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Volumn 525, Issue 7570, 2015, Pages 491-495

Structure of mammalian eIF3 in the context of the 43S preinitiation complex

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 3; MESSENGER RNA; DHX29 PROTEIN, HUMAN; INITIATION FACTOR; INITIATION FACTOR 2; METHIONINE TRANSFER RNA; MULTIPROTEIN COMPLEX; PROTEIN SUBUNIT; RNA HELICASE; START CODON;

EID: 84942531804     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14891     Document Type: Article
Times cited : (189)

References (68)
  • 1
    • 75149196287 scopus 로고    scopus 로고
    • Themechanismof eukaryotic translation initiation and principles of its regulation
    • Jackson,R. J.,Hellen, C. U.&Pestova, T.V.Themechanismof eukaryotic translation initiation and principles of its regulation. Nature Rev. Mol. Cell Biol. 11, 113-127 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 2
    • 33748924333 scopus 로고    scopus 로고
    • EIF3: A versatile scaffold for translation initiation complexes
    • Hinnebusch, A. G. eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem. Sci. 31, 553-562 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 553-562
    • Hinnebusch, A.G.1
  • 3
    • 84863624560 scopus 로고    scopus 로고
    • Ribozoomin'-translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs)
    • Valasek, L. S. 'Ribozoomin'-translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs). Curr. Protein Pept. Sci. 13, 305-330 (2012).
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 305-330
    • Valasek, L.S.1
  • 4
    • 84873643109 scopus 로고    scopus 로고
    • Structural biology of the PCI-protein fold
    • Ellisdon, A. M., Stewart, M. Structural biology of the PCI-protein fold. BioArchitecture 2, 118-123 (2012).
    • (2012) Bio Architecture , vol.2 , pp. 118-123
    • Ellisdon, A.M.1    Stewart, M.2
  • 5
    • 33847053558 scopus 로고    scopus 로고
    • Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa
    • Pena, V., Liu, S., Bujnicki, J. M., Luhrmann, R., Wahl, M. C. Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa. Mol. Cell 25, 615-624 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 615-624
    • Pena, V.1    Liu, S.2    Bujnicki, J.M.3    Luhrmann, R.4    Wahl, M.C.5
  • 6
    • 77951639210 scopus 로고    scopus 로고
    • Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3
    • Enchev, R. I., Schreiber, A., Beuron, F., Morris, E. P. Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. Structure 18, 518-527 (2010).
    • (2010) Structure , vol.18 , pp. 518-527
    • Enchev, R.I.1    Schreiber, A.2    Beuron, F.3    Morris, E.P.4
  • 7
    • 84878333225 scopus 로고    scopus 로고
    • Structure of themammalian ribosomal43S preinitiation complex bound to the scanning factor DHX29
    • Hashem, Y. et al. Structure of themammalian ribosomal43S preinitiation complex bound to the scanning factor DHX29. Cell 153, 1108-1119 (2013).
    • (2013) Cell , vol.153 , pp. 1108-1119
    • Hashem, Y.1
  • 8
    • 84888642485 scopus 로고    scopus 로고
    • Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit
    • Hashem, Y. et al. Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit. Nature 503, 539-543 (2013).
    • (2013) Nature , vol.503 , pp. 539-543
    • Hashem, Y.1
  • 9
    • 84878826802 scopus 로고    scopus 로고
    • Architecture of human translation initiation factor 3
    • Querol-Audi, J. et al. Architecture of human translation initiation factor 3. Structure 21, 920-928 (2013).
    • (2013) Structure , vol.21 , pp. 920-928
    • Querol-Audi, J.1
  • 10
    • 84855492118 scopus 로고    scopus 로고
    • Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3)
    • Sun, C. et al. Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3). Proc. Natl Acad. Sci. USA 108, 20473-20478 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 20473-20478
    • Sun, C.1
  • 11
    • 84866269021 scopus 로고    scopus 로고
    • Near-atomic resolution structural model of the yeast 26S proteasome
    • Beck, F. et al. Near-atomic resolution structural model of the yeast 26S proteasome. Proc. Natl Acad. Sci. USA 109, 14870-14875 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 14870-14875
    • Beck, F.1
  • 12
    • 84856976866 scopus 로고    scopus 로고
    • Complete subunit architecture of the proteasome regulatory particle
    • Lander, G. C. et al. Complete subunit architecture of the proteasome regulatory particle. Nature 482, 186-191 (2012).
    • (2012) Nature , vol.482 , pp. 186-191
    • Lander, G.C.1
  • 13
    • 84906238422 scopus 로고    scopus 로고
    • Crystal structure of the human COP9 signalosome
    • Lingaraju, G. M. et al. Crystal structure of the human COP9 signalosome. Nature 512, 161-165 (2014).
    • (2014) Nature , vol.512 , pp. 161-165
    • Lingaraju, G.M.1
  • 14
    • 34247241059 scopus 로고    scopus 로고
    • Structure of eIF3b RNA recognition motif and its interaction with eIF3j: Structural insights into the recruitment of eIF3bto the 40Sribosomal subunit
    • ElAntak, L., Tzakos, A. G., Locker, N., Lukavsky, P. J. Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3bto the 40Sribosomal subunit. J. Biol.Chem. 282,8165-8174 (2007).
    • (2007) J. Biol.Chem. , vol.282 , pp. 8165-8174
    • El Antak, L.1    Tzakos, A.G.2    Locker, N.3    Lukavsky, P.J.4
  • 15
    • 84863338242 scopus 로고    scopus 로고
    • Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly
    • Herrmannova, A. et al. Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly. Nucleic Acids Res. 40, 2294-2311 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2294-2311
    • Herrmannova, A.1
  • 16
    • 84902342066 scopus 로고    scopus 로고
    • Translation initiation factor eIF3b contains a nine-bladed b-propeller and interacts with the 40S ribosomal subunit
    • Liu, Y. et al. Translation initiation factor eIF3b contains a nine-bladed b-propeller and interacts with the 40S ribosomal subunit. Structure 22, 923-930 (2014).
    • (2014) Structure , vol.22 , pp. 923-930
    • Liu, Y.1
  • 17
    • 84907323467 scopus 로고    scopus 로고
    • Molecular architecture of the 40SeIF1eIF3 translation initiation complex
    • Erzberger, J. P. et al. Molecular architecture of the 40SeIF1eIF3 translation initiation complex. Cell 158, 1123-1135 (2014).
    • (2014) Cell , vol.158 , pp. 1123-1135
    • Erzberger, J.P.1
  • 18
    • 57449083256 scopus 로고    scopus 로고
    • Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3
    • Zhou, M. et al. Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3. Proc. Natl Acad. Sci. USA 105, 18139-18144 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 18139-18144
    • Zhou, M.1
  • 19
    • 84884809999 scopus 로고    scopus 로고
    • Spectrin domainof eukaryotic initiation factor 3a is the docking site for formation of the a:b: I:g subcomplex
    • Dong, Z.,Qi, J.,Peng, H., Liu, J.&Zhang, J.T.Spectrin domainof eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex. J. Biol. Chem. 288, 27951-27959 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 27951-27959
    • Dong, Z.1    Qi, J.2    Peng, H.3    Liu, J.4    Zhang, J.T.5
  • 20
    • 84904511881 scopus 로고    scopus 로고
    • Functional and biochemical characterization of humaneukaryotic translation initiation factor 3 in living cells
    • Wagner, S., Herrmannova, A., Malk, R., Peclinovska, L., Valasek, L. S. Functional and biochemical characterization of humaneukaryotic translation initiation factor 3 in living cells. Mol. Cell. Biol. 34, 3041-3052 (2014).
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 3041-3052
    • Wagner, S.1    Herrmannova, A.2    Malk, R.3    Peclinovska, L.4    Valasek, L.S.5
  • 21
    • 34547178178 scopus 로고    scopus 로고
    • Reconstitution reveals the functional core of mammalian eIF3
    • Masutani, M.,Sonenberg, N., Yokoyama,S.&Imataka, H. Reconstitution reveals the functional core of mammalian eIF3. EMBO J. 26, 3373-3383 (2007).
    • (2007) EMBO J. , vol.26 , pp. 3373-3383
    • Masutani, M.1    Sonenberg, N.2    Yokoyama, S.3    Imataka, H.4
  • 22
    • 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 40 S ribosomal subunits in vitro
    • Fraser, C. S. et al. The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro. J. Biol. Chem. 279, 8946-8956 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 8946-8956
    • Fraser, C.S.1
  • 23
    • 0039183713 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae HCR1 gene encoding a homologue of the p35 subunit of human translation initiation factor 3 (eIF3) is a high copy suppressor of a temperaturesensitive mutation in the Rpg1p subunit of yeast eIF3
    • Valasek, L., Hasek, J., Trachsel, H., Imre, E. M., Ruis, H. The Saccharomyces cerevisiae HCR1 gene encoding a homologue of the p35 subunit of human translation initiation factor 3 (eIF3) is a high copy suppressor of a temperaturesensitive mutation in the Rpg1p subunit of yeast eIF3. J. Biol. Chem. 274, 27567-27572 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27567-27572
    • Valasek, L.1    Hasek, J.2    Trachsel, H.3    Imre, E.M.4    Ruis, H.5
  • 24
    • 84883488318 scopus 로고    scopus 로고
    • Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid
    • Estrin, E., Lopez-Blanco, J. R., Chacon, P., Martin, A. Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid. Structure 21, 1624-1635 (2013).
    • (2013) Structure , vol.21 , pp. 1624-1635
    • Estrin, E.1    Lopez-Blanco, J.R.2    Chacon, P.3    Martin, A.4
  • 25
    • 84877310529 scopus 로고    scopus 로고
    • Structures of the human and Drosophila 80S ribosome
    • Anger, A. M. et al. Structures of the human and Drosophila 80S ribosome. Nature 497, 80-85 (2013).
    • (2013) Nature , vol.497 , pp. 80-85
    • Anger, A.M.1
  • 26
    • 84861321529 scopus 로고    scopus 로고
    • Structure of the ternary initiation complex aIF2-GDPNPmethionylated initiator tRNA
    • Schmitt, E. et al. Structure of the ternary initiation complex aIF2-GDPNPmethionylated initiator tRNA. Nature Struct. Mol. Biol. 19, 450-454 (2012).
    • (2012) Nature Struct. Mol. Biol. , vol.19 , pp. 450-454
    • Schmitt, E.1
  • 27
    • 84869227939 scopus 로고    scopus 로고
    • Roles of individual domains in the function of DHX29, an essential factor required for translation of structured mammalian mRNAs
    • Dhote, V., Sweeney, T. R., Kim, N., Hellen, C. U., Pestova, T. V. Roles of individual domains in the function of DHX29, an essential factor required for translation of structured mammalian mRNAs. Proc. Natl Acad. Sci. USA 109, E3150-E3159 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. E3150-E3159
    • Dhote, V.1    Sweeney, T.R.2    Kim, N.3    Hellen, C.U.4    Pestova, T.V.5
  • 29
    • 84863633085 scopus 로고    scopus 로고
    • Small ribosomal protein RPS0 stimulates translation initiation by mediating 40S-binding of eIF3 via its direct contact with the eIF3a/TIF32 subunit
    • Kouba, T. et al. Small ribosomal protein RPS0 stimulates translation initiation by mediating 40S-binding of eIF3 via its direct contact with the eIF3a/TIF32 subunit. PLoS ONE 7, e40464 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e40464
    • Kouba, T.1
  • 30
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a, NIP1/c, eIF5 make critical connections with the 40S ribosome in vivo
    • Valasek, L. et al. The yeast eIF3 subunits TIF32/a, NIP1/c, eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev. 17, 786-799 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 786-799
    • Valasek, L.1
  • 31
    • 44649095899 scopus 로고    scopus 로고
    • Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
    • Pisarev, A. V., Kolupaeva, V. G., Yusupov, M. M., Hellen, C. U., Pestova, T. V. Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes. EMBO J. 27, 1609-1621 (2008).
    • (2008) EMBO J. , vol.27 , pp. 1609-1621
    • Pisarev, A.V.1    Kolupaeva, V.G.2    Yusupov, M.M.3    Hellen, C.U.4    Pestova, T.V.5
  • 32
    • 27544510262 scopus 로고    scopus 로고
    • PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes
    • Zhou, C. et al. PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes. BMC Biol. 3, 14 (2005).
    • (2005) BMC Biol. , vol.3 , pp. 14
    • Zhou, C.1
  • 33
    • 84924291670 scopus 로고    scopus 로고
    • The translation initiation complex eIF3 in trypanosomatids andotherpathogenic excavates-identificationof conservedanddivergent features based on orthologue analysis
    • Rezende, A. M. et al. The translation initiation complex eIF3 in trypanosomatids andotherpathogenic excavates-identificationof conservedanddivergent features based on orthologue analysis. BMC Genomics 15, 1175 (2014).
    • (2014) BMC Genomics , vol.15 , pp. 1175
    • Rezende, A.M.1
  • 34
    • 33747354635 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3E subunit
    • LeFebvre, A. K. et al. Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3E subunit. J. Biol. Chem. 281, 22917-22932 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 22917-22932
    • LeFebvre, A.K.1
  • 35
    • 84887853618 scopus 로고    scopus 로고
    • Human eukaryotic initiation factor 4G (eIF4G) binds to eIF3c,-d,-e to promote mRNA recruitment to the ribosome
    • Villa, N., Do, A., Hershey, J. W. B., Fraser, C. S. Human eukaryotic initiation factor 4G (eIF4G) binds to eIF3c,-d,-e to promote mRNA recruitment to the ribosome. J. Biol. Chem. 288, 32932-32940 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 32932-32940
    • Villa, N.1    Do, A.2    Hershey, J.W.B.3    Fraser, C.S.4
  • 36
    • 79959452628 scopus 로고    scopus 로고
    • Common conformational changes induced in type 2 picornavirus IRESs by cognate transacting factors
    • Yu, Y., Abaeva, I. S., Marintchev, A., Pestova, T. V., Hellen, C. U. Common conformational changes induced in type 2 picornavirus IRESs by cognate transacting factors. Nucleic Acids Res. 39, 4851-4865 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 4851-4865
    • Yu, Y.1    Abaeva, I.S.2    Marintchev, A.3    Pestova, T.V.4    Hellen, C.U.5
  • 37
    • 77956713468 scopus 로고    scopus 로고
    • The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons
    • Chiu, W. L. et al. The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol. Cell. Biol. 30, 4415-4434 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4415-4434
    • Chiu, W.L.1
  • 38
    • 77649269977 scopus 로고    scopus 로고
    • The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection
    • Elantak, L. et al. The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection. J. Mol. Biol. 396, 1097-1116 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 1097-1116
    • Elantak, L.1
  • 39
    • 77956657467 scopus 로고    scopus 로고
    • The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning
    • Cuchalova, L. et al. The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning. Mol. Cell. Biol. 30, 4671-4686 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4671-4686
    • Cuchalova, L.1
  • 40
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 59UTRs requires DExH-box protein DHX29
    • Pisareva, V. P., Pisarev, A. V., Komar, A. A., Hellen, C. U., Pestova, T. V. Translation initiation on mammalian mRNAs with structured 59UTRs requires DExH-box protein DHX29. Cell 135, 1237-1250 (2008).
    • (2008) Cell , vol.135 , pp. 1237-1250
    • Pisareva, V.P.1    Pisarev, A.V.2    Komar, A.A.3    Hellen, C.U.4    Pestova, T.V.5
  • 41
    • 39149091041 scopus 로고    scopus 로고
    • Preparation of macromolecular complexes for cryo-electron microscopy
    • Grassucci, R. A., Taylor, D. J., Frank, J. Preparation of macromolecular complexes for cryo-electron microscopy. Nature Protocols 2, 3239-3246 (2007).
    • (2007) Nature Protocols , vol.2 , pp. 3239-3246
    • Grassucci, R.A.1    Taylor, D.J.2    Frank, J.3
  • 42
    • 0024007766 scopus 로고
    • Cryo-electron microscopy of vitrified specimens
    • Dubochet, J. et al. Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys. 21, 129-228 (1988).
    • (1988) Q. Rev. Biophys. , vol.21 , pp. 129-228
    • Dubochet, J.1
  • 43
    • 0023787021 scopus 로고
    • Direct localization of the tRNA-anticodon interaction site on the Escherichia coli 30 S ribosomal subunit by electron microscopy and computerized image averaging
    • Wagenknecht, T., Frank, J., Boublik, M., Nurse, K., Ofengand, J. Direct localization of the tRNA-anticodon interaction site on the Escherichia coli 30 S ribosomal subunit by electron microscopy and computerized image averaging. J. Mol. Biol. 203, 753-760 (1988).
    • (1988) J. Mol. Biol. , vol.203 , pp. 753-760
    • Wagenknecht, T.1    Frank, J.2    Boublik, M.3    Nurse, K.4    Ofengand, J.5
  • 44
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: The new Leginon system
    • Suloway, C. et al. Automated molecular microscopy: the new Leginon system. J. Struct. Biol. 151, 41-60 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 41-60
    • Suloway, C.1
  • 45
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 46
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 47
    • 84898598700 scopus 로고    scopus 로고
    • Automated particle picking for low-contrast macromolecules in cryo-electron microscopy
    • Langlois, R. et al. Automated particle picking for low-contrast macromolecules in cryo-electron microscopy. J. Struct. Biol. 186, 1-7 (2014).
    • (2014) J. Struct. Biol. , vol.186 , pp. 1-7
    • Langlois, R.1
  • 48
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 49
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B., Henderson, R. Optimal determination of particle orientation, absolute hand, contrast loss in single-particle electron cryomicroscopy. J.Mol. Biol. 333, 721-745 (2003).
    • (2003) J.Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 50
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013).
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 51
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, S. J., Tagare, D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63-65 (2014).
    • (2014) Nature Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, S.J.2    Tagare, D.3
  • 52
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization systemfor exploratory research and analysis
    • Pettersen, E. F. et al.UCSFChimera-a visualization systemfor exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 53
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, fitting of structures by alignment to regions
    • Pintilie, G. D., Zhang, J., Goddard, T. D., Chiu, W., Gossard, D. C. Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, fitting of structures by alignment to regions. J. Struct. Biol. 170, 427-438 (2010).
    • (2010) J. Struct. Biol. , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 54
    • 84941042486 scopus 로고    scopus 로고
    • CDD: NCBI's conserved domain database
    • Marchler-Bauer, A. et al. CDD: NCBI's conserved domain database. Nucleic Acids Res. 43, D222-D226 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. D222-D226
    • Marchler-Bauer, A.1
  • 55
    • 84946074739 scopus 로고    scopus 로고
    • The InterPro protein families database: The classification resource after 15 years
    • Mitchell, A. et al. The InterPro protein families database: the classification resource after 15 years. Nucleic Acids Res. 43, D213-D221 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. D213-D221
    • Mitchell, A.1
  • 56
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev, A., Wagner, G. Translation initiation: structures, mechanisms and evolution. Q. Rev. Biophys. 37, 197-284 (2004).
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 57
    • 84930373168 scopus 로고    scopus 로고
    • The RNA helicases AtMTR4 and HEN2 target specific subsets of nuclear transcripts for degradation by the nuclear exosomein Arabidopsis thaliana
    • Lange, H. et al. The RNA helicases AtMTR4 and HEN2 target specific subsets of nuclear transcripts for degradation by the nuclear exosomein Arabidopsis thaliana. PLoS Genet. 10, e1004564 (2014).
    • (2014) PLoS Genet. , vol.10 , pp. e1004564
    • Lange, H.1
  • 58
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 59
    • 77954701890 scopus 로고    scopus 로고
    • Bioinformatics strategies in life sciences: From data processing and data warehousing tobiological knowledgeextraction
    • Thiele, H., Glandorf, J.&Hufnagel,P.Bioinformatics strategies in life sciences: from data processinganddatawarehousing tobiological knowledgeextraction. J. Integr. Bioinform. 7, 141 (2010).
    • (2010) J. Integr. Bioinform. , vol.7 , pp. 141
    • Thiele, H.1    Glandorf, J.2    Hufnagel, P.3
  • 60
    • 77449146854 scopus 로고    scopus 로고
    • Target-decoy search strategy for mass spectrometry-based proteomics
    • Elias, J. E., Gygi, S. P. Target-decoy search strategy for mass spectrometry-based proteomics. Methods Mol. Biol. 604, 55-71 (2010).
    • (2010) Methods Mol. Biol. , vol.604 , pp. 55-71
    • Elias, J.E.1    Gygi, S.P.2
  • 61
    • 84898962689 scopus 로고    scopus 로고
    • Structural integrity of the PCI domain of eIF3a/TIF32 is required formRNA recruitment to the 43S pre-initiation complexes
    • Khoshnevis, S. et al. Structural integrity of the PCI domain of eIF3a/TIF32 is required formRNA recruitment to the 43S pre-initiation complexes. Nucleic Acids Res. 42, 4123-4139 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. 4123-4139
    • Khoshnevis, S.1
  • 62
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 63
    • 4544304063 scopus 로고    scopus 로고
    • Crystal structure of human eIF3k, the first structure of eIF3 subunits
    • Wei, Z. et al. Crystal structure of human eIF3k, the first structure of eIF3 subunits. J. Biol. Chem. 279, 34983-34990 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 34983-34990
    • Wei, Z.1
  • 64
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco, L. G., Villa, E., Mitra, K., Frank, J., Schulten, K. Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16, 673-683 (2008).
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 65
    • 84874191297 scopus 로고    scopus 로고
    • High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome
    • Hashem, Y. et al. High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome. Nature 494, 385-389 (2013).
    • (2013) Nature , vol.494 , pp. 385-389
    • Hashem, Y.1
  • 67
    • 84986512474 scopus 로고
    • CHARMM: A programformacromolecular energy, minimization, and dynamics calculations
    • Brooks, B. R. et al.CHARMM: a programformacromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1


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