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Volumn 156, Issue 1-2, 2014, Pages 146-157

Inefficient SRP interaction with a nascent chain triggers a MRNA quality control pathway

Author keywords

[No Author keywords available]

Indexed keywords

ARGONAUTE 2 PROTEIN; MESSENGER RNA; SECRETORY PROTEIN; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE;

EID: 84892768018     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2013.12.017     Document Type: Article
Times cited : (76)

References (67)
  • 1
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • V. Albanèse, A.Y. Yam, J. Baughman, C. Parnot, and J. Frydman Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells Cell 124 2006 75 88
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanèse, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 2
    • 2542452829 scopus 로고    scopus 로고
    • Cotranslational membrane protein biogenesis at the endoplasmic reticulum
    • N.N. Alder, and A.E. Johnson Cotranslational membrane protein biogenesis at the endoplasmic reticulum J. Biol. Chem. 279 2004 22787 22790
    • (2004) J. Biol. Chem. , vol.279 , pp. 22787-22790
    • Alder, N.N.1    Johnson, A.E.2
  • 4
    • 0024523481 scopus 로고
    • Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor
    • D.W. Andrews, L. Lauffer, P. Walter, and V.R. Lingappa Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor J. Cell Biol. 108 1989 797 810
    • (1989) J. Cell Biol. , vol.108 , pp. 797-810
    • Andrews, D.W.1    Lauffer, L.2    Walter, P.3    Lingappa, V.R.4
  • 5
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • J.L. Brodsky Cleaning up: ER-associated degradation to the rescue Cell 151 2012 1163 1167
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 6
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • A. Buchberger, B. Bukau, and T. Sommer Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms Mol. Cell 40 2010 238 252
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 8
    • 78650306521 scopus 로고    scopus 로고
    • Small RNA sorting: Matchmaking for Argonautes
    • B. Czech, and G.J. Hannon Small RNA sorting: matchmaking for Argonautes Nat. Rev. Genet. 12 2011 19 31
    • (2011) Nat. Rev. Genet. , vol.12 , pp. 19-31
    • Czech, B.1    Hannon, G.J.2
  • 9
    • 79551627496 scopus 로고    scopus 로고
    • A parsimonious model for gene regulation by miRNAs
    • S. Djuranovic, A. Nahvi, and R. Green A parsimonious model for gene regulation by miRNAs Science 331 2011 550 553
    • (2011) Science , vol.331 , pp. 550-553
    • Djuranovic, S.1    Nahvi, A.2    Green, R.3
  • 10
    • 36049041612 scopus 로고    scopus 로고
    • RNA quality control in eukaryotes
    • M.K. Doma, and R. Parker RNA quality control in eukaryotes Cell 131 2007 660 668
    • (2007) Cell , vol.131 , pp. 660-668
    • Doma, M.K.1    Parker, R.2
  • 11
    • 17044419154 scopus 로고    scopus 로고
    • Targeting proteins to membranes: Structure of the signal recognition particle
    • P.F. Egea, R.M. Stroud, and P. Walter Targeting proteins to membranes: structure of the signal recognition particle Curr. Opin. Struct. Biol. 15 2005 213 220
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 213-220
    • Egea, P.F.1    Stroud, R.M.2    Walter, P.3
  • 12
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • L. Ellgaard, and A. Helenius Quality control in the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 4 2003 181 191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 13
    • 77953629046 scopus 로고    scopus 로고
    • Regulation of mRNA translation and stability by microRNAs
    • M.R. Fabian, N. Sonenberg, and W. Filipowicz Regulation of mRNA translation and stability by microRNAs Annu. Rev. Biochem. 79 2010 351 379
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 351-379
    • Fabian, M.R.1    Sonenberg, N.2    Filipowicz, W.3
  • 14
    • 38349169664 scopus 로고    scopus 로고
    • Mechanisms of post-transcriptional regulation by microRNAs: Are the answers in sight?
    • W. Filipowicz, S.N. Bhattacharyya, and N. Sonenberg Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight? Nat. Rev. Genet. 9 2008 102 114
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 102-114
    • Filipowicz, W.1    Bhattacharyya, S.N.2    Sonenberg, N.3
  • 16
    • 0035839109 scopus 로고    scopus 로고
    • Argonaute2, a link between genetic and biochemical analyses of RNAi
    • S.M. Hammond, S. Boettcher, A.A. Caudy, R. Kobayashi, and G.J. Hannon Argonaute2, a link between genetic and biochemical analyses of RNAi Science 293 2001 1146 1150
    • (2001) Science , vol.293 , pp. 1146-1150
    • Hammond, S.M.1    Boettcher, S.2    Caudy, A.A.3    Kobayashi, R.4    Hannon, G.J.5
  • 17
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 18
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • J. Hollien, and J.S. Weissman Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response Science 313 2006 104 107
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 20
    • 37549014207 scopus 로고    scopus 로고
    • Argonaute proteins: Key players in RNA silencing
    • G. Hutvagner, and M.J. Simard Argonaute proteins: key players in RNA silencing Nat. Rev. Mol. Cell Biol. 9 2008 22 32
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 22-32
    • Hutvagner, G.1    Simard, M.J.2
  • 21
    • 0036791671 scopus 로고    scopus 로고
    • A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins
    • A. Ishizuka, M.C. Siomi, and H. Siomi A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins Genes Dev. 16 2002 2497 2508
    • (2002) Genes Dev. , vol.16 , pp. 2497-2508
    • Ishizuka, A.1    Siomi, M.C.2    Siomi, H.3
  • 22
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • R.R. Kopito Aggresomes, inclusion bodies and protein aggregation Trends Cell Biol. 10 2000 524 530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 23
    • 0005614190 scopus 로고
    • Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • U.C. Krieg, P. Walter, and A.E. Johnson Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle Proc. Natl. Acad. Sci. USA 83 1986 8604 8608
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3
  • 24
    • 33846651215 scopus 로고    scopus 로고
    • Inefficient targeting to the endoplasmic reticulum by the signal recognition particle elicits selective defects in post-ER membrane trafficking
    • A.K. Lakkaraju, P.P. Luyet, P. Parone, T. Falguières, and K. Strub Inefficient targeting to the endoplasmic reticulum by the signal recognition particle elicits selective defects in post-ER membrane trafficking Exp. Cell Res. 313 2007 834 847
    • (2007) Exp. Cell Res. , vol.313 , pp. 834-847
    • Lakkaraju, A.K.1    Luyet, P.P.2    Parone, P.3    Falguières, T.4    Strub, K.5
  • 27
    • 0037031576 scopus 로고    scopus 로고
    • Single-stranded antisense siRNAs guide target RNA cleavage in RNAi
    • J. Martinez, A. Patkaniowska, H. Urlaub, R. Lührmann, and T. Tuschl Single-stranded antisense siRNAs guide target RNA cleavage in RNAi Cell 110 2002 563 574
    • (2002) Cell , vol.110 , pp. 563-574
    • Martinez, J.1    Patkaniowska, A.2    Urlaub, H.3    Lührmann, R.4    Tuschl, T.5
  • 28
    • 0141992130 scopus 로고    scopus 로고
    • Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins
    • P.J. McCormick, Y. Miao, Y. Shao, J. Lin, and A.E. Johnson Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins Mol. Cell 12 2003 329 341
    • (2003) Mol. Cell , vol.12 , pp. 329-341
    • McCormick, P.J.1    Miao, Y.2    Shao, Y.3    Lin, J.4    Johnson, A.E.5
  • 29
    • 84879414849 scopus 로고    scopus 로고
    • Argonaute proteins: Functional insights and emerging roles
    • G. Meister Argonaute proteins: functional insights and emerging roles Nat. Rev. Genet. 14 2013 447 459
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 447-459
    • Meister, G.1
  • 31
    • 84860388943 scopus 로고    scopus 로고
    • RNAi-independent role for Argonaute2 in CTCF/CP190 chromatin insulator function
    • N. Moshkovich, P. Nisha, P.J. Boyle, B.A. Thompson, R.K. Dale, and E.P. Lei RNAi-independent role for Argonaute2 in CTCF/CP190 chromatin insulator function Genes Dev. 25 2011 1686 1701
    • (2011) Genes Dev. , vol.25 , pp. 1686-1701
    • Moshkovich, N.1    Nisha, P.2    Boyle, P.J.3    Thompson, B.A.4    Dale, R.K.5    Lei, E.P.6
  • 32
    • 1242296375 scopus 로고    scopus 로고
    • MiRNP:mRNA association in polyribosomes in a human neuronal cell line
    • P.T. Nelson, A.G. Hatzigeorgiou, and Z. Mourelatos miRNP:mRNA association in polyribosomes in a human neuronal cell line RNA 10 2004 387 394
    • (2004) RNA , vol.10 , pp. 387-394
    • Nelson, P.T.1    Hatzigeorgiou, A.G.2    Mourelatos, Z.3
  • 34
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • S. Pechmann, F. Willmund, and J. Frydman The ribosome as a hub for protein quality control Mol. Cell 49 2013 411 421
    • (2013) Mol. Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 35
    • 84871922444 scopus 로고    scopus 로고
    • MicroRNA-independent recruitment of Argonaute 1 to nanos mRNA through the Smaug RNA-binding protein
    • B.D. Pinder, and C.A. Smibert microRNA-independent recruitment of Argonaute 1 to nanos mRNA through the Smaug RNA-binding protein EMBO Rep. 14 2013 80 86
    • (2013) EMBO Rep. , vol.14 , pp. 80-86
    • Pinder, B.D.1    Smibert, C.A.2
  • 36
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 37
    • 34247281027 scopus 로고    scopus 로고
    • Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence
    • U. Raue, S. Oellerer, and S. Rospert Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence J. Biol. Chem. 282 2007 7809 7816
    • (2007) J. Biol. Chem. , vol.282 , pp. 7809-7816
    • Raue, U.1    Oellerer, S.2    Rospert, S.3
  • 39
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • M. Schröder, and R.J. Kaufman The mammalian unfolded protein response Annu. Rev. Biochem. 74 2005 739 789
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 40
    • 84861841297 scopus 로고    scopus 로고
    • Translation drives mRNA quality control
    • C.J. Shoemaker, and R. Green Translation drives mRNA quality control Nat. Struct. Mol. Biol. 19 2012 594 601
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 594-601
    • Shoemaker, C.J.1    Green, R.2
  • 41
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • M.H. Smith, H.L. Ploegh, and J.S. Weissman Road to ruin: targeting proteins for degradation in the endoplasmic reticulum Science 334 2011 1086 1090
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 42
    • 4444302947 scopus 로고    scopus 로고
    • Crystal structure of Argonaute and its implications for RISC slicer activity
    • J.J. Song, S.K. Smith, G.J. Hannon, and L. Joshua-Tor Crystal structure of Argonaute and its implications for RISC slicer activity Science 305 2004 1434 1437
    • (2004) Science , vol.305 , pp. 1434-1437
    • Song, J.J.1    Smith, S.K.2    Hannon, G.J.3    Joshua-Tor, L.4
  • 43
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81 2003 678 699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 45
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • G. von Heijne Patterns of amino acids near signal-sequence cleavage sites Eur. J. Biochem. 133 1983 17 21
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 46
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • P. Walter, and D. Ron The unfolded protein response: from stress pathway to homeostatic regulation Science 334 2011 1081 1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 47
    • 0019849075 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein
    • P. Walter, I. Ibrahimi, and G. Blobel Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein J. Cell Biol. 91 1981 545 550
    • (1981) J. Cell Biol. , vol.91 , pp. 545-550
    • Walter, P.1    Ibrahimi, I.2    Blobel, G.3
  • 48
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • C.L. Ward, S. Omura, and R.R. Kopito Degradation of CFTR by the ubiquitin-proteasome pathway Cell 83 1995 121 127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 52
    • 78649874963 scopus 로고    scopus 로고
    • Involvement of argonaute proteins in gene silencing and activation by RNAs complementary to a non-coding transcript at the progesterone receptor promoter
    • Y. Chu, X. Yue, S.T. Younger, B.A. Janowski, and D.R. Corey Involvement of argonaute proteins in gene silencing and activation by RNAs complementary to a non-coding transcript at the progesterone receptor promoter Nucleic Acids Res. 38 2010 7736 7748
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7736-7748
    • Chu, Y.1    Yue, X.2    Younger, S.T.3    Janowski, B.A.4    Corey, D.R.5
  • 53
    • 1042300232 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation in the analysis of large chromatin domains across murine antigen receptor loci
    • D.N. Ciccone, K.B. Morshead, and M.A. Oettinger Chromatin immunoprecipitation in the analysis of large chromatin domains across murine antigen receptor loci Methods Enzymol. 376 2004 334 348
    • (2004) Methods Enzymol. , vol.376 , pp. 334-348
    • Ciccone, D.N.1    Morshead, K.B.2    Oettinger, M.A.3
  • 54
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • H. Do, D. Falcone, J. Lin, D.W. Andrews, and A.E. Johnson The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process Cell 85 1996 369 378
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 55
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • A.H. Erickson, and G. Blobel Cell-free translation of messenger RNA in a wheat germ system Methods Enzymol. 96 1983 38 50
    • (1983) Methods Enzymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 56
    • 23044445800 scopus 로고    scopus 로고
    • The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking
    • S.A. Etchells, A.S. Meyer, A.Y. Yam, A. Roobol, Y. Miao, Y. Shao, M.J. Carden, W.R. Skach, J. Frydman, and A.E. Johnson The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking J. Biol. Chem. 280 2005 28118 28126
    • (2005) J. Biol. Chem. , vol.280 , pp. 28118-28126
    • Etchells, S.A.1    Meyer, A.S.2    Yam, A.Y.3    Roobol, A.4    Miao, Y.5    Shao, Y.6    Carden, M.J.7    Skach, W.R.8    Frydman, J.9    Johnson, A.E.10
  • 57
    • 0038719738 scopus 로고    scopus 로고
    • Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens
    • J.J. Flanagan, J.C. Chen, Y. Miao, Y. Shao, J. Lin, P.E. Bock, and A.E. Johnson Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens J. Biol. Chem. 278 2003 18628 18637
    • (2003) J. Biol. Chem. , vol.278 , pp. 18628-18637
    • Flanagan, J.J.1    Chen, J.C.2    Miao, Y.3    Shao, Y.4    Lin, J.5    Bock, P.E.6    Johnson, A.E.7
  • 58
    • 65849109465 scopus 로고    scopus 로고
    • Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones
    • T. Kaneko, J. Hamazaki, S. Iemura, K. Sasaki, K. Furuyama, T. Natsume, K. Tanaka, and S. Murata Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones Cell 137 2009 914 925
    • (2009) Cell , vol.137 , pp. 914-925
    • Kaneko, T.1    Hamazaki, J.2    Iemura, S.3    Sasaki, K.4    Furuyama, K.5    Natsume, T.6    Tanaka, K.7    Murata, S.8
  • 59
    • 0037806033 scopus 로고    scopus 로고
    • Developmentally programmed gene elimination in Euplotes crassus facilitates a switch in the telomerase catalytic subunit
    • Z. Karamysheva, L. Wang, T. Shrode, J. Bednenko, L.A. Hurley, and D.E. Shippen Developmentally programmed gene elimination in Euplotes crassus facilitates a switch in the telomerase catalytic subunit Cell 113 2003 565 576
    • (2003) Cell , vol.113 , pp. 565-576
    • Karamysheva, Z.1    Wang, L.2    Shrode, T.3    Bednenko, J.4    Hurley, L.A.5    Shippen, D.E.6
  • 60
    • 34247593034 scopus 로고    scopus 로고
    • Impaired microRNA processing enhances cellular transformation and tumorigenesis
    • M.S. Kumar, J. Lu, K.L. Mercer, T.R. Golub, and T. Jacks Impaired microRNA processing enhances cellular transformation and tumorigenesis Nat. Genet. 39 2007 673 677
    • (2007) Nat. Genet. , vol.39 , pp. 673-677
    • Kumar, M.S.1    Lu, J.2    Mercer, K.L.3    Golub, T.R.4    Jacks, T.5
  • 61
    • 34247565615 scopus 로고    scopus 로고
    • The tumor suppressor microRNA let-7 represses the HMGA2 oncogene
    • Y.S. Lee, and A. Dutta The tumor suppressor microRNA let-7 represses the HMGA2 oncogene Genes Dev. 21 2007 1025 1030
    • (2007) Genes Dev. , vol.21 , pp. 1025-1030
    • Lee, Y.S.1    Dutta, A.2
  • 62
    • 6344275146 scopus 로고    scopus 로고
    • Differential regulation of the TRAIL death receptors DR4 and DR5 by the signal recognition particle
    • Y.G. Ren, K.W. Wagner, D.A. Knee, P. Aza-Blanc, M. Nasoff, and Q.L. Deveraux Differential regulation of the TRAIL death receptors DR4 and DR5 by the signal recognition particle Mol. Biol. Cell 15 2004 5064 5074
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5064-5074
    • Ren, Y.G.1    Wagner, K.W.2    Knee, D.A.3    Aza-Blanc, P.4    Nasoff, M.5    Deveraux, Q.L.6
  • 63
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • T.D. Schmittgen, and K.J. Livak Analyzing real-time PCR data by the comparative C(T) method Nat. Protoc. 3 2008 1101 1108
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 64
    • 80053540457 scopus 로고    scopus 로고
    • A screen to identify cellular modulators of soluble levels of an amyotrophic lateral sclerosis (ALS)-causing mutant SOD1
    • B.R. Somalinga, G.A. Miller, H.T. Malik, W.C. Wigley, and P.J. Thomas A screen to identify cellular modulators of soluble levels of an amyotrophic lateral sclerosis (ALS)-causing mutant SOD1 J. Biomol. Screen. 16 2011 974 985
    • (2011) J. Biomol. Screen. , vol.16 , pp. 974-985
    • Somalinga, B.R.1    Miller, G.A.2    Malik, H.T.3    Wigley, W.C.4    Thomas, P.J.5
  • 65
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • P. Walter, and G. Blobel Preparation of microsomal membranes for cotranslational protein translocation Methods Enzymol. 96 1983 84 93
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 66
    • 0021010426 scopus 로고
    • Signal recognition particle: A ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties
    • P. Walter, and G. Blobel Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties Methods Enzymol. 96 1983 682 691
    • (1983) Methods Enzymol. , vol.96 , pp. 682-691
    • Walter, P.1    Blobel, G.2
  • 67
    • 82655189968 scopus 로고    scopus 로고
    • Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1
    • Z.C. Zhang, N. Satterly, B.M. Fontoura, and Y.M. Chook Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1 Mol. Biol. Cell 22 2011 4657 4668
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4657-4668
    • Zhang, Z.C.1    Satterly, N.2    Fontoura, B.M.3    Chook, Y.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.