic, R. Sprangers, G. Stier, Z. Rhani, A. Krämer, and M. Sattler Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP Mol. Cell 11 2003 965 976
    • (2003) Mol. Cell , vol.11 , pp. 965-976
    • Selenko, P.1    Gregorovic, G.2    Sprangers, R.3    Stier, G.4    Rhani, Z.5    Krämer, A.6    Sattler, M.7
  • 75
    • 0032001610 scopus 로고    scopus 로고
    • Thermoreversible gelation in solutions of associative polymers. 1. Statics
    • A.N. Semenov, and M. Rubinstein Thermoreversible gelation in solutions of associative polymers. 1. Statics Macromolecules 31 1998 1373 1385
    • (1998) Macromolecules , vol.31 , pp. 1373-1385
    • Semenov, A.N.1    Rubinstein, M.2
  • 76
    • 84942293974 scopus 로고    scopus 로고
    • Fuzzy complexes: Specific binding without complete folding
    • R. Sharma, Z. Raduly, M. Miskei, and M. Fuxreiter Fuzzy complexes: Specific binding without complete folding FEBS Lett. 589 19 Pt A 2015 2533 2542
    • (2015) FEBS Lett. , vol.589 , Issue.19 , pp. 2533-2542
    • Sharma, R.1    Raduly, Z.2    Miskei, M.3    Fuxreiter, M.4
  • 77
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Z. Sun, Z. Diaz, X. Fang, M.P. Hart, A. Chesi, J. Shorter, and A.D. Gitler Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS PLoS Biol. 9 2011 e1000614
    • (2011) PLoS Biol. , vol.9 , pp. e1000614
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 78
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • M. Tanaka, P. Chien, N. Naber, R. Cooke, and J.S. Weissman Conformational variations in an infectious protein determine prion strain differences Nature 428 2004 323 328
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 79
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • P.R. ten Wolde, and D. Frenkel Enhancement of protein crystal nucleation by critical density fluctuations Science 277 1997 1975 1978
    • (1997) Science , vol.277 , pp. 1975-1978
    • Ten Wolde, P.R.1    Frenkel, D.2
  • 80
    • 0033524982 scopus 로고    scopus 로고
    • Oligomeric structure of the human EphB2 receptor SAM domain
    • C.D. Thanos, K.E. Goodwill, and J.U. Bowie Oligomeric structure of the human EphB2 receptor SAM domain Science 283 1999 833 836
    • (1999) Science , vol.283 , pp. 833-836
    • Thanos, C.D.1    Goodwill, K.E.2    Bowie, J.U.3
  • 81
    • 70349249705 scopus 로고    scopus 로고
    • Structural disorder in amyloid fibrils: Its implication in dynamic interactions of proteins
    • P. Tompa Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins FEBS J. 276 2009 5406 5415
    • (2009) FEBS J. , vol.276 , pp. 5406-5415
    • Tompa, P.1
  • 82
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • P. Tompa, and M. Fuxreiter Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions Trends Biochem. Sci. 33 2008 2 8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 83
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • M.L. Tradewell, Z. Yu, M. Tibshirani, M.C. Boulanger, H.D. Durham, and S. Richard Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations Hum. Mol. Genet. 21 2012 136 149
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 84
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • C. Wasmer, A. Lange, H. Van Melckebeke, A.B. Siemer, R. Riek, and B.H. Meier Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core Science 319 2008 1523 1526
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 87
    • 0041625934 scopus 로고    scopus 로고
    • PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62
    • M.I. Wilson, D.J. Gill, O. Perisic, M.T. Quinn, and R.L. Williams PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62 Mol. Cell 12 2003 39 50
    • (2003) Mol. Cell , vol.12 , pp. 39-50
    • Wilson, M.I.1    Gill, D.J.2    Perisic, O.3    Quinn, M.T.4    Williams, R.L.5
  • 88
    • 84874040052 scopus 로고    scopus 로고
    • Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling
    • F. Wippich, B. Bodenmiller, M.G. Trajkovska, S. Wanka, R. Aebersold, and L. Pelkmans Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling Cell 152 2013 791 805
    • (2013) Cell , vol.152 , pp. 791-805
    • Wippich, F.1    Bodenmiller, B.2    Trajkovska, M.G.3    Wanka, S.4    Aebersold, R.5    Pelkmans, L.6
  • 89
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • P.E. Wright, and H.J. Dyson Intrinsically disordered proteins in cellular signalling and regulation Nat. Rev. Mol. Cell Biol. 16 2015 18 29
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 90
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • H. Wu Higher-order assemblies in a new paradigm of signal transduction Cell 153 2013 287 292
    • (2013) Cell , vol.153 , pp. 287-292
    • Wu, H.1
  • 91
    • 77957578665 scopus 로고    scopus 로고
    • Involvement of the AIM2, NLRC4, and NLRP3 inflammasomes in caspase-1 activation by Listeria monocytogenes
    • J. Wu, T. Fernandes-Alnemri, and E.S. Alnemri Involvement of the AIM2, NLRC4, and NLRP3 inflammasomes in caspase-1 activation by Listeria monocytogenes J. Clin. Immunol. 30 2010 693 702
    • (2010) J. Clin. Immunol. , vol.30 , pp. 693-702
    • Wu, J.1    Fernandes-Alnemri, T.2    Alnemri, E.S.3
  • 93
    • 84946221201 scopus 로고    scopus 로고
    • The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei
    • S. Xiang, M. Kato, L.C. Wu, Y. Lin, M. Ding, Y. Zhang, Y. Yu, and S.L. McKnight The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei Cell 163 2015 829 839
    • (2015) Cell , vol.163 , pp. 829-839
    • Xiang, S.1    Kato, M.2    Wu, L.C.3    Lin, Y.4    Ding, M.5    Zhang, Y.6    Yu, Y.7    McKnight, S.L.8
  • 95
    • 84927544825 scopus 로고    scopus 로고
    • Structural Biology of Innate Immunity Annu. Rev
    • Q. Yin, T.M. Fu, J. Li, and H. Wu Structural Biology of Innate Immunity Annu. Rev Immunology 33 2015 393 416
    • (2015) Immunology , vol.33 , pp. 393-416
    • Yin, Q.1    Fu, T.M.2    Li, J.3    Wu, H.4
  • 96
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • H. Yu, J.K. Chen, S. Feng, D.C. Dalgarno, A.W. Brauer, and S.L. Schreiber Structural basis for the binding of proline-rich peptides to SH3 domains Cell 76 1994 933 945
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3    Dalgarno, D.C.4    Brauer, A.W.5    Schreiber, S.L.6


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