메뉴 건너뛰기




Volumn 206, Issue 5, 2014, Pages 579-588

Assemblages: Functional units formed by cellular phase separation

Author keywords

[No Author keywords available]

Indexed keywords

CELL FUNCTION; CELL SUBPOPULATION; PHASE SEPARATION; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; REVIEW;

EID: 84906877425     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201404124     Document Type: Review
Times cited : (206)

References (128)
  • 1
    • 84875141193 scopus 로고    scopus 로고
    • Uncovering nuclear pore complexity with innovation
    • Adams, R.L., and S.R. Wente. 2013. Uncovering nuclear pore complexity with innovation. Cell. 152:1218-1221. http://dx.doi.org/10.1016/j.cell.2013 .02.042
    • (2013) Cell , vol.152 , pp. 1218-1221
    • Adams, R.L.1    Wente, S.R.2
  • 4
    • 0345574994 scopus 로고
    • The ultrastructure of the vitelline body in the oocyte of the spider Tegenaria parietina
    • André, J., and C. Rouiller. 1957. The ultrastructure of the vitelline body in the oocyte of the spider Tegenaria parietina. J. Biophys. Biochem. Cytol. 3:977-984. http://dx.doi.org/10.1083/jcb.3.6.977
    • (1957) J. Biophys. Biochem. Cytol. , vol.3 , pp. 977-984
    • André, J.1    Rouiller, C.2
  • 7
    • 84872149848 scopus 로고    scopus 로고
    • Conserved spatial organization of FG domains in the nuclear pore complex
    • Atkinson, C.E., A.L. Mattheyses, M. Kampmann, and S.M. Simon. 2013. Conserved spatial organization of FG domains in the nuclear pore complex. Biophys. J. 104:37-50. http://dx.doi.org/10.1016/j.bpj.2012.11.3823
    • (2013) Biophys. J. , vol.104 , pp. 37-50
    • Atkinson, C.E.1    Mattheyses, A.L.2    Kampmann, M.3    Simon, S.M.4
  • 11
    • 84893364894 scopus 로고    scopus 로고
    • Phase transitions and size scaling of membrane-less organelles
    • Brangwynne, C.P. 2013. Phase transitions and size scaling of membrane-less organelles. J. Cell Biol. 203:875-881. http://dx.doi.org/10.1083/jcb.201308087
    • (2013) J. Cell Biol. , vol.203 , pp. 875-881
    • Brangwynne, C.P.1
  • 13
    • 0344270858 scopus 로고    scopus 로고
    • Differential hydrophobicity drives self-assembly in Huntington's disease
    • Burke, M.G., R. Woscholski, and S.N. Yaliraki. 2003. Differential hydrophobicity drives self-assembly in Huntington's disease. Proc. Natl. Acad. Sci. USA. 100:13928-13933. http://dx.doi.org/10.1073/pnas.1936025100
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 13928-13933
    • Burke, M.G.1    Woscholski, R.2    Yaliraki, S.N.3
  • 14
    • 84883388081 scopus 로고    scopus 로고
    • Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin
    • Caron, N.S., C.R. Desmond, J. Xia, and R. Truant. 2013. Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin.Proc.Natl.Acad.Sci.USA.110:14610-14615.http://dx.doi.org/10.1073/pnas.1301342110
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. 14610-14615
    • Caron, N.S.1    Desmond, C.R.2    Xia, J.3    Truant, R.4
  • 15
    • 84887705196 scopus 로고    scopus 로고
    • Single-molecule imaging in vivo: the dancing building blocks of the cell
    • Coelho, M., N. Maghelli, and I.M. Tolić-Nørrelykke. 2013. Single-molecule imaging in vivo: the dancing building blocks of the cell. Integr. Biol. (Camb.). 5:748-758. http://dx.doi.org/10.1039/c3ib40018b
    • (2013) Integr. Biol. (Camb. ). , vol.5 , pp. 748-758
    • Coelho, M.1    Maghelli, N.2    Tolić-Nørrelykke, I.M.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
    • Crick, S.L., K.M. Ruff, K. Garai, C. Frieden, and R.V. Pappu. 2013. 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. http://dx.doi.org/10.1073/pnas.1320626110
    • (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
    • 84866671396 scopus 로고    scopus 로고
    • Mechanisms of small-molecule binding to intrinsically disordered proteins
    • Cuchillo, R., and J. Michel. 2012. Mechanisms of small-molecule binding to intrinsically disordered proteins. Biochem. Soc. Trans. 40:1004-1008. http://dx.doi.org/10.1042/BST20120086
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1004-1008
    • Cuchillo, R.1    Michel, J.2
  • 19
    • 84882364963 scopus 로고    scopus 로고
    • Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues
    • Das,R.K.,and R.V.Pappu.2013.Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues.Proc.Natl.Acad.Sci.USA.110:13392-13397.http://dx.doi.org/10.1073/pnas.1304749110
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. 13392-13397
    • Das, R.K.1    Pappu, R.V.2
  • 20
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28
    • Daughdrill, G.W., M.S. Chadsey, J.E. Karlinsey, K.T. Hughes, and F.W. Dahlquist. 1997. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nat. Struct. Biol. 4:285-291. http://dx.doi.org/10.1038/nsb0497-285
    • (1997) Nat. Struct. Biol , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 21
    • 84881170268 scopus 로고    scopus 로고
    • Neurofilament sidearms modulate parallel and crossed-filament orientations inducing nematic to isotropic and re-entrant birefringent hydrogels
    • Deek, J., P.J. Chung, J. Kayser, A.R. Bausch, and C.R. Safinya. 2013. Neurofilament sidearms modulate parallel and crossed-filament orientations inducing nematic to isotropic and re-entrant birefringent hydrogels. Nat. Commun. 4:2224. http://dx.doi.org/10.1038/ncomms3224
    • (2013) Nat. Commun. , vol.4 , pp. 2224
    • Deek, J.1    Chung, P.J.2    Kayser, J.3    Bausch, A.R.4    Safinya, C.R.5
  • 23
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded
    • Denning, D.P., S.S. Patel, V. Uversky, A.L. Fink, and M. Rexach. 2003. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl. Acad. Sci. USA. 100:2450-2455. http://dx.doi.org/10.1073/pnas.0437902100
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 24
    • 73649136475 scopus 로고    scopus 로고
    • Hydrophobicity as a possible reason for gelation of FG-rich nucleoporins
    • Diesinger, P.M., and D.W. Heermann. 2010. Hydrophobicity as a possible reason for gelation of FG-rich nucleoporins. Eur. Biophys. J. 39:299-306. http://dx.doi.org/10.1007/s00249-009-0544-8
    • (2010) Eur. Biophys. J. , vol.39 , pp. 299-306
    • Diesinger, P.M.1    Heermann, D.W.2
  • 25
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker, A.K., and Z. Obradovic. 2001. The protein trinity-linking function and disorder. Nat. Biotechnol. 19:805-806. http://dx.doi.org/10.1038/nbt0901-805
    • (2001) Nat. Biotechnol. , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 26
    • 78149497463 scopus 로고    scopus 로고
    • Drugs for 'protein clouds': targeting intrinsically disordered transcription factors
    • Dunker, A.K., and V.N. Uversky. 2010. Drugs for 'protein clouds': targeting intrinsically disordered transcription factors. Curr. Opin. Pharmacol. 10:782-788. http://dx.doi.org/10.1016/j.coph.2010.09.005
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 782-788
    • Dunker, A.K.1    Uversky, V.N.2
  • 28
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker, A.K., M.S. Cortese, P. Romero, L.M. Iakoucheva, and V.N. Uversky. 2005. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J. 272:5129-5148. http://dx.doi.org/10.1111/j.1742-4658.2005.04948.x
    • (2005) FEBS J. , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 29
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J., and P.E. Wright. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6:197-208. http://dx.doi.org/10.1038/ nrm1589
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 31
    • 84889583170 scopus 로고    scopus 로고
    • Pleomorphic ensembles: formation of large clusters composed of weakly interacting multivalent molecules
    • Falkenberg, C.V., M.L. Blinov, and L.M. Loew. 2013. Pleomorphic ensembles: formation of large clusters composed of weakly interacting multivalent molecules. Biophys. J. 105:2451-2460. http://dx.doi.org/10.1016/j.bpj.2013.10.016
    • (2013) Biophys. J. , vol.105 , pp. 2451-2460
    • Falkenberg, C.V.1    Blinov, M.L.2    Loew, L.M.3
  • 33
    • 84885179258 scopus 로고    scopus 로고
    • A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells
    • Feric, M., and C.P. Brangwynne. 2013. A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells. Nat. Cell Biol. 15:1253-1259. http://dx.doi.org/10.1038/ncb2830
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1253-1259
    • Feric, M.1    Brangwynne, C.P.2
  • 34
    • 84891389848 scopus 로고    scopus 로고
    • Entry into the nuclear pore complex is controlled by a cytoplasmic exclusion zone containing dynamic GLFG-repeat nucleoporin domains
    • Fiserova, J., M. Spink, S.A. Richards, C. Saunter, and M.W. Goldberg. 2014. Entry into the nuclear pore complex is controlled by a cytoplasmic exclusion zone containing dynamic GLFG-repeat nucleoporin domains. J. Cell Sci. 127:124-136. http://dx.doi.org/10.1242/jcs.133272
    • (2014) J. Cell Sci. , vol.127 , pp. 124-136
    • Fiserova, J.1    Spink, M.2    Richards, S.A.3    Saunter, C.4    Goldberg, M.W.5
  • 35
    • 78650441363 scopus 로고    scopus 로고
    • Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins
    • Fiumara, F., L. Fioriti, E.R. Kandel, and W.A. Hendrickson. 2010. Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins. Cell. 143:1121-1135. http://dx.doi.org/10 .1016/j.cell.2010.11.042
    • (2010) Cell , vol.143 , pp. 1121-1135
    • Fiumara, F.1    Fioriti, L.2    Kandel, E.R.3    Hendrickson, W.A.4
  • 36
    • 56049097680 scopus 로고    scopus 로고
    • Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules
    • Follis, A.V., D.I. Hammoudeh, H. Wang, E.V. Prochownik, and S.J. Metallo. 2008. Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules. Chem. Biol. 15:1149-1155. http://dx.doi.org/10.1016/j.chembiol.2008.09.011
    • (2008) Chem. Biol. , vol.15 , pp. 1149-1155
    • Follis, A.V.1    Hammoudeh, D.I.2    Wang, H.3    Prochownik, E.V.4    Metallo, S.J.5
  • 37
    • 84879751760 scopus 로고    scopus 로고
    • p53 Aggregates penetrate cells and induce the co-aggregation of intracellular p53
    • Forget, K.J., G. Tremblay, and X. Roucou. 2013. p53 Aggregates penetrate cells and induce the co-aggregation of intracellular p53. PLoS ONE. 8:e69242. http://dx.doi.org/10.1371/journal.pone.0069242
    • (2013) PLoS ONE , vol.8
    • Forget, K.J.1    Tremblay, G.2    Roucou, X.3
  • 39
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey, S., and D. Görlich. 2007. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell. 130:512- 523. http://dx.doi.org/10.1016/j.cell.2007.06.024
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Görlich, D.2
  • 40
    • 84903735072 scopus 로고    scopus 로고
    • In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery
    • Fromm, S.A., J. Kamenz, E.R. Nöldeke, A. Neu, G. Zocher, and R. Sprangers. 2014. In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery. Angew. Chem. Int. Ed. Engl. 53:7354-7359. http://dx.doi.org/10.1002/anie.201402885
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 7354-7359
    • Fromm, S.A.1    Kamenz, J.2    Nöldeke, E.R.3    Neu, A.4    Zocher, G.5    Sprangers, R.6
  • 41
    • 84881545245 scopus 로고    scopus 로고
    • Next generation organelles: structure and role of germ granules in the germline
    • Gao, M., and A.L. Arkov. 2013. Next generation organelles: structure and role of germ granules in the germline. Mol. Reprod. Dev. 80:610-623. http:// dx.doi.org/10.1002/mrd.22115
    • (2013) Mol. Reprod. Dev. , vol.80 , pp. 610-623
    • Gao, M.1    Arkov, A.L.2
  • 42
    • 84877576480 scopus 로고    scopus 로고
    • Single-molecule imaging of transcription factor binding to DNA in live mammalian cells
    • Gebhardt, J.C., D.M. Suter, R. Roy, Z.W. Zhao, A.R. Chapman, S. Basu, T. Maniatis, and X.S. Xie. 2013. Single-molecule imaging of transcription factor binding to DNA in live mammalian cells. Nat. Methods. 10:421- 426. http://dx.doi.org/10.1038/nmeth.2411
    • (2013) Nat. Methods. , vol.10 , pp. 421-426
    • Gebhardt, J.C.1    Suter, D.M.2    Roy, R.3    Zhao, Z.W.4    Chapman, A.R.5    Basu, S.6    Maniatis, T.7    Xie, X.S.8
  • 43
    • 80052802585 scopus 로고    scopus 로고
    • RNA-binding proteins with prion-like domains in ALS and FTLD-U
    • Gitler, A.D., and J. Shorter. 2011. RNA-binding proteins with prion-like domains in ALS and FTLD-U. Prion. 5:179-187. http://dx.doi.org/10.4161/pri .5.3.17230
    • (2011) Prion , vol.5 , pp. 179-187
    • Gitler, A.D.1    Shorter, J.2
  • 44
    • 35349007481 scopus 로고    scopus 로고
    • Allosteric inhibition of the protein-protein interaction between the leukemia-associated proteins Runx1 and CBFB. Chem
    • Gorczynski, M.J., J. Grembecka, Y. Zhou, Y. Kong, L. Roudaia, M.G. Douvas, M. Newman, I. Bielnicka, G. Baber, T. Corpora, et al. 2007. Allosteric inhibition of the protein-protein interaction between the leukemia-associated proteins Runx1 and CBFB. Chem. Biol. 14:1186-1197. http://dx.doi.org/10 .1016/j.chembiol.2007.09.006
    • (2007) Biol , vol.14 , pp. 1186-1197
    • Gorczynski, M.J.1    Grembecka, J.2    Zhou, Y.3    Kong, Y.4    Roudaia, L.5    Douvas, M.G.6    Newman, M.7    Bielnicka, I.8    Baber, G.9    Corpora, T.10
  • 45
    • 84870427355 scopus 로고    scopus 로고
    • Cellular strategies for regulating functional and nonfunctional protein aggregation
    • Gsponer, J., and M.M. Babu. 2012. Cellular strategies for regulating functional and nonfunctional protein aggregation. Cell Reports. 2:1425-1437. http:// dx.doi.org/10.1016/j.celrep.2012.09.036
    • (2012) Cell Reports , vol.2 , pp. 1425-1437
    • Gsponer, J.1    Babu, M.M.2
  • 46
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: from transcript synthesis to protein degradation
    • Gsponer, J., M.E. Futschik, S.A. Teichmann, and M.M. Babu. 2008. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science. 322:1365-1368. http://dx.doi.org/10.1126/ science.1163581
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 47
    • 84860863700 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies
    • Han, T.W., M. Kato, S. Xie, L.C. Wu, H. Mirzaei, J. Pei, M. Chen, Y. Xie, J. Allen, G. Xiao, and S.L. McKnight. 2012. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell. 149:768-779. http://dx.doi.org/10.1016/j.cell.2012.04.016
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1    Kato, M.2    Xie, S.3    Wu, L.C.4    Mirzaei, H.5    Pei, J.6    Chen, M.7    Xie, Y.8    Allen, J.9    Xiao, G.10    McKnight, S.L.11
  • 49
    • 84888344975 scopus 로고    scopus 로고
    • Recent discoveries and applications involving small-molecule microarrays
    • Hong, J.A., D.V. Neel, D. Wassaf, F. Caballero, and A.N. Koehler. 2014a. Recent discoveries and applications involving small-molecule microarrays. Curr. Opin. Chem. Biol. 18:21-28. http://dx.doi.org/10.1016/j .cbpa.2013.09.020
    • (2014) Curr. Opin. Chem. Biol. , vol.18 , pp. 21-28
    • Hong, J.A.1    Neel, D.V.2    Wassaf, D.3    Caballero, F.4    Koehler, A.N.5
  • 51
    • 78650512639 scopus 로고    scopus 로고
    • Breaking the diffraction barrier: super-resolution imaging of cells
    • Huang, B., H. Babcock, and X. Zhuang. 2010. Breaking the diffraction barrier: super-resolution imaging of cells. Cell. 143:1047-1058. http://dx.doi.org/10 .1016/j.cell.2010.12.002
    • (2010) Cell , vol.143 , pp. 1047-1058
    • Huang, B.1    Babcock, H.2    Zhuang, X.3
  • 52
    • 84865260520 scopus 로고    scopus 로고
    • The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model
    • Hülsmann, B.B., A.A. Labokha, and D. Görlich. 2012. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell. 150:738-751. http://dx.doi.org/10.1016/j.cell.2012.07.019
    • (2012) Cell , vol.150 , pp. 738-751
    • Hülsmann, B.B.1    Labokha, A.A.2    Görlich, D.3
  • 53
    • 0036408751 scopus 로고    scopus 로고
    • Intrinsic disorder in cell-signaling and cancer-associated proteins
    • Iakoucheva, L.M., C.J. Brown, J.D. Lawson, Z. Obradović, and A.K. Dunker. 2002. Intrinsic disorder in cell-signaling and cancer-associated proteins. J. Mol. Biol. 323:573-584. http://dx.doi.org/10.1016/S0022-2836(02)00969-5
    • (2002) J. Mol. Biol. , vol.323 , pp. 573-584
    • Iakoucheva, L.M.1    Brown, C.J.2    Lawson, J.D.3    Obradović, Z.4    Dunker, A.K.5
  • 55
    • 4544253735 scopus 로고    scopus 로고
    • Reversible aggregation plays a crucial role on the folding landscape of p53 core domain
    • Ishimaru, D., L.M. Lima, L.F. Maia, P.M. Lopez, A.P. Ano Bom, A.P. Valente, and J.L. Silva. 2004. Reversible aggregation plays a crucial role on the folding landscape of p53 core domain. Biophys. J. 87:2691-2700. http:// dx.doi.org/10.1529/biophysj.104.044685
    • (2004) Biophys. J. , vol.87 , pp. 2691-2700
    • Ishimaru, D.1    Lima, L.M.2    Maia, L.F.3    Lopez, P.M.4    Ano Bom, A.P.5    Valente, A.P.6    Silva, J.L.7
  • 56
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels
    • Kato, M., T.W. Han, S. Xie, K. Shi, X. Du, L.C. Wu, H. Mirzaei, E.J. Goldsmith, J. Longgood, J. Pei, et al. 2012. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell. 149:753-767. http://dx.doi.org/10.1016/j.cell.2012.04.017
    • (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
  • 57
    • 84884587610 scopus 로고    scopus 로고
    • Stress granules and cell signaling: more than just a passing phase?
    • Kedersha, N., P. Ivanov, and P. Anderson. 2013. Stress granules and cell signaling: more than just a passing phase? Trends Biochem. Sci. 38:494-506. http://dx.doi.org/10.1016/j.tibs.2013.07.004
    • (2013) Trends Biochem Sci , vol.38 , pp. 494-506
    • Kedersha, N.1    Ivanov, P.2    Anderson, P.3
  • 58
    • 84857911980 scopus 로고    scopus 로고
    • Unbiased binding assays for discovering small-molecule probes and drugs
    • Kemp, M.M., M. Weïwer, and A.N. Koehler. 2012. Unbiased binding assays for discovering small-molecule probes and drugs. Bioorg. Med. Chem. 20:1979-1989. http://dx.doi.org/10.1016/j.bmc.2011.11.071
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 1979-1989
    • Kemp, M.M.1    Weïwer, M.2    Koehler, A.N.3
  • 61
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King, O.D., A.D. Gitler, and J. Shorter. 2012. The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res. 1462:61-80.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 62
    • 79251573834 scopus 로고    scopus 로고
    • Dr. Jekyll and Mr. Hyde: The two faces of the FUS/EWS/ TAF15 protein family
    • Kovar, H. 2011. Dr. Jekyll and Mr. Hyde: The two faces of the FUS/EWS/ TAF15 protein family. Sarcoma. 2011:837474. http://dx.doi.org/10 .1155/2011/837474
    • (2011) Sarcoma , vol.2011 , pp. 837474
    • Kovar, H.1
  • 63
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity
    • Kriwacki, R.W., L. Hengst, L. Tennant, S.I. Reed, and P.E. Wright. 1996. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. USA. 93:11504-11509. http://dx.doi.org/10.1073/pnas.93.21.11504
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 64
    • 84888440451 scopus 로고    scopus 로고
    • Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains
    • Kwon, I., M. Kato, S. Xiang, L. Wu, P. Theodoropoulos, H. Mirzaei, T. Han, S. Xie, J.L. Corden, and S.L. McKnight. 2013. Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains. Cell. 155:1049-1060. http://dx.doi.org/10.1016/j.cell.2013 .10.033
    • (2013) Cell , vol.155 , pp. 1049-1060
    • Kwon, I.1    Kato, M.2    Xiang, S.3    Wu, L.4    Theodoropoulos, P.5    Mirzaei, H.6    Han, T.7    Xie, S.8    Corden, J.L.9    McKnight, S.L.10
  • 65
    • 84880730823 scopus 로고    scopus 로고
    • Huntington's disease: underlying molecular mechanisms and emerging concepts
    • Labbadia, J., and R.I. Morimoto. 2013. Huntington's disease: underlying molecular mechanisms and emerging concepts. Trends Biochem. Sci. 38:378- 385. http://dx.doi.org/10.1016/j.tibs.2013.05.003
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 378-385
    • Labbadia, J.1    Morimoto, R.I.2
  • 66
    • 34247347737 scopus 로고    scopus 로고
    • Ewings family oncoproteins: drunk, disorderly and in search of partners
    • Lee, K.A. 2007. Ewings family oncoproteins: drunk, disorderly and in search of partners. Cell Res. 17:286-288. http://dx.doi.org/10.1038/cr.2007.22
    • (2007) Cell Res , vol.17 , pp. 286-288
    • Lee, K.A.1
  • 67
    • 84897061952 scopus 로고    scopus 로고
    • Nucleolar dysfunction in Huntington's disease
    • Lee, J., Y.J. Hwang, H. Ryu, N.W. Kowall, and H. Ryu. 2014. Nucleolar dysfunction in Huntington's disease. Biochim. Biophys. Acta. 1842:785- 790. http://dx.doi.org/10.1016/j.bbadis.2013.09.017
    • (2014) Biochim. Biophys. Acta. , vol.1842 , pp. 785-790
    • Lee, J.1    Hwang, Y.J.2    Ryu, H.3    Kowall, N.W.4    Ryu, H.5
  • 69
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y.R., O.D. King, J. Shorter, and A.D. Gitler. 2013. Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201:361-372. http://dx.doi.org/ 10.1083/jcb.201302044
    • (2013) J. Cell Biol. , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 70
    • 84876288161 scopus 로고    scopus 로고
    • Protein disorder, prion propensities, and self-organizing macromolecular collectives
    • Malinovska, L., S. Kroschwald, and S. Alberti. 2013. Protein disorder, prion propensities, and self-organizing macromolecular collectives. Biochim. Biophys. Acta. 1834:918-931. http://dx.doi.org/10.1016/j.bbapap.2013.01.003
    • (2013) Biochim. Biophys. Acta. , vol.1834 , pp. 918-931
    • Malinovska, L.1    Kroschwald, S.2    Alberti, S.3
  • 71
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • Mao, A.H., S.L. Crick, A. Vitalis, C.L. Chicoine, and R.V. Pappu. 2010. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc. Natl. Acad. Sci. USA. 107:8183-8188. http:// dx.doi.org/10.1073/pnas.0911107107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 72
    • 49249114156 scopus 로고    scopus 로고
    • Bucky ball functions in Balbiani body assembly and animal-vegetal polarity in the oocyte and follicle cell layer in zebrafish
    • Marlow, F.L., and M.C. Mullins. 2008. Bucky ball functions in Balbiani body assembly and animal-vegetal polarity in the oocyte and follicle cell layer in zebrafish. Dev. Biol. 321:40-50. http://dx.doi.org/10.1016/j.ydbio.2008.05.557
    • (2008) Dev. Biol. , vol.321 , pp. 40-50
    • Marlow, F.L.1    Mullins, M.C.2
  • 73
    • 0033963010 scopus 로고    scopus 로고
    • Synthesis and structural characterization of poly(LGGVG), an elastin-like polypeptide
    • Martino, M., A. Coviello, and A.M. Tamburro. 2000. Synthesis and structural characterization of poly(LGGVG), an elastin-like polypeptide. Int. J. Biol. Macromol. 27:59-64. http://dx.doi.org/10.1016/S0141-8130(99) 00118-X
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 59-64
    • Martino, M.1    Coviello, A.2    Tamburro, A.M.3
  • 74
    • 77955327536 scopus 로고    scopus 로고
    • Intrinsically disordered proteins are potential drug targets
    • Metallo, S.J. 2010. Intrinsically disordered proteins are potential drug targets. Curr. Opin. Chem. Biol. 14:481-488. http://dx.doi.org/10.1016/j.cbpa .2010.06.169
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 481-488
    • Metallo, S.J.1
  • 75
    • 0035866357 scopus 로고    scopus 로고
    • Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hyperthermia
    • Meyer, D.E., G.A. Kong, M.W. Dewhirst, M.R. Zalutsky, and A. Chilkoti. 2001. Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hyperthermia. Cancer Res. 61:1548-1554.
    • (2001) Cancer Res , vol.61 , pp. 1548-1554
    • Meyer, D.E.1    Kong, G.A.2    Dewhirst, M.W.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 76
    • 67650385638 scopus 로고    scopus 로고
    • Protein disorder in the human diseasome: unfoldomics of human genetic diseases
    • Midic, U., C.J. Oldfield, A.K. Dunker, Z. Obradovic, and V.N. Uversky. 2009. Protein disorder in the human diseasome: unfoldomics of human genetic diseases. BMC Genomics. 10(Suppl 1):S12. http://dx.doi.org/10.1186/ 1471-2164-10-S1-S12
    • (2009) BMC Genomics , vol.10 , Issue.1 SUPPL
    • Midic, U.1    Oldfield, C.J.2    Dunker, A.K.3    Obradovic, Z.4    Uversky, V.N.5
  • 77
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: implications for nuclear architecture and gene expression
    • Misteli, T. 2001. Protein dynamics: implications for nuclear architecture and gene expression. Science. 291:843-847. http://dx.doi.org/10.1126/science .291.5505.843
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 78
    • 33947581390 scopus 로고    scopus 로고
    • The impact of translocations and gene fusions on cancer causation
    • Mitelman, F., B. Johansson, and F. Mertens. 2007. The impact of translocations and gene fusions on cancer causation. Nat. Rev. Cancer. 7:233-245. http://dx.doi.org/10.1038/nrc2091
    • (2007) Nat. Rev. Cancer. , vol.7 , pp. 233-245
    • Mitelman, F.1    Johansson, B.2    Mertens, F.3
  • 80
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag, T., L.E. Kay, and J.D. Forman-Kay. 2010. Protein dynamics and conformational disorder in molecular recognition. J. Mol. Recognit. 23:105-116.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 84
    • 33846317372 scopus 로고    scopus 로고
    • Multiple aromatic side chains within a disordered structure are critical for transcription and transforming activity of EWS family oncoproteins
    • Ng, K.P., G. Potikyan, R.O. Savene, C.T. Denny, V.N. Uversky, and K.A. Lee. 2007. Multiple aromatic side chains within a disordered structure are critical for transcription and transforming activity of EWS family oncoproteins. Proc. Natl. Acad. Sci. USA. 104:479-484. http://dx.doi.org/10 .1073/pnas.0607007104
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 479-484
    • Ng, K.P.1    Potikyan, G.2    Savene, R.O.3    Denny, C.T.4    Uversky, V.N.5    Lee, K.A.6
  • 85
    • 84893037928 scopus 로고    scopus 로고
    • Protein interactions in Xenopus germ plasm RNP particles
    • Nijjar, S., and H.R. Woodland. 2013. Protein interactions in Xenopus germ plasm RNP particles. PLoS ONE. 8:e80077. http://dx.doi.org/10.1371/ journal.pone.0080077
    • (2013) PLoS ONE , vol.8
    • Nijjar, S.1    Woodland, H.R.2
  • 86
    • 28444459361 scopus 로고
    • Electron microscopy: cytology of cell fractions
    • Novikoff, A.B. 1956. Electron microscopy: cytology of cell fractions. Science. 124:969-972. http://dx.doi.org/10.1126/science.124.3229.969
    • (1956) Science , vol.124 , pp. 969-972
    • Novikoff, A.B.1
  • 88
    • 70349972615 scopus 로고    scopus 로고
    • Analysis of Ewing sarcoma (EWS)-binding proteins: interaction with hnRNP M, U, and RNA-helicases p68/72 within protein-RNA complexes
    • Pahlich, S., L. Quero, B. Roschitzki, R.P. Leemann-Zakaryan, and H. Gehring. 2009. Analysis of Ewing sarcoma (EWS)-binding proteins: interaction with hnRNP M, U, and RNA-helicases p68/72 within protein-RNA complexes. J. Proteome Res. 8:4455-4465. http://dx.doi.org/10.1021/ pr900235t
    • (2009) J. Proteome Res. , vol.8 , pp. 4455-4465
    • Pahlich, S.1    Quero, L.2    Roschitzki, B.3    Leemann-Zakaryan, R.P.4    Gehring, H.5
  • 89
    • 36749056299 scopus 로고    scopus 로고
    • A polymer physics perspective on driving forces and mechanisms for protein aggregation
    • Pappu, R.V., X. Wang, A. Vitalis, and S.L. Crick. 2008. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Arch. Biochem. Biophys. 469:132-141. http://dx.doi.org/10.1016/j.abb .2007.08.033
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 132-141
    • Pappu, R.V.1    Wang, X.2    Vitalis, A.3    Crick, S.L.4
  • 90
    • 79960925229 scopus 로고    scopus 로고
    • The Ewing sarcoma protein regulates DNA damage-induced alternative splicing
    • Paronetto, M.P., B. Miñana, and J. Valcárcel. 2011. The Ewing sarcoma protein regulates DNA damage-induced alternative splicing. Mol. Cell. 43:353- 368. http://dx.doi.org/10.1016/j.molcel.2011.05.035
    • (2011) Mol. Cell , vol.43 , pp. 353-368
    • Paronetto, M.P.1    Miñana, B.2    Valcárcel, J.3
  • 91
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel, S.S., B.J. Belmont, J.M. Sante, and M.F. Rexach. 2007. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell. 129:83-96. http://dx.doi.org/10.1016/j.cell.2007.01.044
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 92
    • 77949360998 scopus 로고    scopus 로고
    • Modularity of intrinsic disorder in the human proteome
    • Pentony, M.M., and D.T. Jones. 2010. Modularity of intrinsic disorder in the human proteome. Proteins. 78:212-221. http://dx.doi.org/10.1002/prot.22504
    • (2010) Proteins , vol.78 , pp. 212-221
    • Pentony, M.M.1    Jones, D.T.2
  • 93
    • 0035943050 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: diffusion channel or phase transition? Curr
    • Rabut, G., and J. Ellenberg. 2001. Nucleocytoplasmic transport: diffusion channel or phase transition? Curr. Biol. 11:R551-R554. http://dx.doi.org/10 .1016/S0960-9822(01)00340-2
    • (2001) Biol , vol.11
    • Rabut, G.1    Ellenberg, J.2
  • 94
    • 0029021567 scopus 로고
    • The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex
    • Radu, A., M.S. Moore, and G. Blobel. 1995. The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell. 81:215-222. http://dx.doi.org/10.1016/0092-8674(95)90331-3
    • (1995) Cell , vol.81 , pp. 215-222
    • Radu, A.1    Moore, M.S.2    Blobel, G.3
  • 95
    • 0035188314 scopus 로고    scopus 로고
    • Sequence complexity of disordered protein
    • Romero, P., Z. Obradovic, X. Li, E.C. Garner, C.J. Brown, and A.K. Dunker. 2001. Sequence complexity of disordered protein. Proteins. 42:38-48. http://dx.doi .org/10.1002/1097-0134(20010101)42:1<38::AID-PROT50>3.0.CO;2-3
    • (2001) Proteins , vol.42 , pp. 38-48
    • Romero, P.1    Obradovic, Z.2    Li, X.3    Garner, E.C.4    Brown, C.J.5    Dunker, A.K.6
  • 98
    • 34250719724 scopus 로고    scopus 로고
    • Generation of a fluorescently labeled endogenous protein library in living human cells
    • Sigal, A., T. Danon, A. Cohen, R. Milo, N. Geva-Zatorsky, G. Lustig, Y. Liron, U. Alon, and N. Perzov. 2007. Generation of a fluorescently labeled endogenous protein library in living human cells. Nat. Protoc. 2:1515-1527. http://dx.doi.org/10.1038/nprot.2007.197
    • (2007) Nat. Protoc. , vol.2 , pp. 1515-1527
    • Sigal, A.1    Danon, T.2    Cohen, A.3    Milo, R.4    Geva-Zatorsky, N.5    Lustig, G.6    Liron, Y.7    Alon, U.8    Perzov, N.9
  • 99
    • 84897513201 scopus 로고    scopus 로고
    • Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments
    • Soranno, A., I. Koenig, M.B. Borgia, H. Hofmann, F. Zosel, D. Nettels, and B. Schuler. 2014. Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments. Proc. Natl. Acad. Sci. USA. 111:4874-4879. http://dx.doi.org/10.1073/pnas.1322611111
    • (2014) Proc. Natl. Acad. Sci. USA. , vol.111 , pp. 4874-4879
    • Soranno, A.1    Koenig, I.2    Borgia, M.B.3    Hofmann, H.4    Zosel, F.5    Nettels, D.6    Schuler, B.7
  • 101
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn, L.A., T. Shen, N. Shulga, D.S. Goldfarb, and S.R. Wente. 2004. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat. Cell Biol. 6:197-206. http://dx.doi.org/10.1038/ncb1097
    • (2004) Nat. Cell Biol. , vol.6 , pp. 197-206
    • Strawn, L.A.1    Shen, T.2    Shulga, N.3    Goldfarb, D.S.4    Wente, S.R.5
  • 102
    • 34748839688 scopus 로고    scopus 로고
    • Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex
    • Terry, L.J., and S.R. Wente. 2007. Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex. J. Cell Biol. 178:1121-1132. http://dx.doi.org/10.1083/jcb.200704174
    • (2007) J. Cell Biol. , vol.178 , pp. 1121-1132
    • Terry, L.J.1    Wente, S.R.2
  • 103
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. 2002. Intrinsically unstructured proteins. Trends Biochem. Sci. 27:527- 533. http://dx.doi.org/10.1016/S0968-0004(02)02169-2
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 104
    • 84904005219 scopus 로고    scopus 로고
    • Hydrogel formation by multivalent IDPs: A reincarnation of the microtrabecular lattice? Intrinsically Disord
    • Tompa, P. 2013. Hydrogel formation by multivalent IDPs: A reincarnation of the microtrabecular lattice? Intrinsically Disord. Proteins. 1:e24068. http:// dx.doi.org/10.4161/idp.24068
    • (2013) Proteins , vol.1
    • Tompa, P.1
  • 105
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa, P., and M. Fuxreiter. 2008. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 33:2- 8. http://dx.doi.org/10.1016/j.tibs.2007.10.003
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 106
    • 79955497151 scopus 로고    scopus 로고
    • P granules extend the nuclear pore complex environment in the C. elegans germ line
    • Updike, D.L., S.J. Hachey, J. Kreher, and S. Strome. 2011. P granules extend the nuclear pore complex environment in the C. elegans germ line. J. Cell Biol. 192:939-948. http://dx.doi.org/10.1083/jcb.201010104
    • (2011) J. Cell Biol. , vol.192 , pp. 939-948
    • Updike, D.L.1    Hachey, S.J.2    Kreher, J.3    Strome, S.4
  • 107
    • 33744502102 scopus 로고    scopus 로고
    • Ewing's sarcoma oncoprotein EWS-FLI1: the perfect target without a therapeutic agent
    • Üren, A., and J.A. Toretsky. 2005. Ewing's sarcoma oncoprotein EWS-FLI1: the perfect target without a therapeutic agent. Future Oncol. 1:521-528. http://dx.doi.org/10.2217/14796694.1.4.521
    • (2005) Future Oncol , vol.1 , pp. 521-528
    • Üren, A.1    Toretsky, J.A.2
  • 108
    • 6344280796 scopus 로고    scopus 로고
    • Recombinant EWS-FLI1 oncoprotein activates transcription
    • Üren, A., O. Tcherkasskaya, and J.A. Toretsky. 2004. Recombinant EWS-FLI1 oncoprotein activates transcription. Biochemistry. 43:13579-13589. http://dx.doi.org/10.1021/bi048776q
    • (2004) Biochemistry , vol.43 , pp. 13579-13589
    • Üren, A.1    Tcherkasskaya, O.2    Toretsky, J.A.3
  • 111
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri, T., J.I. Semple, R. Garcia-Verdugo, and B. Lehner. 2009. Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell. 138:198-208. http://dx.doi.org/10.1016/ j.cell.2009.04.029
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 112
    • 77958095167 scopus 로고    scopus 로고
    • Phase transitions of folded proteins
    • Vekilov, P.G. 2010. Phase transitions of folded proteins. Soft Matter. 6:5254- 5272. http://dx.doi.org/10.1039/c0sm00215a
    • (2010) Soft Matter , vol.6 , pp. 5254-5272
    • Vekilov, P.G.1
  • 114
    • 0041418213 scopus 로고    scopus 로고
    • Flavors of protein disorder
    • Vucetic, S., C.J. Brown, A.K. Dunker, and Z. Obradovic. 2003. Flavors of protein disorder. Proteins. 52:573-584. http://dx.doi.org/10.1002/prot.10437
    • (2003) Proteins , vol.52 , pp. 573-584
    • Vucetic, S.1    Brown, C.J.2    Dunker, A.K.3    Obradovic, Z.4
  • 115
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J.J., J.S. Sodhi, L.J. McGuffin, B.F. Buxton, and D.T. Jones. 2004. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337:635-645. http://dx.doi.org/10 .1016/j.jmb.2004.02.002
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 116
    • 84861964894 scopus 로고    scopus 로고
    • Getting RNA and protein in phase
    • Weber, S.C., and C.P. Brangwynne. 2012. Getting RNA and protein in phase. Cell. 149:1188-1191. http://dx.doi.org/10.1016/j.cell.2012.05.022
    • (2012) Cell , vol.149 , pp. 1188-1191
    • Weber, S.C.1    Brangwynne, C.P.2
  • 117
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P.H., W. Zhen, A.W. Poon, K.A. Conway, and P.T. Lansbury Jr. 1996. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry. 35:13709-13715. http://dx.doi .org/10.1021/bi961799n
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr, P.T.5
  • 118
    • 0026463881 scopus 로고
    • A new family of yeast nuclear pore complex proteins
    • Wente, S.R., M.P. Rout, and G. Blobel. 1992. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119:705-723. http://dx.doi.org/10 .1083/jcb.119.4.705
    • (1992) J. Cell Biol. , vol.119 , pp. 705-723
    • Wente, S.R.1    Rout, M.P.2    Blobel, G.3
  • 119
    • 0027049622 scopus 로고
    • A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1
    • Wimmer, C., V. Doye, P. Grandi, U. Nehrbass, and E.C. Hurt. 1992. A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. EMBO J. 11:5051-5061.
    • (1992) EMBO J , vol.11 , pp. 5051-5061
    • Wimmer, C.1    Doye, V.2    Grandi, P.3    Nehrbass, U.4    Hurt, E.C.5
  • 120
    • 84874040052 scopus 로고    scopus 로고
    • Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling
    • Wippich, F., B. Bodenmiller, M.G. Trajkovska, S. Wanka, R. Aebersold, and L. Pelkmans. 2013. Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling. Cell. 152:791-805. http://dx.doi.org/10.1016/j.cell.2013.01.033
    • (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
  • 121
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: reassessing the protein structure-function paradigm
    • Wright, P.E., and H.J. Dyson. 1999. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J. Mol. Biol. 293:321- 331. http://dx.doi.org/10.1006/jmbi.1999.3110
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 122
    • 60349101875 scopus 로고    scopus 로고
    • Linking folding and binding
    • Wright, P.E., and H.J. Dyson. 2009. Linking folding and binding. Curr. Opin. Struct. Biol. 19:31-38. http://dx.doi.org/10.1016/j.sbi.2008.12.003
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 31-38
    • Wright, P.E.1    Dyson, H.J.2
  • 126
    • 0142057146 scopus 로고    scopus 로고
    • Low molecular weight inhibitors of Myc-Max interaction and function
    • Yin, X., C. Giap, J.S. Lazo, and E.V. Prochownik. 2003. Low molecular weight inhibitors of Myc-Max interaction and function. Oncogene. 22:6151- 6159. http://dx.doi.org/10.1038/sj.onc.1206641
    • (2003) Oncogene , vol.22 , pp. 6151-6159
    • Yin, X.1    Giap, C.2    Lazo, J.S.3    Prochownik, E.V.4
  • 127
    • 84892562730 scopus 로고    scopus 로고
    • Spatial organization of RNA polymerase II inside a mammalian cell nucleus revealed by reflected light-sheet superresolution microscopy
    • Zhao, Z.W., R. Roy, J.C. Gebhardt, D.M. Suter, A.R. Chapman, and X.S. Xie. 2014. Spatial organization of RNA polymerase II inside a mammalian cell nucleus revealed by reflected light-sheet superresolution microscopy. Proc. Natl. Acad. Sci. USA. 111:681-686. http://dx.doi.org/10.1073/ pnas.1318496111
    • (2014) Proc. Natl. Acad. Sci. USA. , vol.111 , pp. 681-686
    • Zhao, Z.W.1    Roy, R.2    Gebhardt, J.C.3    Suter, D.M.4    Chapman, A.R.5    Xie, X.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.