메뉴 건너뛰기




Volumn 11, Issue 98, 2014, Pages

Ribosome recycling induces optimal translation rate at low ribosomal availability

Author keywords

ABCE1; Ribosome recycling; Rli1; Totally asymmetric simple exclusion process; Translation

Indexed keywords

CRYSTAL LATTICES; RECYCLING; RNA; TRANSLATION (LANGUAGES);

EID: 84905053622     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2014.0589     Document Type: Article
Times cited : (30)

References (47)
  • 1
    • 46249091565 scopus 로고    scopus 로고
    • Translation factors promote the formation of two states of the closed-loop mRNP
    • doi:10.1038/nature06974
    • Amrani N, Ghosh S, Mangus DA, Jacobson A. 2008 Translation factors promote the formation of two states of the closed-loop mRNP. Nature 453, 1276-1280. (doi:10.1038/nature06974)
    • (2008) Nature , vol.453 , pp. 1276-1280
    • Amrani, N.1    Ghosh, S.2    Mangus, D.A.3    Jacobson, A.4
  • 3
    • 79952750280 scopus 로고    scopus 로고
    • Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1
    • doi:10.1073/pnas.1015953108
    • Barthelme D, Dinkelaker S, Albers S-V, Londei P, Ermler U, Tampé R. 2011 Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proc. Natl Acad. Sci. USA 108, 3228-3233. (doi:10.1073/pnas.1015953108)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 3228-3233
    • Barthelme, D.1    Dinkelaker, S.2    Albers, S.-V.3    Londei, P.4    Ermler, U.5    Tampé, R.6
  • 4
    • 84857396073 scopus 로고    scopus 로고
    • Structural basis of highly conserved ribosome recycling in eukaryotes and archaea
    • doi:10.1038/nature10829
    • Becker T et al. 2012 Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. Nature 482, 501-506. (doi:10.1038/ nature10829)
    • (2012) Nature , vol.482 , pp. 501-506
    • Becker, T.1
  • 6
    • 4744350877 scopus 로고    scopus 로고
    • The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly
    • doi:10.1074/jbc. M404502200
    • Dong J, Lai R, Nielsen K, Fekete CA, Qiu H, Hinnebusch AG. 2004 The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J. Biol. Chem. 279, 42 157-42 168. (doi:10.1074/jbc. M404502200)
    • (2004) J. Biol. Chem. , vol.279 , pp. 42157-42168
    • Dong, J.1    Lai, R.2    Nielsen, K.3    Fekete, C.A.4    Qiu, H.5    Hinnebusch, A.G.6
  • 7
    • 1542305510 scopus 로고    scopus 로고
    • The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40S ribosomal subunits in vitro
    • doi:10.1074/jbc.M312745200
    • Fraser CS, Lee JY, Mayeur GL, Bushell M, Doudna JA, Hershey JWB. 2004 The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40S ribosomal subunits in vitro. J. Biol. Chem. 279, 8946-8956. (doi:10.1074/jbc.M312745200)
    • (2004) J. Biol. Chem. , vol.279 , pp. 8946-8956
    • Fraser, C.S.1    Lee, J.Y.2    Mayeur, G.L.3    Bushell, M.4    Doudna, J.A.5    Hershey, J.W.B.6
  • 8
    • 84870391243 scopus 로고    scopus 로고
    • Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue
    • doi:10.1016/j.sbi.2012.08.002
    • Franckenberg S, Becker T, Beckmann R. 2012 Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue. Curr. Opin. Struct. Biol. 22, 786-796. (doi:10.1016/j.sbi.2012.08.002)
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 786-796
    • Franckenberg, S.1    Becker, T.2    Beckmann, R.3
  • 9
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • doi:10.1038/sj.emboj.7600540
    • Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC. 2005 Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 24, 580-588. (doi:10.1038/sj.emboj.7600540)
    • (2005) EMBO J , vol.24 , pp. 580-588
    • Yarunin, A.1    Panse, V.G.2    Petfalski, E.3    Dez, C.4    Tollervey, D.5    Hurt, E.C.6
  • 10
    • 20044391418 scopus 로고    scopus 로고
    • Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria
    • doi:10.1038/sj.emboj.7600541
    • Kispal G et al. 2005 Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria. EMBO J. 24, 589-598. (doi:10.1038/sj.emboj.7600541)
    • (2005) EMBO J , vol.24 , pp. 589-598
    • Kispal, G.1
  • 11
    • 33645399045 scopus 로고    scopus 로고
    • A model of protein translation including codon bias, nonsense errors and ribosome recycling
    • doi:10.1016/j.jtbi.2005.08.007
    • Gilchrist MA, Wagner A. 2006 A model of protein translation including codon bias, nonsense errors and ribosome recycling. J. Theor. Biol. 239, 417-434. (doi:10.1016/j.jtbi.2005.08.007)
    • (2006) J. Theor. Biol. , vol.239 , pp. 417-434
    • Gilchrist, M.A.1    Wagner, A.2
  • 12
    • 0042845842 scopus 로고    scopus 로고
    • Ribosome recycling, diffusion, and mRNA loop formation in translational regulation
    • doi:10.1016/S0006-3495(03)74518-4
    • Chou T. 2003 Ribosome recycling, diffusion, and mRNA loop formation in translational regulation. Biophys. J. 85, 755-773. (doi:10.1016/S0006-3495(03) 74518-4)
    • (2003) Biophys. J. , vol.85 , pp. 755-773
    • Chou, T.1
  • 13
    • 80052524231 scopus 로고    scopus 로고
    • Stochastic theory of protein synthesis and polysome: Ribosome profile on a single mRNA transcript
    • doi:10.1016/j.jtbi.2011.08.023
    • Sharma AK, Chowdhury D. 2011 Stochastic theory of protein synthesis and polysome: ribosome profile on a single mRNA transcript. J. Theor. Biol. 289, 36-46. (doi:10.1016/j.jtbi.2011.08.023)
    • (2011) J. Theor. Biol. , vol.289 , pp. 36-46
    • Sharma, A.K.1    Chowdhury, D.2
  • 14
    • 84891463251 scopus 로고    scopus 로고
    • Ribosome flow model with positive feedback
    • doi:10.1098/rsif.2013.0267
    • Margaliot M, Tuller T. 2013 Ribosome flow model with positive feedback. J. R. Soc. Interface 10, 20130267. (doi:10.1098/rsif.2013.0267)
    • (2013) J. R. Soc. Interface , vol.10 , pp. 20130267
    • Margaliot, M.1    Tuller, T.2
  • 15
    • 84855501083 scopus 로고    scopus 로고
    • Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast
    • doi:10.1073/pnas.1113956108
    • Shoemaker CJ, Green R. 2011 Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc. Natl Acad. Sci. 108, E1392-E1398. (doi:10.1073/pnas.1113956108)
    • (2011) Proc. Natl Acad. Sci. , vol.108
    • Shoemaker, C.J.1    Green, R.2
  • 16
    • 84888230681 scopus 로고    scopus 로고
    • Translation initiation factors eIF3 and HCR1 control translation termination and stop codon readthrough in yeast cells
    • doi:10.1371/journal.pgen.1003962
    • Beznosková P, Cuchalová L, Wagner S, Shoemaker CJ, Gunišová S, von der Haar T, Valá šek LS. 2013 Translation initiation factors eIF3 and HCR1 control translation termination and stop codon readthrough in yeast cells. PLoS Genet. 9, e1003962. (doi:10.1371/journal.pgen.1003962)
    • (2013) PLoS Genet , vol.9
    • Beznosková, P.1    Cuchalová, L.2    Wagner, S.3    Shoemaker, C.J.4    Gunišová, S.5    Von Der Haar, T.6    Valá Šek, L.S.7
  • 17
    • 0024591905 scopus 로고
    • The poly(A)- poly(A)-binding protein complex is a major determinant of mRNA stability in vitro
    • doi:10.1128/MCB.9.2.659
    • Bernstein P, Peltz SW, Ross J. 1989 The poly(A)- poly(A)-binding protein complex is a major determinant of mRNA stability in vitro. Mol. Cell Biol. 9, 659-670. (doi:10.1128/MCB.9.2.659)
    • (1989) Mol. Cell Biol. , vol.9 , pp. 659-670
    • Bernstein, P.1    Peltz, S.W.2    Ross, J.3
  • 18
    • 84877301308 scopus 로고    scopus 로고
    • Two-step model of stop codon recognition by eukaryotic release factor eRF1
    • doi:10.1093/nar/gkt113
    • Kryuchkova P, Grishin A, Eliseev B, Karyagina A, Frolova L, Alkalaeva E. 2013 Two-step model of stop codon recognition by eukaryotic release factor eRF1. Nucleic Acids Res. 41, 4573-4586. (doi:10.1093/nar/gkt113)
    • (2013) Nucleic Acids Res , vol.41 , pp. 4573-4586
    • Kryuchkova, P.1    Grishin, A.2    Eliseev, B.3    Karyagina, A.4    Frolova, L.5    Alkalaeva, E.6
  • 19
    • 0040261379 scopus 로고
    • Interaction of Markov processes
    • doi:10.1007/978-1-4612-0459-6-5
    • Spitzer F. 1970 Interaction of Markov processes. Adv. Math. 5, 246-290. (doi:10.1007/978-1-4612-0459-6-5)
    • (1970) Adv. Math. , vol.5 , pp. 246-290
    • Spitzer, F.1
  • 20
    • 0001366373 scopus 로고
    • An exact solution of a one-dimensional asymmetric exclusion model with open boundaries
    • doi:10.1088/0305-4470/26/7/011
    • Derrida B, Domany E, Mukamel D. 1992 An exact solution of a one-dimensional asymmetric exclusion model with open boundaries. J. Stat. Phys. 69, 667-687. (doi:10.1088/0305-4470/26/7/011)
    • (1992) J. Stat. Phys. , vol.69 , pp. 667-687
    • Derrida, B.1    Domany, E.2    Mukamel, D.3
  • 21
    • 80055088002 scopus 로고    scopus 로고
    • Non-equilibrium statistical mechanics: From a paradigmatic model to biological transport
    • doi:10.1088/0034-4885/74/11/116601
    • Chou T, Mallick K, Zia RKP. 2011 Non-equilibrium statistical mechanics: from a paradigmatic model to biological transport. Rep. Prog. Phys. 74, 116601. (doi:10.1088/0034-4885/74/11/116601)
    • (2011) Rep. Prog. Phys. , vol.74 , pp. 116601
    • Chou, T.1    Mallick, K.2    Zia, R.K.P.3
  • 22
    • 84863328349 scopus 로고    scopus 로고
    • A multi-lane TASEP model for crossing pedestrian traffic flows
    • doi:10.1088/1742- 5468/2012/06/P06009
    • Hilhorst HJ, Appert-Rolland C. 2012 A multi-lane TASEP model for crossing pedestrian traffic flows. J. Stat. Mech. 2012, P06009. (doi:10.1088/1742- 5468/2012/06/P06009)
    • (2012) J. Stat. Mech. , vol.2012
    • Hilhorst, H.J.1    Appert-Rolland, C.2
  • 23
    • 0035895856 scopus 로고    scopus 로고
    • Empirical evidence for a boundary-induced nonequilibrium phase transition
    • doi:10.1088/0305-4470/34/6/103
    • Popkov V, Santen L, Schadschneider A, Schütz GM. 2001 Empirical evidence for a boundary-induced nonequilibrium phase transition. J. Phys. A Math. Gen. 34, L45-L52. (doi:10.1088/0305-4470/34/6/103)
    • (2001) J. Phys. A Math. Gen. , vol.34
    • Popkov, V.1    Santen, L.2    Schadschneider, A.3    Schütz, G.M.4
  • 24
    • 80051478443 scopus 로고    scopus 로고
    • Totally asymmetric simple exclusion process on networks
    • doi:10.1103/ PhysRevLett.107.068702
    • Neri I, Kern N, Parmeggiani A. 2011 Totally asymmetric simple exclusion process on networks. Phys. Rev. Lett. 107, 068702. (doi:10.1103/ PhysRevLett.107.068702)
    • (2011) Phys. Rev. Lett. , vol.107 , pp. 068702
    • Neri, I.1    Kern, N.2    Parmeggiani, A.3
  • 25
    • 28844464300 scopus 로고    scopus 로고
    • Physics of transport and traffic phenomena in biology: From molecular motors and cells to organisms
    • doi:10. 1016/j.plrev.2005.09.001
    • Chowdhury D, Schadschneider A, Nishinari K. 2005 Physics of transport and traffic phenomena in biology: from molecular motors and cells to organisms. Phys. Life Rev. 2, 318-352. (doi:10. 1016/j.plrev.2005.09.001)
    • (2005) Phys. Life Rev. , vol.2 , pp. 318-352
    • Chowdhury, D.1    Schadschneider, A.2    Nishinari, K.3
  • 26
    • 0014245158 scopus 로고
    • Kinetics of biopolymerization on nucleic acid templates
    • doi:10.1002/bip.1968. 360060102
    • MacDonald CT, Gibbs JH, Pipkin AC. 1968 Kinetics of biopolymerization on nucleic acid templates. Biopolymers 6, 1-25. (doi:10.1002/bip.1968. 360060102)
    • (1968) Biopolymers , vol.6 , pp. 1-25
    • MacDonald, C.T.1    Gibbs, J.H.2    Pipkin, A.C.3
  • 27
    • 42749107428 scopus 로고    scopus 로고
    • Totally asymmetric exclusion process with extended objects: A model for protein synthesis
    • doi:10.1103/PhysRevE.68.021910
    • Shaw LB, Zia RKP, Lee KH. 2003 Totally asymmetric exclusion process with extended objects: a model for protein synthesis. Phys. Rev. E 68, 021910. (doi:10.1103/PhysRevE.68.021910)
    • (2003) Phys. Rev. E , vol.68 , pp. 021910
    • Shaw, L.B.1    Zia, R.K.P.2    Lee, K.H.3
  • 28
    • 66049160486 scopus 로고    scopus 로고
    • Queuing phase transition: Theory of translation
    • doi:10.1103/ PhysRevLett.102.198104
    • Romano MC, Thiel M, Stansfield I, Grebogi C. 2009 Queuing phase transition: theory of translation. Phys. Rev. Lett. 102, 198104. (doi:10.1103/ PhysRevLett.102.198104)
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 198104
    • Romano, M.C.1    Thiel, M.2    Stansfield, I.3    Grebogi, C.4
  • 29
    • 77952020413 scopus 로고    scopus 로고
    • Role of the particle's stepping cycle in an asymmetric exclusion process: A model of mRNA translation
    • doi:10.1103/PhysRevE.81. 051904
    • Ciandrini L, Stansfield I, Romano MC. 2010 Role of the particle's stepping cycle in an asymmetric exclusion process: a model of mRNA translation. Phys. Rev. E 81, 051904. (doi:10.1103/PhysRevE.81. 051904)
    • (2010) Phys. Rev. E , vol.81 , pp. 051904
    • Ciandrini, L.1    Stansfield, I.2    Romano, M.C.3
  • 30
    • 80055093840 scopus 로고    scopus 로고
    • The dynamics of supply and demand in mRNA translation
    • doi:10. 1371/journal.pcbi.1002203
    • Brackley CA, Romano MC, Thiel M. 2011 The dynamics of supply and demand in mRNA translation. PLoS Comput. Biol. 7, e1002203. (doi:10. 1371/journal.pcbi.1002203)
    • (2011) PLoS Comput. Biol. , vol.7
    • Brackley, C.A.1    Romano, M.C.2    Thiel, M.3
  • 31
    • 79960980919 scopus 로고    scopus 로고
    • Modeling translation in protein synthesis with TASEP: A tutorial and recent developments
    • doi:10.1007/s10955-011-0183-1
    • Zia RKP, Dong JJ, Schmittmann B. 2011 Modeling translation in protein synthesis with TASEP: a tutorial and recent developments. J. Stat. Phys. 144, 405-428. (doi:10.1007/s10955-011-0183-1)
    • (2011) J. Stat. Phys. , vol.144 , pp. 405-428
    • Zia, R.K.P.1    Dong, J.J.2    Schmittmann, B.3
  • 32
    • 0040531676 scopus 로고    scopus 로고
    • Phase diagram of one-dimensional driven lattice gases with open boundaries
    • doi:10.1088/0305-4470/31/33/003
    • Kolomeisky AB, Schütz GM, Kolomeisky EB, Straley JP. 1998 Phase diagram of one-dimensional driven lattice gases with open boundaries. J. Phys. A Math. Gen. 31, 6911-6919. (doi:10.1088/0305-4470/31/33/003)
    • (1998) J. Phys. A Math. Gen. , vol.31 , pp. 6911-6919
    • Kolomeisky, A.B.1    Schütz, G.M.2    Kolomeisky, E.B.3    Straley, J.P.4
  • 33
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • doi:10. 1126/science.1168978
    • Ingolia NT, Ghaemmaghami S, Newman JRS, Weissman JS. 2009 Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324, 218-223. (doi:10. 1126/science.1168978)
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.S.3    Weissman, J.S.4
  • 34
    • 84873510362 scopus 로고    scopus 로고
    • Ribosome traffic on mRNAs maps to gene ontology: Genome-wide quantification of translation initiation rates and polysome size regulation
    • doi:10.1371/journal.pcbi. 1002866
    • Ciandrini L, Stansfield I, Romano MC. 2013 Ribosome traffic on mRNAs maps to gene ontology: genome-wide quantification of translation initiation rates and polysome size regulation. PLoS Comput. Biol. 9, e1002866. (doi:10.1371/journal.pcbi. 1002866)
    • (2013) PLoS Comput. Biol. , vol.9
    • Ciandrini, L.1    Stansfield, I.2    Romano, M.C.3
  • 35
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • doi:10.1021/j100540a008
    • Gillespie DT. 1977 Exact stochastic simulation of coupled chemical reactions. J. Phys. Chem. 81, 2340-2361. (doi:10.1021/j100540a008)
    • (1977) J. Phys. Chem. , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 36
    • 84872395280 scopus 로고    scopus 로고
    • A yeast tRNA mutant that causes pseudohyphal growth exhibits reduced rates of CAG codon translation
    • doi:10.1111/mmi.12096
    • Kemp AJ, Betney R, Ciandrini L, Schwenger ACM, Romano MC, Stansfield I. 2013 A yeast tRNA mutant that causes pseudohyphal growth exhibits reduced rates of CAG codon translation. Mol. Microbiol. 87, 284-300. (doi:10.1111/mmi.12096)
    • (2013) Mol. Microbiol. , vol.87 , pp. 284-300
    • Kemp, A.J.1    Betney, R.2    Ciandrini, L.3    Schwenger, A.C.M.4    Romano, M.C.5    Stansfield, I.6
  • 37
    • 77951715627 scopus 로고    scopus 로고
    • An evolutionarily conserved mechanism for controlling the efficiency of protein translation
    • doi:10.1016/j.cell. 2010.03.031
    • Tuller T et al. 2010 An evolutionarily conserved mechanism for controlling the efficiency of protein translation. Cell 141, 344-354. (doi:10.1016/j.cell. 2010.03.031)
    • (2010) Cell , vol.141 , pp. 344-354
    • Tuller, T.1
  • 38
    • 17444449538 scopus 로고    scopus 로고
    • Transfer RNA gene redundancy and translational selection in Saccharomyces cerevisiae
    • doi:10.1006/jmbi.1997.0942
    • Percudani R, Pavesi A, Ottonello S. 1997 Transfer RNA gene redundancy and translational selection in Saccharomyces cerevisiae. J. Mol. Biol. 268, 322-330. (doi:10.1006/jmbi.1997.0942)
    • (1997) J. Mol. Biol. , vol.268 , pp. 322-330
    • Percudani, R.1    Pavesi, A.2    Ottonello, S.3
  • 39
    • 84873570699 scopus 로고    scopus 로고
    • Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding
    • doi:10.1038/nsmb.2466
    • Pechmann S, Frydman J. 2013 Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding. Nat. Struct. Mol. Biol. 20, 237-243. (doi:10.1038/nsmb.2466)
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 237-243
    • Pechmann, S.1    Frydman, J.2
  • 40
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • doi:10.1016/S0014-5793(99) 01566-5
    • Komar A, Lesnik T, Reiss C. 1999 Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Lett. 462, 387-391. (doi:10.1016/S0014-5793(99) 01566-5)
    • (1999) FEBS Lett , vol.462 , pp. 387-391
    • Komar, A.1    Lesnik, T.2    Reiss, C.3
  • 41
    • 81755184408 scopus 로고    scopus 로고
    • Wobble base-pairing slows in vivo translation elongation in metazoans
    • doi:10.1261/rna.02890211
    • Stadler M, Fire A. 2011 Wobble base-pairing slows in vivo translation elongation in metazoans. RNA 17, 2063-2073. (doi:10.1261/rna.02890211)
    • (2011) RNA , vol.17 , pp. 2063-2073
    • Stadler, M.1    Fire, A.2
  • 42
    • 0021764898 scopus 로고
    • Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains
    • doi:10.1016/0022-2836(84)90027-5
    • Varenne S, Buc J, Lloubes R, Lazdunski C. 1984 Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains. J. Mol. Biol. 180, 549-576. (doi:10.1016/0022- 2836(84)90027-5)
    • (1984) J. Mol. Biol. , vol.180 , pp. 549-576
    • Varenne, S.1    Buc, J.2    Lloubes, R.3    Lazdunski, C.4
  • 43
    • 48249093081 scopus 로고    scopus 로고
    • Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host
    • doi:10.1371/journal. pone.0002189
    • Angov E, Hillier CJ, Kincaid RL, Lyon JA. 2008 Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host. PLoS ONE 3, e2189. (doi:10.1371/journal. pone.0002189)
    • (2008) PLoS ONE , vol.3
    • Angov, E.1    Hillier, C.J.2    Kincaid, R.L.3    Lyon, J.A.4
  • 44
    • 84870717729 scopus 로고    scopus 로고
    • Determinants of translation elongation speed and ribosomal profiling biases in mouse embryonic stem cells
    • doi:10.1371/journal.pcbi.1002755
    • Dana A, Tuller T. 2012 Determinants of translation elongation speed and ribosomal profiling biases in mouse embryonic stem cells. PLoS Comput. Biol. 8, e1002755. (doi:10.1371/journal.pcbi.1002755)
    • (2012) PLoS Comput. Biol. , vol.8
    • Dana, A.1    Tuller, T.2
  • 45
    • 45549088326 scopus 로고    scopus 로고
    • The transcriptional landscape of the yeast genome defined by RNA sequencing
    • doi:10.1126/ science.1158441
    • Nagalakshmi U, Wang Z, Waern K, Shou C, Raha D, Gerstein M, Snyder M. 2008 The transcriptional landscape of the yeast genome defined by RNA sequencing. Science 320, 1344-1349. (doi:10.1126/ science.1158441)
    • (2008) Science , vol.320 , pp. 1344-1349
    • Nagalakshmi, U.1    Wang, Z.2    Waern, K.3    Shou, C.4    Raha, D.5    Gerstein, M.6    Snyder, M.7
  • 47
    • 2642566765 scopus 로고    scopus 로고
    • Gene expression analyzed by high-resolution state array analysis and quantitative proteomics
    • doi:10.1074/mcp.M300129-MCP200
    • MacKay VL et al. 2004 Gene expression analyzed by high-resolution state array analysis and quantitative proteomics. Mol. Cell. Proteomics 3, 478-498. (doi:10.1074/mcp.M300129-MCP200)
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 478-498
    • MacKay, V.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.