메뉴 건너뛰기




Volumn 42, Issue 10, 2017, Pages 765-776

There Is an Inclusion for That: Material Properties of Protein Granules Provide a Platform for Building Diverse Cellular Functions

Author keywords

aggregation; amyloid; clustering; liquid liquid phase separation; phase transition; RNA protein granules

Indexed keywords

CELL FUNCTION; CELL METABOLISM; CELL STRUCTURE; ENZYME MODIFICATION; LIQUID LIQUID EXTRACTION; MEMORY CONSOLIDATION; NUCLEAR PORE COMPLEX; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; REVIEW; CHEMISTRY; HUMAN; METABOLISM;

EID: 85028466326     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2017.08.002     Document Type: Review
Times cited : (46)

References (90)
  • 1
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose, G.D., et al. Hydrophobicity of amino acid residues in globular proteins. Science 229 (1985), 834–838.
    • (1985) Science , vol.229 , pp. 834-838
    • Rose, G.D.1
  • 2
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhnovich, E.I., Theoretical studies of protein-folding thermodynamics and kinetics. Curr. Opin. Struct. Biol. 7 (1997), 29–40.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 3
    • 79960182560 scopus 로고    scopus 로고
    • Allostery in protein domains reflects a balance of steric and hydrophobic effects
    • England, J.L., Allostery in protein domains reflects a balance of steric and hydrophobic effects. Structure 19 (2011), 967–975.
    • (2011) Structure , vol.19 , pp. 967-975
    • England, J.L.1
  • 4
    • 84884587610 scopus 로고    scopus 로고
    • Stress granules and cell signaling: more than just a passing phase?
    • Kedersha, N., et al. Stress granules and cell signaling: more than just a passing phase?. Trends Biochem. Sci. 38 (2013), 494–506.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 494-506
    • Kedersha, N.1
  • 5
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito, R.R., Sitia, R., Aggresomes and Russell bodies. Symptoms of cellular indigestion?. EMBO Rep. 1 (2000), 225–231.
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 6
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich, D., et al. Misfolded proteins partition between two distinct quality control compartments. Nature, 454, 2008, 1088.
    • (2008) Nature , vol.454 , pp. 1088
    • Kaganovich, D.1
  • 7
    • 0020826867 scopus 로고
    • Formation of cytoplasmic
    • Nover, L., et al. Formation of cytoplasmic. Mol. Cell. Biol. 3 (1983), 1648–1655.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1648-1655
    • Nover, L.1
  • 8
    • 84991238633 scopus 로고    scopus 로고
    • Principles and properties of stress granules
    • Protter, D.S.W., Parker, R., Principles and properties of stress granules. Trends Cell Biol. 26 (2016), 668–679.
    • (2016) Trends Cell Biol. , vol.26 , pp. 668-679
    • Protter, D.S.W.1    Parker, R.2
  • 9
    • 84868149498 scopus 로고    scopus 로고
    • Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast
    • Spokoini, R., et al. Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep. 2 (2012), 738–747.
    • (2012) Cell Rep. , vol.2 , pp. 738-747
    • Spokoini, R.1
  • 10
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston, J., et al. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143 (1998), 1883–1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.1
  • 11
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., et al. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004), 805–810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1
  • 12
    • 85005975973 scopus 로고    scopus 로고
    • A new view into the regulation of purine metabolism: the purinosome
    • Pedley, A.M., Benkovic, S.J., A new view into the regulation of purine metabolism: the purinosome. Trends Biochem. Sci. 42 (2016), 141–154.
    • (2016) Trends Biochem. Sci. , vol.42 , pp. 141-154
    • Pedley, A.M.1    Benkovic, S.J.2
  • 13
    • 33745824614 scopus 로고    scopus 로고
    • ALIS are stress-induced protein storage compartments for substrates of the proteasome and autophagy
    • Szeto, J., et al. ALIS are stress-induced protein storage compartments for substrates of the proteasome and autophagy. Autophagy, 2, 2006, 189.
    • (2006) Autophagy , vol.2 , pp. 189
    • Szeto, J.1
  • 14
    • 1442358797 scopus 로고    scopus 로고
    • Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins
    • Lelouard, H., et al. Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins. J. Cell Biol. 164 (2004), 667–675.
    • (2004) J. Cell Biol. , vol.164 , pp. 667-675
    • Lelouard, H.1
  • 15
    • 84921936587 scopus 로고    scopus 로고
    • Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease. Cell. Mol
    • Amen, T., Kaganovich, D., Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease. Cell. Mol. Life Sci. 72 (2015), 401–415.
    • (2015) Life Sci. , vol.72 , pp. 401-415
    • Amen, T.1    Kaganovich, D.2
  • 16
    • 84980413864 scopus 로고    scopus 로고
    • Droplet organelles?
    • Courchaine, E.M., et al. Droplet organelles?. EMBO J. 35 (2016), 1603–1612.
    • (2016) EMBO J. , vol.35 , pp. 1603-1612
    • Courchaine, E.M.1
  • 17
    • 84866883258 scopus 로고    scopus 로고
    • Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity
    • Weisberg, S.J., et al. Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 15811–15816.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 15811-15816
    • Weisberg, S.J.1
  • 18
    • 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. U. S. A. 111 (2014), 8049–8054.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 8049-8054
    • Ogrodnik, M.1
  • 19
    • 84898003419 scopus 로고    scopus 로고
    • The aggregation and inheritance of damaged proteins determines cell fate during mitosis
    • Bufalino, M.R., van der Kooy, D., The aggregation and inheritance of damaged proteins determines cell fate during mitosis. Cell Cycle 13 (2014), 1201–1207.
    • (2014) Cell Cycle , vol.13 , pp. 1201-1207
    • Bufalino, M.R.1    van der Kooy, D.2
  • 20
    • 85045772441 scopus 로고    scopus 로고
    • Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes
    • Rujano, M.A., et al. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol., 4, 2006, e417.
    • (2006) PLoS Biol. , vol.4 , pp. e417
    • Rujano, M.A.1
  • 21
    • 78651350812 scopus 로고    scopus 로고
    • Polyglutamine shows a urea-like affinity for unfolded cytosolic protein
    • England, J.L., Kaganovich, D., Polyglutamine shows a urea-like affinity for unfolded cytosolic protein. FEBS Lett. 585 (2011), 381–384.
    • (2011) FEBS Lett. , vol.585 , pp. 381-384
    • England, J.L.1    Kaganovich, D.2
  • 22
    • 84946554664 scopus 로고    scopus 로고
    • Polymer physics of intracellular phase transitions
    • Brangwynne, C.P., et al. Polymer physics of intracellular phase transitions. Nat. Phys. 11 (2015), 899–904.
    • (2015) Nat. Phys. , vol.11 , pp. 899-904
    • Brangwynne, C.P.1
  • 23
    • 85017114294 scopus 로고    scopus 로고
    • Minimum energetic cost to maintain a target nonequilibrium state
    • 042102
    • Horowitz, J.M., et al. Minimum energetic cost to maintain a target nonequilibrium state. Phys. Rev., 95, 2017 042102.
    • (2017) Phys. Rev. , vol.95
    • Horowitz, J.M.1
  • 24
    • 85045777544 scopus 로고    scopus 로고
    • A first order phase transition underlies the formation of sub-diffractive protein aggregates in mammalian cells
    • Narayanan, A., et al. A first order phase transition underlies the formation of sub-diffractive protein aggregates in mammalian cells. bioRxiv, 2017, 10.1101/148395.
    • (2017) bioRxiv
    • Narayanan, A.1
  • 25
    • 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 (2009), 1729–1732.
    • (2009) Science , vol.324 , pp. 1729-1732
    • Brangwynne, C.P.1
  • 26
    • 84996561763 scopus 로고    scopus 로고
    • Biophysical characterization of organelle-based RNA/protein liquid phases using microfluidics
    • Taylor, N., et al. Biophysical characterization of organelle-based RNA/protein liquid phases using microfluidics. Soft Matter 12 (2016), 9142–9150.
    • (2016) Soft Matter , vol.12 , pp. 9142-9150
    • Taylor, N.1
  • 27
    • 56849099636 scopus 로고    scopus 로고
    • Prion switching in response to environmental stress
    • Tyedmers, J., et al. Prion switching in response to environmental stress. PLoS Biol., 6, 2008, e294.
    • (2008) PLoS Biol. , vol.6 , pp. e294
    • Tyedmers, J.1
  • 28
    • 78049361927 scopus 로고    scopus 로고
    • Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits
    • Halfmann, R., Lindquist, S., Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science 330 (2010), 629–632.
    • (2010) Science , vol.330 , pp. 629-632
    • Halfmann, R.1    Lindquist, S.2
  • 29
    • 23044455461 scopus 로고    scopus 로고
    • A possible epigenetic mechanism for the persistence of memory
    • Si, K., et al. A possible epigenetic mechanism for the persistence of memory. Cold Spring Harb. Symp. Quant. Biol. 69 (2004), 497–498.
    • (2004) Cold Spring Harb. Symp. Quant. Biol. , vol.69 , pp. 497-498
    • Si, K.1
  • 30
    • 84962191260 scopus 로고    scopus 로고
    • Protein aggregation as a mechanism of adaptive cellular responses
    • Saarikangas, J., Barral, Y., Protein aggregation as a mechanism of adaptive cellular responses. Curr Genet. 62 (2016), 711–724.
    • (2016) Curr Genet. , vol.62 , pp. 711-724
    • Saarikangas, J.1    Barral, Y.2
  • 31
    • 70349705441 scopus 로고    scopus 로고
    • Prions: protein aggregation and infectious diseases
    • Aguzzi, A., Calella, A.M., Prions: protein aggregation and infectious diseases. Physiol. Rev. 89 (2009), 1105–1152.
    • (2009) Physiol. Rev. , vol.89 , pp. 1105-1152
    • Aguzzi, A.1    Calella, A.M.2
  • 32
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti, S., et al. 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
  • 33
    • 84988447127 scopus 로고    scopus 로고
    • Are aberrant phase transitions a driver of cellular aging?
    • Alberti, S., Hyman, A.A., Are aberrant phase transitions a driver of cellular aging?. Bioessays 8 (2016), 959–968.
    • (2016) Bioessays , vol.8 , pp. 959-968
    • Alberti, S.1    Hyman, A.A.2
  • 34
    • 84978472995 scopus 로고    scopus 로고
    • Compositional control of phase-separated cellular bodies
    • Banani, S.F., et al. Compositional control of phase-separated cellular bodies. Cell 166 (2016), 651–663.
    • (2016) Cell , vol.166 , pp. 651-663
    • Banani, S.F.1
  • 35
    • 0028308104 scopus 로고
    • URE3 as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner, R.B., URE3 as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264 (1994), 566–569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 36
    • 85014627153 scopus 로고    scopus 로고
    • Cross-b polymerization of low complexity sequence domains
    • a023598
    • Kato, M., Mcknight, S.L., Cross-b polymerization of low complexity sequence domains. Cold Spring Harb. Perspect. Biol., 9, 2016 a023598.
    • (2016) Cold Spring Harb. Perspect. Biol. , vol.9
    • Kato, M.1    Mcknight, S.L.2
  • 37
    • 84961869803 scopus 로고    scopus 로고
    • Phase separation: linking cellular compartmentalization to disease
    • Aguzzi, A., Altmeyer, M., Phase separation: linking cellular compartmentalization to disease. Trends Cell Biol. 26 (2016), 547–558.
    • (2016) Trends Cell Biol. , vol.26 , pp. 547-558
    • Aguzzi, A.1    Altmeyer, M.2
  • 38
    • 85009211737 scopus 로고    scopus 로고
    • Spatiotemporal control of intracellular phase transitions using light-activated optodroplets
    • Shin, Y., et al. Spatiotemporal control of intracellular phase transitions using light-activated optodroplets. Cell 168 (2017), 159–171.
    • (2017) Cell , vol.168 , pp. 159-171
    • Shin, Y.1
  • 39
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • An, S., et al. Reversible compartmentalization of de novo purine biosynthetic complexes in living cells. Science 320 (2008), 103–106.
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1
  • 40
    • 84924943411 scopus 로고    scopus 로고
    • Quantitative analysis of purine nucleotides indicates that purinosomes increase de novo purine biosynthesis
    • Zhao, H., et al. Quantitative analysis of purine nucleotides indicates that purinosomes increase de novo purine biosynthesis. J. Biol. Chem. 290 (2015), 6705–6713.
    • (2015) J. Biol. Chem. , vol.290 , pp. 6705-6713
    • Zhao, H.1
  • 41
    • 84962634585 scopus 로고    scopus 로고
    • Glycolytic enzymes localize to synapses under energy stress to support synaptic function
    • Jang, S.R., et al. Glycolytic enzymes localize to synapses under energy stress to support synaptic function. Neuron 90 (2016), 278–291.
    • (2016) Neuron , vol.90 , pp. 278-291
    • Jang, S.R.1
  • 42
    • 84979502187 scopus 로고    scopus 로고
    • RNA Polymerase II cluster dynamics predict mRNA output in living cells
    • Cho, W.K., et al. RNA Polymerase II cluster dynamics predict mRNA output in living cells. Elife 5 (2016), 1–31.
    • (2016) Elife , vol.5 , pp. 1-31
    • Cho, W.K.1
  • 43
    • 84975297725 scopus 로고    scopus 로고
    • Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis
    • Tatomer, D.C., et al. Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis. J. Cell Biol. 213 (2016), 557–570.
    • (2016) J. Cell Biol. , vol.213 , pp. 557-570
    • Tatomer, D.C.1
  • 44
    • 84962798412 scopus 로고    scopus 로고
    • Phase separation of signaling molecules promotes T cell receptor signal transduction
    • Su, X., et al. Phase separation of signaling molecules promotes T cell receptor signal transduction. Science 352 (2016), 595–599.
    • (2016) Science , vol.352 , pp. 595-599
    • Su, X.1
  • 45
    • 84928596005 scopus 로고    scopus 로고
    • Nuclear bodies: the emerging biophysics of nucleoplasmic phases
    • Zhu, L., Brangwynne, C.P., Nuclear bodies: the emerging biophysics of nucleoplasmic phases. Curr. Opin. Cell Biol. 34 (2015), 23–30.
    • (2015) Curr. Opin. Cell Biol. , vol.34 , pp. 23-30
    • Zhu, L.1    Brangwynne, C.P.2
  • 46
    • 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). Nat. Commun., 6, 2015, 8088.
    • (2015) Nat. Commun. , vol.6 , pp. 8088
    • Altmeyer, M.1
  • 47
    • 84923878820 scopus 로고    scopus 로고
    • Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles
    • Nott, T.J., et al. Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. Mol. Cell 57 (2015), 936–947.
    • (2015) Mol. Cell , vol.57 , pp. 936-947
    • Nott, T.J.1
  • 48
    • 84971323601 scopus 로고    scopus 로고
    • Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters
    • Nott, T.J., et al. Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters. Nat. Chem. 8 (2016), 569–575.
    • (2016) Nat. Chem. , vol.8 , pp. 569-575
    • Nott, T.J.1
  • 49
    • 84951794735 scopus 로고    scopus 로고
    • Transport selectivity of nuclear pores, phase separation, and membraneless organelles
    • Schmidt, H.B., Görlich, D., Transport selectivity of nuclear pores, phase separation, and membraneless organelles. Trends Biochem. Sci. 41 (2016), 46–61.
    • (2016) Trends Biochem. Sci. , vol.41 , pp. 46-61
    • Schmidt, H.B.1    Görlich, D.2
  • 50
    • 85047593740 scopus 로고    scopus 로고
    • Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity
    • Schmidt, H.B., Görlich, D., 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
  • 51
    • 84900329183 scopus 로고    scopus 로고
    • Cellular maintenance of nuclear protein homeostasis
    • Gallagher, P.S., et al. Cellular maintenance of nuclear protein homeostasis. Cell. Mol. Life Sci. 71 (2014), 1865–1879.
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 1865-1879
    • Gallagher, P.S.1
  • 52
    • 85013025287 scopus 로고    scopus 로고
    • Restricted access: spatial sequestration of damaged proteins during stress and aging
    • Hill, S.M., et al. Restricted access: spatial sequestration of damaged proteins during stress and aging. EMBO Rep. 18 (2017), 377–391.
    • (2017) EMBO Rep. , vol.18 , pp. 377-391
    • Hill, S.M.1
  • 53
    • 84865277422 scopus 로고    scopus 로고
    • Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
    • Malinovska, L., et al. Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol. Biol. Cell 23 (2012), 3041–3056.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3041-3056
    • Malinovska, L.1
  • 54
    • 85045771987 scopus 로고    scopus 로고
    • A surveillance function of the HSPB8-BAG3-HSP70 chaperone complex ensures stress
    • Ganassi, M., et al. A surveillance function of the HSPB8-BAG3-HSP70 chaperone complex ensures stress. Mol. Cell 63 (2016), 1–15.
    • (2016) Mol. Cell , vol.63 , pp. 1-15
    • Ganassi, M.1
  • 55
    • 84941339084 scopus 로고    scopus 로고
    • Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress
    • Wallace, E.W.J., et al. Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress. Cell 162 (2015), 1286–1298.
    • (2015) Cell , vol.162 , pp. 1286-1298
    • Wallace, E.W.J.1
  • 56
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • Escusa-Toret, S., et al. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat. Cell Biol. 15 (2013), 1231–1243.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1
  • 57
    • 84978472948 scopus 로고    scopus 로고
    • Asymmetric inheritance of aggregated proteins and age reset in yeast are regulated by Vac17-dependent vacuolar functions
    • Hill, S.M., et al. Asymmetric inheritance of aggregated proteins and age reset in yeast are regulated by Vac17-dependent vacuolar functions. Cell Rep. 16 (2016), 826–838.
    • (2016) Cell Rep. , vol.16 , pp. 826-838
    • Hill, S.M.1
  • 58
    • 84930577438 scopus 로고    scopus 로고
    • Lipid droplets are essential for efficient clearance of cytosolic inclusion bodies
    • Moldavski, O., et al. Lipid droplets are essential for efficient clearance of cytosolic inclusion bodies. Dev. Cell 33 (2016), 603–610.
    • (2016) Dev. Cell , vol.33 , pp. 603-610
    • Moldavski, O.1
  • 59
    • 85002045810 scopus 로고    scopus 로고
    • Creating age asymmetry: consequences of inheriting damaged goods in mammalian cells
    • Moore, D.L., Jessberger, S., Creating age asymmetry: consequences of inheriting damaged goods in mammalian cells. Trends Cell Biol. 27 (2017), 82–92.
    • (2017) Trends Cell Biol. , vol.27 , pp. 82-92
    • Moore, D.L.1    Jessberger, S.2
  • 60
    • 84898615077 scopus 로고    scopus 로고
    • Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance
    • Öling, D., et al. Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance. EMBO J. 33 (2014), 747–761.
    • (2014) EMBO J. , vol.33 , pp. 747-761
    • Öling, D.1
  • 61
    • 84949945857 scopus 로고    scopus 로고
    • Protein aggregates are associated with replicative aging without compromising protein quality control
    • Saarikangas, J., Barral, Y., Protein aggregates are associated with replicative aging without compromising protein quality control. Elife 4 (2015), 1–24.
    • (2015) Elife , vol.4 , pp. 1-24
    • Saarikangas, J.1    Barral, Y.2
  • 62
    • 85014061117 scopus 로고    scopus 로고
    • Compartmentalization of ER-bound chaperone confines protein deposit formation to the aging yeast cell
    • Saarikangas, J., et al. Compartmentalization of ER-bound chaperone confines protein deposit formation to the aging yeast cell. Curr. Biol. 27 (2017), 773–783.
    • (2017) Curr. Biol. , vol.27 , pp. 773-783
    • Saarikangas, J.1
  • 63
    • 84926302528 scopus 로고    scopus 로고
    • Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control
    • Gallina, I., et al. Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control. Nat. Commun., 6, 2015, 6533.
    • (2015) Nat. Commun. , vol.6 , pp. 6533
    • Gallina, I.1
  • 64
    • 84924864644 scopus 로고    scopus 로고
    • Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition
    • Miller, S.B.M., et al. Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. EMBO J. 34 (2015), 778–797.
    • (2015) EMBO J. , vol.34 , pp. 778-797
    • Miller, S.B.M.1
  • 65
    • 84962292317 scopus 로고    scopus 로고
    • A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy
    • Munder, M.C., et al. A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy. Elife 5 (2016), 1–30.
    • (2016) Elife , vol.5 , pp. 1-30
    • Munder, M.C.1
  • 66
    • 84930353020 scopus 로고    scopus 로고
    • The protein quality control machinery regulates its misassembled proteasome subunits
    • Peters, L.Z., et al. The protein quality control machinery regulates its misassembled proteasome subunits. PLoS Genet., 11, 2015, e1005178.
    • (2015) PLoS Genet. , vol.11 , pp. e1005178
    • Peters, L.Z.1
  • 67
    • 67649875630 scopus 로고    scopus 로고
    • Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation
    • Narayanaswamy, R., et al. Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 10147–10152.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10147-10152
    • Narayanaswamy, R.1
  • 68
    • 84899657388 scopus 로고    scopus 로고
    • Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation
    • Petrovska, I., et al. Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation. Elife, 25, 2014, 10.7554/eLife.02409.
    • (2014) Elife , vol.25
    • Petrovska, I.1
  • 69
    • 84986247611 scopus 로고    scopus 로고
    • Polar positioning of phase-separated liquid compartments in cells regulated by an mRNA competition mechanism
    • Saha, S., et al. Polar positioning of phase-separated liquid compartments in cells regulated by an mRNA competition mechanism. Cell 166 (2016), 1–13.
    • (2016) Cell , vol.166 , pp. 1-13
    • Saha, S.1
  • 70
    • 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 (2015), 641–646.
    • (2015) Curr. Biol. , vol.25 , pp. 641-646
    • Weber, S.C.1    Brangwynne, C.P.2
  • 71
    • 85011088235 scopus 로고    scopus 로고
    • The synaptonemal complex has liquid crystalline properties and spatially regulates meiotic recombination factors
    • Rog, O., et al. The synaptonemal complex has liquid crystalline properties and spatially regulates meiotic recombination factors. Elife 6 (2017), 1–26.
    • (2017) Elife , vol.6 , pp. 1-26
    • Rog, O.1
  • 72
    • 84986185216 scopus 로고    scopus 로고
    • Distinct stages in stress granule assembly and disassembly
    • Wheeler, J.R., et al. Distinct stages in stress granule assembly and disassembly. Elife, 5, 2016, e18413.
    • (2016) Elife , vol.5 , pp. e18413
    • Wheeler, J.R.1
  • 73
    • 84863393644 scopus 로고    scopus 로고
    • Smaug1 mRNA-silencing foci respond to NMDA and modulate synapse formation
    • Baez, M.V., et al. Smaug1 mRNA-silencing foci respond to NMDA and modulate synapse formation. J. Cell Biol. 195 (2011), 1141–1157.
    • (2011) J. Cell Biol. , vol.195 , pp. 1141-1157
    • Baez, M.V.1
  • 74
    • 84876881246 scopus 로고    scopus 로고
    • Synaptic activity regulated mRNA-silencing foci for the fine tuning of local protein synthesis at the synapse
    • Pascual, M.L., et al. Synaptic activity regulated mRNA-silencing foci for the fine tuning of local protein synthesis at the synapse. Commun. Integr. Biol. 5 (2012), 388–392.
    • (2012) Commun. Integr. Biol. , vol.5 , pp. 388-392
    • Pascual, M.L.1
  • 75
    • 84928550463 scopus 로고    scopus 로고
    • Synaptic control of mRNA translation by reversible assembly of XRN1 bodies
    • Luchelli, L., et al. Synaptic control of mRNA translation by reversible assembly of XRN1 bodies. J. Cell Sci. 128 (2015), 1542–1554.
    • (2015) J. Cell Sci. , vol.128 , pp. 1542-1554
    • Luchelli, L.1
  • 76
    • 84890061807 scopus 로고    scopus 로고
    • A super-assembly of Whi3 encodes memory of deceptive encounters by single cells during yeast courtship
    • Caudron, F., Barral, Y., A super-assembly of Whi3 encodes memory of deceptive encounters by single cells during yeast courtship. Cell 155 (2013), 1244–1257.
    • (2013) Cell , vol.155 , pp. 1244-1257
    • Caudron, F.1    Barral, Y.2
  • 77
    • 84958730297 scopus 로고    scopus 로고
    • Dynamic sumoylation of a conserved transcription corepressor prevents persistent inclusion formation during hyperosmotic stress
    • Oeser, M.L., et al. Dynamic sumoylation of a conserved transcription corepressor prevents persistent inclusion formation during hyperosmotic stress. PLoS Genet., 12, 2016, e1005809.
    • (2016) PLoS Genet. , vol.12 , pp. e1005809
    • Oeser, M.L.1
  • 78
    • 84931574130 scopus 로고    scopus 로고
    • The persistence of hippocampal-based memory requires protein synthesis mediated by the prion-like protein CPEB3
    • Fioriti, L., et al. The persistence of hippocampal-based memory requires protein synthesis mediated by the prion-like protein CPEB3. Neuron 86 (2015), 1433–1448.
    • (2015) Neuron , vol.86 , pp. 1433-1448
    • Fioriti, L.1
  • 79
    • 84937630419 scopus 로고    scopus 로고
    • SUMOylation is an inhibitory constraint that regulates the prion-like aggregation and activity of CPEB3
    • Drisaldi, B., et al. SUMOylation is an inhibitory constraint that regulates the prion-like aggregation and activity of CPEB3. Cell Rep. 11 (2015), 1694–1702.
    • (2015) Cell Rep. , vol.11 , pp. 1694-1702
    • Drisaldi, B.1
  • 80
    • 84959268188 scopus 로고    scopus 로고
    • Prions and protein assemblies that convey biological information in health and disease
    • Sanders, D.W., et al. Prions and protein assemblies that convey biological information in health and disease. Neuron 89 (2016), 433–448.
    • (2016) Neuron , vol.89 , pp. 433-448
    • Sanders, D.W.1
  • 81
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter, J., Lindquist, S., Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genet. 6 (2005), 435–450.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 82
    • 84990841704 scopus 로고    scopus 로고
    • Intrinsically disordered proteins drive emergence and inheritance of biological traits
    • e12
    • Chakrabortee, S., et al. Intrinsically disordered proteins drive emergence and inheritance of biological traits. Cell 167 (2016), 369–381 e12.
    • (2016) Cell , vol.167 , pp. 369-381
    • Chakrabortee, S.1
  • 83
    • 78650644709 scopus 로고    scopus 로고
    • Hsp90 and environmental stress transform the adaptive value of natural genetic variation
    • Jarosz, D.F., Lindquist, S., Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 330 (2010), 1820–1824.
    • (2010) Science , vol.330 , pp. 1820-1824
    • Jarosz, D.F.1    Lindquist, S.2
  • 84
    • 85016462611 scopus 로고    scopus 로고
    • Exosome secretion affects social motility in Trypanosoma brucei
    • Eliaz, D., et al. Exosome secretion affects social motility in Trypanosoma brucei. PLoS Pathog., 13, 2017, e1006245.
    • (2017) PLoS Pathog. , vol.13 , pp. e1006245
    • Eliaz, D.1
  • 85
    • 84890408539 scopus 로고    scopus 로고
    • Exosomes: a novel pathway of local and distant intercellular communication that facilitates the growth and metastasis of neoplastic lesions
    • Zhang, H.G., Grizzle, W.E., Exosomes: a novel pathway of local and distant intercellular communication that facilitates the growth and metastasis of neoplastic lesions. Am. J. Pathol. 184 (2014), 28–41.
    • (2014) Am. J. Pathol. , vol.184 , pp. 28-41
    • Zhang, H.G.1    Grizzle, W.E.2
  • 86
    • 84979581124 scopus 로고    scopus 로고
    • Amyloid-like self-assembly of a cellular compartment
    • Boke, E., et al. Amyloid-like self-assembly of a cellular compartment. Cell 166 (2016), 637–650.
    • (2016) Cell , vol.166 , pp. 637-650
    • Boke, E.1
  • 87
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis
    • Ling, S.-C., et al. Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 79 (2013), 416–438.
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.-C.1
  • 88
    • 85015326326 scopus 로고    scopus 로고
    • Tardigrades use intrinsically disordered proteins to survive desiccation
    • Boothby, T., et al. Tardigrades use intrinsically disordered proteins to survive desiccation. Mol. Cell 65 (2017), 975–984.
    • (2017) Mol. Cell , vol.65 , pp. 975-984
    • Boothby, T.1
  • 89
    • 84940403835 scopus 로고    scopus 로고
    • A liquid-to-solid phase transition of the ALS Protein FUS accelerated by disease mutation
    • Patel, A., et al. A liquid-to-solid phase transition of the ALS Protein FUS accelerated by disease mutation. Cell 162 (2015), 1066–1077.
    • (2015) Cell , vol.162 , pp. 1066-1077
    • Patel, A.1
  • 90
    • 85017348777 scopus 로고    scopus 로고
    • An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function
    • Mateju, D., et al. An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. EMBO J. 36 (2017), 1669–1687.
    • (2017) EMBO J. , vol.36 , pp. 1669-1687
    • Mateju, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.