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Volumn 153, Issue 7, 2013, Pages 1461-

XEukaryotic stress granules are cleared by autophagy and Cdc48/VCP function

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 48; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN;

EID: 84879349589     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2013.05.037     Document Type: Article
Times cited : (556)

References (72)
  • 2
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-transcriptional and epigenetic modulators of gene expression
    • P. Anderson, and N. Kedersha RNA granules: post-transcriptional and epigenetic modulators of gene expression Nat. Rev. Mol. Cell Biol. 10 2009 430 436
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 3
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • K. Arimoto, H. Fukuda, S. Imajoh-Ohmi, H. Saito, and M. Takekawa Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways Nat. Cell Biol. 10 2008 1324 1332
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 5
    • 41849103099 scopus 로고    scopus 로고
    • P bodies, stress granules, and viral life cycles
    • C.J. Beckham, and R. Parker P bodies, stress granules, and viral life cycles Cell Host Microbe 3 2008 206 212
    • (2008) Cell Host Microbe , vol.3 , pp. 206-212
    • Beckham, C.J.1    Parker, R.2
  • 7
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • M. Brengues, D. Teixeira, and R. Parker Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies Science 310 2005 486 489
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 8
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • J.R. Buchan, and R. Parker Eukaryotic stress granules: the ins and outs of translation Mol. Cell 36 2009 932 941
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 9
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • J.R. Buchan, D. Muhlrad, and R. Parker P bodies promote stress granule assembly in Saccharomyces cerevisiae J. Cell Biol. 183 2008 441 455
    • (2008) J. Cell Biol. , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 11
    • 84873838455 scopus 로고    scopus 로고
    • Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase
    • 10.1002/cmdc.201200520
    • T.F. Chou, K. Li, K.J. Frankowski, F.J. Schoenen, and R.J. Deshaies Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase ChemMedChem 8 2013 297 312 10.1002/cmdc.201200520
    • (2013) ChemMedChem , vol.8 , pp. 297-312
    • Chou, T.F.1    Li, K.2    Frankowski, K.J.3    Schoenen, F.J.4    Deshaies, R.J.5
  • 12
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • C.J. Decker, D. Teixeira, and R. Parker Edc3p and a glutamine/asparagine- rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae J. Cell Biol. 179 2007 437 449
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 13
    • 84862128438 scopus 로고    scopus 로고
    • TDP-43 aggregation in neurodegeneration: Are stress granules the key?
    • C.M. Dewey, B. Cenik, C.F. Sephton, B.A. Johnson, J. Herz, and G. Yu TDP-43 aggregation in neurodegeneration: are stress granules the key? Brain Res. 1462 2012 16 25
    • (2012) Brain Res. , vol.1462 , pp. 16-25
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Johnson, B.A.4    Herz, J.5    Yu, G.6
  • 14
    • 63049130206 scopus 로고    scopus 로고
    • Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly
    • M.C. Didiot, M. Subramanian, E. Flatter, J.L. Mandel, and H. Moine Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly Mol. Biol. Cell 20 2009 428 437
    • (2009) Mol. Biol. Cell , vol.20 , pp. 428-437
    • Didiot, M.C.1    Subramanian, M.2    Flatter, E.3    Mandel, J.L.4    Moine, H.5
  • 15
    • 80052235798 scopus 로고    scopus 로고
    • Mechanisms of dendritic mRNA transport and its role in synaptic tagging
    • M. Doyle, and M.A. Kiebler Mechanisms of dendritic mRNA transport and its role in synaptic tagging EMBO J. 30 2011 3540 3552
    • (2011) EMBO J. , vol.30 , pp. 3540-3552
    • Doyle, M.1    Kiebler, M.A.2
  • 16
    • 79551530753 scopus 로고    scopus 로고
    • Cytoplasmic mRNP granules at a glance
    • S.L. Erickson, and J. Lykke-Andersen Cytoplasmic mRNP granules at a glance J. Cell Sci. 124 2011 293 297
    • (2011) J. Cell Sci. , vol.124 , pp. 293-297
    • Erickson, S.L.1    Lykke-Andersen, J.2
  • 17
    • 78649949096 scopus 로고    scopus 로고
    • Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense-mediated mRNA decay
    • T.M. Franks, G. Singh, and J. Lykke-Andersen Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense-mediated mRNA decay Cell 143 2010 938 950
    • (2010) Cell , vol.143 , pp. 938-950
    • Franks, T.M.1    Singh, G.2    Lykke-Andersen, J.3
  • 18
    • 69949117622 scopus 로고    scopus 로고
    • Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity
    • D.J. Gibbings, C. Ciaudo, M. Erhardt, and O. Voinnet Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity Nat. Cell Biol. 11 2009 1143 1149
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1143-1149
    • Gibbings, D.J.1    Ciaudo, C.2    Erhardt, M.3    Voinnet, O.4
  • 22
    • 77957768017 scopus 로고    scopus 로고
    • Translational control mechanisms in long-lasting synaptic plasticity and memory
    • C. Gkogkas, N. Sonenberg, and M. Costa-Mattioli Translational control mechanisms in long-lasting synaptic plasticity and memory J. Biol. Chem. 285 2010 31913 31917
    • (2010) J. Biol. Chem. , vol.285 , pp. 31913-31917
    • Gkogkas, C.1    Sonenberg, N.2    Costa-Mattioli, M.3
  • 23
    • 82955198538 scopus 로고    scopus 로고
    • Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS
    • D. Ito, and N. Suzuki Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS Neurology 77 2011 1636 1643
    • (2011) Neurology , vol.77 , pp. 1636-1643
    • Ito, D.1    Suzuki, N.2
  • 25
    • 57649198447 scopus 로고    scopus 로고
    • Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease
    • J.S. Ju, S.E. Miller, P.I. Hanson, and C.C. Weihl Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease J. Biol. Chem. 283 2008 30289 30299
    • (2008) J. Biol. Chem. , vol.283 , pp. 30289-30299
    • Ju, J.S.1    Miller, S.E.2    Hanson, P.I.3    Weihl, C.C.4
  • 26
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • M. Kato, T.W. Han, S. Xie, K. Shi, X. Du, L.C. Wu, H. Mirzaei, E.J. Goldsmith, J. Longgood, and J. Pei Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels Cell 149 2012 753 767
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5    Wu, L.C.6    Mirzaei, H.7    Goldsmith, E.J.8    Longgood, J.9    Pei, J.10
  • 27
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • N. Kedersha, and P. Anderson Mammalian stress granules and processing bodies Methods Enzymol. 431 2007 61 81
    • (2007) Methods Enzymol. , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 28
    • 84876070458 scopus 로고    scopus 로고
    • VCP Is Essential for Mitochondrial Quality Control by PINK1/Parkin and this Function Is Impaired by VCP Mutations
    • 10.1016/j.neuron.2013.02.029
    • N.C. Kim, E. Tresse, R.M. Kolaitis, A. Molliex, R.E. Thomas, N.H. Alami, B. Wang, A. Joshi, R.B. Smith, and G.P. Ritson VCP Is Essential for Mitochondrial Quality Control by PINK1/Parkin and this Function Is Impaired by VCP Mutations Neuron 78 2013 65 80 10.1016/j.neuron.2013.02.029
    • (2013) Neuron , vol.78 , pp. 65-80
    • Kim, N.C.1    Tresse, E.2    Kolaitis, R.M.3    Molliex, A.4    Thomas, R.E.5    Alami, N.H.6    Wang, B.7    Joshi, A.8    Smith, R.B.9    Ritson, G.P.10
  • 29
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • D.J. Klionsky, Z. Elazar, P.O. Seglen, and D.C. Rubinsztein Does bafilomycin A1 block the fusion of autophagosomes with lysosomes? Autophagy 4 2008 849 950
    • (2008) Autophagy , vol.4 , pp. 849-950
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4
  • 31
    • 37449030154 scopus 로고    scopus 로고
    • The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response
    • S. Kwon, Y. Zhang, and P. Matthias The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response Genes Dev. 21 2007 3381 3394
    • (2007) Genes Dev. , vol.21 , pp. 3381-3394
    • Kwon, S.1    Zhang, Y.2    Matthias, P.3
  • 32
    • 33845295461 scopus 로고    scopus 로고
    • Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules
    • A.K. Leung, J.M. Calabrese, and P.A. Sharp Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules Proc. Natl. Acad. Sci. USA 103 2006 18125 18130
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18125-18130
    • Leung, A.K.1    Calabrese, J.M.2    Sharp, P.A.3
  • 33
    • 70450285065 scopus 로고    scopus 로고
    • Dynein and kinesin regulate stress-granule and P-body dynamics
    • M. Loschi, C.C. Leishman, N. Berardone, and G.L. Boccaccio Dynein and kinesin regulate stress-granule and P-body dynamics J. Cell Sci. 122 2009 3973 3982
    • (2009) J. Cell Sci. , vol.122 , pp. 3973-3982
    • Loschi, M.1    Leishman, C.C.2    Berardone, N.3    Boccaccio, G.L.4
  • 34
    • 34347406608 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system induces stress granule formation
    • R. Mazroui, S. Di Marco, R.J. Kaufman, and I.E. Gallouzi Inhibition of the ubiquitin-proteasome system induces stress granule formation Mol. Biol. Cell 18 2007 2603 2618
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2603-2618
    • Mazroui, R.1    Di Marco, S.2    Kaufman, R.J.3    Gallouzi, I.E.4
  • 35
    • 84865257040 scopus 로고    scopus 로고
    • Principles and roles of mRNA localization in animal development
    • C. Medioni, K. Mowry, and F. Besse Principles and roles of mRNA localization in animal development Development 139 2012 3263 3276
    • (2012) Development , vol.139 , pp. 3263-3276
    • Medioni, C.1    Mowry, K.2    Besse, F.3
  • 36
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • H. Meyer, M. Bug, and S. Bremer Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system Nat. Cell Biol. 14 2012 117 123
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 37
    • 79957916809 scopus 로고    scopus 로고
    • V-ATPase engagement in autophagic processes
    • D. Mijaljica, M. Prescott, and R.J. Devenish V-ATPase engagement in autophagic processes Autophagy 7 2011 666 668
    • (2011) Autophagy , vol.7 , pp. 666-668
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 43
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • R. Parker, and U. Sheth P bodies and the control of mRNA translation and degradation Mol. Cell 25 2007 635 646
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 44
    • 43949088191 scopus 로고    scopus 로고
    • Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo
    • F. Peri, and C. Nüsslein-Volhard Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo Cell 133 2008 916 927
    • (2008) Cell , vol.133 , pp. 916-927
    • Peri, F.1    Nüsslein-Volhard, C.2
  • 45
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • C. Peters, M.J. Bayer, S. Bühler, J.S. Andersen, M. Mann, and A. Mayer Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion Nature 409 2001 581 588
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Bühler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 46
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • M.A. Reijns, R.D. Alexander, M.P. Spiller, and J.D. Beggs A role for Q/N-rich aggregation-prone regions in P-body localization J. Cell Sci. 121 2008 2463 2472
    • (2008) J. Cell Sci. , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 48
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • U. Sheth, and R. Parker Decapping and decay of messenger RNA occur in cytoplasmic processing bodies Science 300 2003 805 808
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 49
    • 33744977432 scopus 로고    scopus 로고
    • Targeting of aberrant mRNAs to cytoplasmic processing bodies
    • U. Sheth, and R. Parker Targeting of aberrant mRNAs to cytoplasmic processing bodies Cell 125 2006 1095 1109
    • (2006) Cell , vol.125 , pp. 1095-1109
    • Sheth, U.1    Parker, R.2
  • 50
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: New features for data integration and network visualization
    • M.E. Smoot, K. Ono, J. Ruscheinski, P.L. Wang, and T. Ideker Cytoscape 2.8: new features for data integration and network visualization Bioinformatics 27 2011 431 432
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.L.4    Ideker, T.5
  • 51
    • 78649375395 scopus 로고    scopus 로고
    • Translational regulation of gene expression during conditions of cell stress
    • K.A. Spriggs, M. Bushell, and A.E. Willis Translational regulation of gene expression during conditions of cell stress Mol. Cell 40 2010 228 237
    • (2010) Mol. Cell , vol.40 , pp. 228-237
    • Spriggs, K.A.1    Bushell, M.2    Willis, A.E.3
  • 53
    • 84864308260 scopus 로고    scopus 로고
    • Transient sequestration of TORC1 into stress granules during heat stress
    • T. Takahara, and T. Maeda Transient sequestration of TORC1 into stress granules during heat stress Mol. Cell 47 2012 242 252
    • (2012) Mol. Cell , vol.47 , pp. 242-252
    • Takahara, T.1    Maeda, T.2
  • 54
    • 0035910577 scopus 로고    scopus 로고
    • Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, a putative lipase
    • S.A. Teter, K.P. Eggerton, S.V. Scott, J. Kim, A.M. Fischer, and D.J. Klionsky Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, a putative lipase J. Biol. Chem. 276 2001 2083 2087
    • (2001) J. Biol. Chem. , vol.276 , pp. 2083-2087
    • Teter, S.A.1    Eggerton, K.P.2    Scott, S.V.3    Kim, J.4    Fischer, A.M.5    Klionsky, D.J.6
  • 55
    • 0037033030 scopus 로고    scopus 로고
    • The Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways
    • C.W. Wang, P.E. Stromhaug, J. Shima, and D.J. Klionsky The Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways J. Biol. Chem. 277 2002 47917 47927
    • (2002) J. Biol. Chem. , vol.277 , pp. 47917-47927
    • Wang, C.W.1    Stromhaug, P.E.2    Shima, J.3    Klionsky, D.J.4
  • 56
    • 72649087184 scopus 로고    scopus 로고
    • Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
    • X. Wang, H. Fan, Z. Ying, B. Li, H. Wang, and G. Wang Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system Neurosci. Lett. 469 2010 112 116
    • (2010) Neurosci. Lett. , vol.469 , pp. 112-116
    • Wang, X.1    Fan, H.2    Ying, Z.3    Li, B.4    Wang, H.5    Wang, G.6
  • 57
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • I.F. Wang, B.S. Guo, Y.C. Liu, C.C. Wu, C.H. Yang, K.J. Tsai, and C.K. Shen Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43 Proc. Natl. Acad. Sci. USA 109 2012 15024 15029
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15024-15029
    • Wang, I.F.1    Guo, B.S.2    Liu, Y.C.3    Wu, C.C.4    Yang, C.H.5    Tsai, K.J.6    Shen, C.K.7
  • 58
    • 77951217000 scopus 로고    scopus 로고
    • Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class i and III phosphoinositide 3-kinase
    • Y.T. Wu, H.L. Tan, G. Shui, C. Bauvy, Q. Huang, M.R. Wenk, C.N. Ong, P. Codogno, and H.M. Shen Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase J. Biol. Chem. 285 2010 10850 10861
    • (2010) J. Biol. Chem. , vol.285 , pp. 10850-10861
    • Wu, Y.T.1    Tan, H.L.2    Shui, G.3    Bauvy, C.4    Huang, Q.5    Wenk, M.R.6    Ong, C.N.7    Codogno, P.8    Shen, H.M.9
  • 59
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • A. Yamamoto, Y. Tagawa, T. Yoshimori, Y. Moriyama, R. Masaki, and Y. Tashiro Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells Cell Struct. Funct. 23 1998 33 42
    • (1998) Cell Struct. Funct. , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 60
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • T. Yorimitsu, and D.J. Klionsky Autophagy: molecular machinery for self-eating Cell Death Differ. 12 Suppl 2 2005 1542 1552
    • (2005) Cell Death Differ. , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 61
    • 58249085224 scopus 로고    scopus 로고
    • SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans
    • Y. Zhang, L. Yan, Z. Zhou, P. Yang, E. Tian, K. Zhang, Y. Zhao, Z. Li, B. Song, and J. Han SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans Cell 136 2009 308 321
    • (2009) Cell , vol.136 , pp. 308-321
    • Zhang, Y.1    Yan, L.2    Zhou, Z.3    Yang, P.4    Tian, E.5    Zhang, K.6    Zhao, Y.7    Li, Z.8    Song, B.9    Han, J.10
  • 62
    • 77956047670 scopus 로고    scopus 로고
    • Analyzing P-bodies and stress granules in Saccharomyces cerevisiae
    • J.R. Buchan, T. Nissan, and R. Parker Analyzing P-bodies and stress granules in Saccharomyces cerevisiae Methods Enzymol. 470 2010 619 640
    • (2010) Methods Enzymol. , vol.470 , pp. 619-640
    • Buchan, J.R.1    Nissan, T.2    Parker, R.3
  • 63
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • J. Coller, and R. Parker General translational repression by activators of mRNA decapping Cell 122 2005 875 886
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 64
    • 0034804505 scopus 로고    scopus 로고
    • Yeast mRNA decapping enzyme
    • T. Dunckley, and R. Parker Yeast mRNA decapping enzyme Methods Enzymol. 342 2001 226 233
    • (2001) Methods Enzymol. , vol.342 , pp. 226-233
    • Dunckley, T.1    Parker, R.2
  • 65
    • 0029791555 scopus 로고    scopus 로고
    • Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae
    • L. Hatfield, C.A. Beelman, A. Stevens, and R. Parker Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae Mol. Cell. Biol. 16 1996 5830 5838
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5830-5838
    • Hatfield, L.1    Beelman, C.A.2    Stevens, A.3    Parker, R.4
  • 66
    • 79955370792 scopus 로고    scopus 로고
    • Cdc48 and cofactors Npl4-Ufd1 are important for G1 progression during heat stress by maintaining cell wall integrity in Saccharomyces cerevisiae
    • M.T. Hsieh, and R.H. Chen Cdc48 and cofactors Npl4-Ufd1 are important for G1 progression during heat stress by maintaining cell wall integrity in Saccharomyces cerevisiae PLoS ONE 6 2011 e18988
    • (2011) PLoS ONE , vol.6 , pp. 18988
    • Hsieh, M.T.1    Chen, R.H.2
  • 68
    • 0036901104 scopus 로고    scopus 로고
    • Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway
    • T. Shintani, W.P. Huang, P.E. Stromhaug, and D.J. Klionsky Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway Dev. Cell 3 2002 825 837
    • (2002) Dev. Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 70
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • K.D. Swisher, and R. Parker Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae PLoS ONE 5 2010 e10006
    • (2010) PLoS ONE , vol.5 , pp. 10006
    • Swisher, K.D.1    Parker, R.2
  • 71
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • E. Tresse, F.A. Salomons, J. Vesa, L.C. Bott, V. Kimonis, T.P. Yao, N.P. Dantuma, and J.P. Taylor VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD Autophagy 6 2010 217 227
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.