메뉴 건너뛰기




Volumn 11, Issue 11, 2015, Pages 899-904

Polymer physics of intracellular phase transitions

Author keywords

[No Author keywords available]

Indexed keywords

LIQUIDS; PROTEINS;

EID: 84946554664     PISSN: 17452473     EISSN: 17452481     Source Type: Journal    
DOI: 10.1038/nphys3532     Document Type: Article
Times cited : (1094)

References (67)
  • 1
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu, A. et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell 156, 1193-1206 (2014).
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1
  • 2
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • Li, J. et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150, 339-350 (2012).
    • (2012) Cell , vol.150 , pp. 339-350
    • Li, J.1
  • 3
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • An, S., Kumar, R., Sheets, E. D. & Benkovic, S. J. Reversible compartmentalization of de novo purine biosynthetic complexes in living cells. Science 320, 103-106 (2008).
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 4
    • 84903710066 scopus 로고    scopus 로고
    • Centrosomes are autocatalytic droplets of pericentriolar material organized by centrioles
    • Zwicker, D., Decker, M., Jaensch, S., Hyman, A. A. & Julicher, F. Centrosomes are autocatalytic droplets of pericentriolar material organized by centrioles. Proc. Natl Acad. Sci. USA 111, E2636-E2645 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E2636-E2645
    • Zwicker, D.1    Decker, M.2    Jaensch, S.3    Hyman, A.A.4    Julicher, F.5
  • 5
    • 31544482776 scopus 로고    scopus 로고
    • An architectural framework that may lie at the core of the postsynaptic density
    • Baron, M. K. et al. An architectural framework that may lie at the core of the postsynaptic density. Science 311, 531-535 (2006).
    • (2006) Science , vol.311 , pp. 531-535
    • Baron, M.K.1
  • 6
    • 84901856381 scopus 로고    scopus 로고
    • Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin
    • Ogrodnik, M. et al. Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin. Proc. Natl Acad. Sci. USA 111, 8049-8054 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 8049-8054
    • Ogrodnik, M.1
  • 7
    • 79960622503 scopus 로고    scopus 로고
    • Biogenesis and function of nuclear bodies
    • Mao, Y. S., Zhang, B. & Spector, D. L. Biogenesis and function of nuclear bodies. Trends Genet. 27, 295-306 (2011).
    • (2011) Trends Genet , vol.27 , pp. 295-306
    • Mao, Y.S.1    Zhang, B.2    Spector, D.L.3
  • 8
    • 84882801549 scopus 로고    scopus 로고
    • Altered ribostasis: RNA-protein granules in degenerative disorders
    • Ramaswami, M., Taylor, J. P. & Parker, R. Altered ribostasis: RNA-protein granules in degenerative disorders. Cell 154, 727-736 (2013).
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 9
    • 67649976463 scopus 로고    scopus 로고
    • Germline P granules are liquid droplets that localize by controlled dissolution/condensation
    • Brangwynne, C. P. et al. Germline P granules are liquid droplets that localize by controlled dissolution/condensation. Science 324, 1729-1732 (2009).
    • (2009) Science , vol.324 , pp. 1729-1732
    • Brangwynne, C.P.1
  • 10
    • 84883207900 scopus 로고    scopus 로고
    • Spatial organization of the cell cytoplasm by position-dependent phase separation
    • Lee, C. F., Brangwynne, C. P., Gharakhani, J., Hyman, A. A. & Julicher, F. Spatial organization of the cell cytoplasm by position-dependent phase separation. Phys. Rev. Lett. 111, 088101 (2013).
    • (2013) Phys. Rev. Lett , vol.111 , pp. 088101
    • Lee, C.F.1    Brangwynne, C.P.2    Gharakhani, J.3    Hyman, A.A.4    Julicher, F.5
  • 11
    • 84930960021 scopus 로고    scopus 로고
    • The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics
    • Elbaum-Garfinkle, S. et al. The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. Proc. Natl Acad. Sci. USA 112, 7189-7194 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 7189-7194
    • Elbaum-Garfinkle, S.1
  • 12
    • 84886617003 scopus 로고    scopus 로고
    • Translation repressors, an RNA helicase, and developmental cues control RNP phase transitions during early development
    • Hubstenberger, A., Noble, S. L., Cameron, C. & Evans, T. C. Translation repressors, an RNA helicase, and developmental cues control RNP phase transitions during early development. Dev. Cell 27, 161-173 (2013).
    • (2013) Dev. Cell , vol.27 , pp. 161-173
    • Hubstenberger, A.1    Noble, S.L.2    Cameron, C.3    Evans, T.C.4
  • 13
    • 79952723337 scopus 로고    scopus 로고
    • Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes
    • Brangwynne, C. P., Mitchison, T. J. & Hyman, A. A. Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes. Proc. Natl Acad. Sci. USA 108, 4334-4339 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 4334-4339
    • Brangwynne, C.P.1    Mitchison, T.J.2    Hyman, A.A.3
  • 14
    • 84885179258 scopus 로고    scopus 로고
    • A nuclear F-actin scaold stabilizes RNP droplets against gravity in large cells
    • Feric, M. & Brangwynne, C. P. A nuclear F-actin sca-old stabilizes RNP droplets against gravity in large cells. Nature Cell Biol. 15, 1253-1259 (2013).
    • (2013) Nature Cell Biol , vol.15 , pp. 1253-1259
    • Feric, M.1    Brangwynne, C.P.2
  • 15
    • 84924804206 scopus 로고    scopus 로고
    • Inverse size scaling of the nucleolus by a concentration-dependent phase transition
    • Weber, S. C. & Brangwynne, C. P. Inverse size scaling of the nucleolus by a concentration-dependent phase transition. Curr. Biol. 25, 641-646 (2015).
    • (2015) Curr. Biol , vol.25 , pp. 641-646
    • Weber, S.C.1    Brangwynne, C.P.2
  • 17
    • 84874040052 scopus 로고    scopus 로고
    • Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling
    • Wippich, F. et al. Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling. Cell 152, 791-805 (2013).
    • (2013) Cell , vol.152 , pp. 791-805
    • Wippich, F.1
  • 18
    • 34249068245 scopus 로고    scopus 로고
    • Dishevelled: A protein that functions in living cells by phase separating
    • Sear, R. P. Dishevelled: A protein that functions in living cells by phase separating. Soft Matter 3, 680-684 (2006).
    • (2006) Soft Matter , vol.3 , pp. 680-684
    • Sear, R.P.1
  • 19
    • 84862776582 scopus 로고    scopus 로고
    • Phase transitions in the assembly of multivalent signalling proteins
    • Li, P. et al. Phase transitions in the assembly of multivalent signalling proteins. Nature 483, 336-340 (2012).
    • (2012) Nature , vol.483 , pp. 336-340
    • Li, P.1
  • 20
    • 80054680620 scopus 로고    scopus 로고
    • An inducible nuclear body in the Drosophila germinal vesicle
    • Singer, A. B. & Gall, J. G. An inducible nuclear body in the Drosophila germinal vesicle. Nucleus 2, 403-409 (2011).
    • (2011) Nucleus , vol.2 , pp. 403-409
    • Singer, A.B.1    Gall, J.G.2
  • 21
    • 84939825873 scopus 로고    scopus 로고
    • Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)
    • Altmeyer, M. et al. Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose). Nature Commun. 6, 8088 (2015).
    • (2015) Nature Commun , vol.6 , pp. 8088
    • Altmeyer, M.1
  • 22
    • 84923878820 scopus 로고    scopus 로고
    • Phase transition of a disordered Nuage protein generates environmentally responsive membraneless organelles
    • Nott, T. et al. Phase transition of a disordered Nuage protein generates environmentally responsive membraneless organelles. Mol. Cell 57, 936-947 (2015).
    • (2015) Mol. Cell , vol.57 , pp. 936-947
    • Nott, T.1
  • 23
    • 84903735072 scopus 로고    scopus 로고
    • Vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery
    • Fromm, S. A. et al. In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery. Angew. Chem. 53, 7354-7359 (2014).
    • (2014) Angew. Chem , vol.53 , pp. 7354-7359
    • Fromm, S.A.1
  • 24
    • 84943801809 scopus 로고    scopus 로고
    • Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles
    • Hennig, S. et al. Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles. J. Cell Biol. 210, 529-539 (2015).
    • (2015) J. Cell Biol , vol.210 , pp. 529-539
    • Hennig, S.1
  • 25
    • 84939860220 scopus 로고    scopus 로고
    • Phase transitions of multivalent proteins can promote clustering of membrane receptors
    • Banjade, S. & Rosen, M. K. Phase transitions of multivalent proteins can promote clustering of membrane receptors. eLife 3, e04123 (2014).
    • (2014) Life , vol.3 , pp. e04123
    • Banjade, S.1    Rosen, M.K.2
  • 26
    • 84902446851 scopus 로고    scopus 로고
    • Classification of intrinsically disordered regions and proteins
    • van der Lee, R. et al. Classification of intrinsically disordered regions and proteins. Chem. Rev. 114, 6589-6631 (2014).
    • (2014) Chem. Rev , vol.114 , pp. 6589-6631
    • Van Der Lee, R.1
  • 27
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • Wright, P. E. & Dyson, H. J. Intrinsically disordered proteins in cellular signalling and regulation. Nature Rev. Mol. Cell Biol. 16, 18-29 (2015).
    • (2015) Nature Rev. Mol. Cell Biol , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 28
    • 84918825645 scopus 로고    scopus 로고
    • Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
    • Uversky, V. N., Kuznetsova, I. M., Turoverov, K. K. & Zaslavsky, B. Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates. FEBS Lett. 589, 15-22 (2015).
    • (2015) FEBS Lett , vol.589 , pp. 15-22
    • Uversky, V.N.1    Kuznetsova, I.M.2    Turoverov, K.K.3    Zaslavsky, B.4
  • 29
    • 84926529027 scopus 로고    scopus 로고
    • Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. Elegans
    • Wang, J. T. et al. Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. elegans. eLife 3, e04591 (2014).
    • (2014) Life , vol.3 , pp. e04591
    • Wang, J.T.1
  • 30
    • 84924303298 scopus 로고    scopus 로고
    • Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation
    • Holehouse, A. S., Garai, K., Lyle, N., Vitalis, A. & Pappu, R. V. Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation. J. Am. Chem. Soc. 137, 2984-2995 (2015).
    • (2015) J. Am. Chem. Soc , vol.137 , pp. 2984-2995
    • Holehouse, A.S.1    Garai, K.2    Lyle, N.3    Vitalis, A.4    Pappu, R.V.5
  • 31
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • Crick, S. L., Jayaraman, M., Frieden, C.,Wetzel, R. & Pappu, R. V. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc. Natl Acad. Sci. USA 103, 16764-16769 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 32
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • Mukhopadhyay, S., Krishnan, R., Lemke, E. A., Lindquist, S. & Deniz, A. A. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc. Natl Acad. Sci. USA 104, 2649-2654 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 33
    • 44949262123 scopus 로고    scopus 로고
    • Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins
    • Tran, H. T., Mao, A. & Pappu, R. V. Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins. J. Am. Chem. Soc. 130, 7380-7392 (2008).
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 7380-7392
    • Tran, H.T.1    Mao, A.2    Pappu, R.V.3
  • 34
    • 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
    • Crick, S. L., Ru, K. M., Garai, K., Frieden, C. & Pappu, R. V. 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, 20075-20080 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 20075-20080
    • Crick, S.L.1    Ru, K.M.2    Garai, K.3    Frieden, C.4    Pappu, R.V.5
  • 35
    • 84866869780 scopus 로고    scopus 로고
    • Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity
    • Lai, J. et al. Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity. Proc. Natl Acad. Sci. USA 109, 15781-15786 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 15781-15786
    • Lai, J.1
  • 37
    • 84882364963 scopus 로고    scopus 로고
    • Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues
    • Das, R. K. & Pappu, R. V. Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc. Natl Acad. Sci. USA 110, 13392-13397 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 13392-13397
    • Das, R.K.1    Pappu, R.V.2
  • 38
    • 85047593740 scopus 로고    scopus 로고
    • Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity
    • Schmidt, H. B. & Gorlich, D. Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity. eLife 4, e04251 (2015).
    • (2015) Life , vol.4 , pp. e04251
    • Schmidt, H.B.1    Gorlich, D.2
  • 39
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti, S., Halfmann, R., King, O., Kapila, A. & Lindquist, S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137, 146-158 (2009).
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 40
    • 84875605133 scopus 로고    scopus 로고
    • Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
    • Kim, H. J. et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495, 467-473 (2013).
    • (2013) Nature , vol.495 , pp. 467-473
    • Kim, H.J.1
  • 41
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato, M. et al. Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels. Cell 149, 753-767 (2012).
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1
  • 42
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y. R., King, O. D., Shorter, J. & Gitler, A. D. Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201, 361-372 (2013).
    • (2013) J. Cell Biol , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 43
    • 84861964894 scopus 로고    scopus 로고
    • Getting RNA and protein in phase
    • Weber, S. C. & Brangwynne, C. P. Getting RNA and protein in phase. Cell 149, 1188-1191 (2012).
    • (2012) Cell , vol.149 , pp. 1188-1191
    • Weber, S.C.1    Brangwynne, C.P.2
  • 44
    • 84940403835 scopus 로고    scopus 로고
    • A liquid-to-solid phase transition of the ALS ProteinFUS accelerated by disease mutation
    • Patel, A. et al. A liquid-to-solid phase transition of the ALS ProteinFUS accelerated by disease mutation. Cell 162, 1066-1077 (2015).
    • (2015) Cell , vol.162 , pp. 1066-1077
    • Patel, A.1
  • 45
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low-complexity domains promotes stress granule assembly and drives pathological fibrillization
    • Molliex, A. et al. Phase separation by low-complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 163, 123-133 (2015).
    • (2015) Cell , vol.163 , pp. 123-133
    • Molliex, A.1
  • 46
    • 84944884978 scopus 로고    scopus 로고
    • Formation and maturation of phase separated liquid droplets by RNA binding proteins
    • Lin, Y., Protter, D. S.W., Rosen, M. K. & Parker, R. Formation and maturation of phase separated liquid droplets by RNA binding proteins. Mol. Cell 60, 1-12 (2015).
    • (2015) Mol. Cell , vol.60 , pp. 1-12
    • Lin, Y.1    Protter, D.S.W.2    Rosen, M.K.3    Parker, R.4
  • 47
    • 84944884155 scopus 로고    scopus 로고
    • RNA controls PolyQ protein phase transitions
    • Zhang, H. et al. RNA controls PolyQ protein phase transitions. Mol. Cell 60, 220-230 (2015).
    • (2015) Mol. Cell , vol.60 , pp. 220-230
    • Zhang, H.1
  • 49
    • 0030040281 scopus 로고    scopus 로고
    • Phase separation in aqueous solutions of lens gamma-crystallins: Special role of gammas
    • Liu, C. et al. Phase separation in aqueous solutions of lens gamma-crystallins: Special role of gamma s. Proc. Natl Acad. Sci. USA 93, 377-382 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 377-382
    • Liu, C.1
  • 50
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • tenWolde, P. R. & Frenkel, D. Enhancement of protein crystal nucleation by critical density fluctuations. Science 277, 1975-1978 (1997).
    • (1997) Science , vol.277 , pp. 1975-1978
    • TenWolde, P.R.1    Frenkel, D.2
  • 51
    • 84940503517 scopus 로고    scopus 로고
    • Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
    • Kroschwald, S. et al. Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules. eLife 4, e06807 (2015).
    • (2015) Life , vol.4 , pp. e06807
    • Kroschwald, S.1
  • 52
    • 84879349589 scopus 로고    scopus 로고
    • Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function
    • Buchan, J. R., Kolaitis, R. M., Taylor, J. P. & Parker, R. Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell 153, 1461-1474 (2013).
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.M.2    Taylor, J.P.3    Parker, R.4
  • 53
    • 84924037150 scopus 로고    scopus 로고
    • The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation
    • Sweeny, E. A. et al. The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation. Mol. Cell 57, 836-849 (2015).
    • (2015) Mol. Cell , vol.57 , pp. 836-849
    • Sweeny, E.A.1
  • 54
    • 84892828598 scopus 로고    scopus 로고
    • The bacterial cytoplasm has glass-like properties and is fluidized by metabolic activity
    • Parry, B. R. et al. The bacterial cytoplasm has glass-like properties and is fluidized by metabolic activity. Cell 156, 183-194 (2014).
    • (2014) Cell , vol.156 , pp. 183-194
    • Parry, B.R.1
  • 55
    • 84860807645 scopus 로고    scopus 로고
    • Nonthermal ATP-dependent fluctuations contribute to the in vivo motion of chromosomal loci
    • Weber, S. C., Spakowitz, A. J. & Theriot, J. A. Nonthermal ATP-dependent fluctuations contribute to the in vivo motion of chromosomal loci. Proc. Natl Acad. Sci. USA 109, 7338-7343 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 7338-7343
    • Weber, S.C.1    Spakowitz, A.J.2    Theriot, J.A.3
  • 56
    • 84907369302 scopus 로고    scopus 로고
    • Probing the stochastic, motor-driven properties of the cytoplasm using force spectrum microscopy
    • Guo, M. et al. Probing the stochastic, motor-driven properties of the cytoplasm using force spectrum microscopy. Cell 158, 822-832 (2014).
    • (2014) Cell , vol.158 , pp. 822-832
    • Guo, M.1
  • 57
    • 21744453240 scopus 로고    scopus 로고
    • Cytoskeletal remodelling and slow dynamics in the living cell
    • Bursac, P. et al. Cytoskeletal remodelling and slow dynamics in the living cell. Nature Mater. 4, 557-561 (2005).
    • (2005) Nature Mater , vol.4 , pp. 557-561
    • Bursac, P.1
  • 60
    • 84555218378 scopus 로고    scopus 로고
    • Preparation and relaxation of very stable glassy states of a simulated liquid
    • Jack, R. L., Hedges, L. O., Garrahan, J. P. & Chandler, D. Preparation and relaxation of very stable glassy states of a simulated liquid. Phys. Rev. Lett. 107, 275702 (2011).
    • (2011) Phys. Rev. Lett , vol.107 , pp. 275702
    • Jack, R.L.1    Hedges, L.O.2    Garrahan, J.P.3    Chandler, D.4
  • 61
    • 84907344348 scopus 로고    scopus 로고
    • Dynamical phase transitions reveal amyloid-like states on protein folding landscapes
    • Weber, J. K., Jack, R. L., Schwantes, C. R. & Pande, V. S. Dynamical phase transitions reveal amyloid-like states on protein folding landscapes. Biophys. J. 107, 974-982 (2014).
    • (2014) Biophys. J , vol.107 , pp. 974-982
    • Weber, J.K.1    Jack, R.L.2    Schwantes, C.R.3    Pande, V.S.4
  • 62
    • 80052951973 scopus 로고    scopus 로고
    • Regulation of the MEX-5 gradient by a spatially segregated kinase/phosphatase cycle
    • Grin, E. E., Odde, D. J. & Seydoux, G. Regulation of the MEX-5 gradient by a spatially segregated kinase/phosphatase cycle. Cell 146, 955-968 (2011).
    • (2011) Cell , vol.146 , pp. 955-968
    • Grin, E.E.1    Odde, D.J.2    Seydoux, G.3
  • 63
    • 77951622022 scopus 로고    scopus 로고
    • Role of GW182 proteins and PABPC1 in the miRNA pathway: A sense of déjà vu
    • Tritschler, F., Huntzinger, E. & Izaurralde, E. Role of GW182 proteins and PABPC1 in the miRNA pathway: A sense of déjà vu. Nature Rev. Mol. Cell Biol. 11, 379-384 (2010).
    • (2010) Nature Rev. Mol. Cell Biol , vol.11 , pp. 379-384
    • Tritschler, F.1    Huntzinger, E.2    Izaurralde, E.3
  • 64
    • 33947562256 scopus 로고
    • Some properties of solutions of long-chain compounds
    • Huggins, M. L. Some properties of solutions of long-chain compounds. J. Phys. Chem. 46, 151-158 (1942).
    • (1942) J. Phys. Chem , vol.46 , pp. 151-158
    • Huggins, M.L.1
  • 65
    • 0008883222 scopus 로고
    • Thermodynamics of high polymer solutions
    • Flory, P. J. Thermodynamics of high polymer solutions. J. Chem. Phys. 10, 51-61 (1942).
    • (1942) J. Chem. Phys , vol.10 , pp. 51-61
    • Flory, P.J.1
  • 66
    • 84961288478 scopus 로고    scopus 로고
    • Relating sequence encoded information to form and function of intrinsically disordered proteins
    • Das, R. K., Ru, K. M. & Pappu, R. V. Relating sequence encoded information to form and function of intrinsically disordered proteins. Curr. Opin. Struct. Biol. 32, 102-112 (2015).
    • (2015) Curr. Opin. Struct. Biol , vol.32 , pp. 102-112
    • Das, R.K.1    Ru, K.M.2    Pappu, R.V.3
  • 67
    • 70449160290 scopus 로고
    • Phase separation in polyelectrolyte solutions. Theory of complex coacervation
    • Overbeek, J. T. G. & Voorn, M. J. Phase separation in polyelectrolyte solutions. Theory of complex coacervation. J. Cell. Comp. Physiol. 49, 7-26 (1957).
    • (1957) J. Cell. Comp. Physiol , vol.49 , pp. 7-26
    • Overbeek, J.T.G.1    Voorn, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.