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Volumn 22, Issue 10, 2015, Pages 767-773

Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SARCIN; BACILLUS SUBTILIS SIGNAL RECOGNITION PARTICLE; BACTERIAL PROTEIN; BACTERIAL RNA; ELONGATION FACTOR; RIBOSOME RNA; RICIN; RNA 23S; RNA BINDING PROTEIN; RNA BINDING PROTEIN SRP54; SIGNAL RECOGNITION PARTICLE; UNCLASSIFIED DRUG; OLIGONUCLEOTIDE; PROTEIN BINDING; PROTEIN SUBUNIT; RNA;

EID: 84943450001     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3086     Document Type: Article
Times cited : (29)

References (59)
  • 1
    • 84878941023 scopus 로고    scopus 로고
    • Signal recognition particle: An essential protein-targeting machine
    • Akopian, D., Shen, K., Zhang, X. &Shan, S.O. Signal recognition particle: an essential protein-targeting machine. Annu. Rev. Biochem. 82, 693-721 (2013).
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 693-721
    • Akopian, D.1    Shen, K.2    Zhang, X.3    Shan, S.O.4
  • 2
    • 84880641715 scopus 로고    scopus 로고
    • Co-translational targeting and translocation of proteins to the endoplasmic reticulum
    • Nyathi, Y., Wilkinson, B.M. &Pool, M.R. Co-translational targeting and translocation of proteins to the endoplasmic reticulum. Biochim. Biophys. Acta 1833, 2392-2402 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2392-2402
    • Nyathi, Y.1    Wilkinson, B.M.2    Pool, M.R.3
  • 4
    • 85017331117 scopus 로고    scopus 로고
    • Real-time observation of signal recognition particle binding to actively translating ribosomes
    • Noriega, T.R., Chen, J., Walter, P. &Puglisi, J.D. Real-time observation of signal recognition particle binding to actively translating ribosomes. eLife 3, e04418 (2014).
    • (2014) ELife , vol.3 , pp. e04418
    • Noriega, T.R.1    Chen, J.2    Walter, P.3    Puglisi, J.D.4
  • 5
    • 0034626729 scopus 로고    scopus 로고
    • Structure and assembly of the Alu domain of the mammalian signal recognition particle
    • Weichenrieder, O., Wild, K., Strub, K. &Cusack, S. Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature 408, 167-173 (2000).
    • (2000) Nature , vol.408 , pp. 167-173
    • Weichenrieder, O.1    Wild, K.2    Strub, K.3    Cusack, S.4
  • 6
    • 0035051603 scopus 로고    scopus 로고
    • Hierarchical assembly of the Alu domain of the mammalian signal recognition particle
    • Weichenrieder, O. et al. Hierarchical assembly of the Alu domain of the mammalian signal recognition particle. RNA 7, 731-740 (2001).
    • (2001) RNA , vol.7 , pp. 731-740
    • Weichenrieder, O.1
  • 7
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic, M. et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808-814 (2004).
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1
  • 8
    • 84923584465 scopus 로고    scopus 로고
    • Structure of the complete bacterial SRP Alu domain
    • Kempf, G., Wild, K. &Sinning, I. Structure of the complete bacterial SRP Alu domain. Nucleic Acids Res. 42, 12284-12294 (2014).
    • (2014) Nucleic Acids Res , vol.42 , pp. 12284-12294
    • Kempf, G.1    Wild, K.2    Sinning, I.3
  • 9
    • 84911461912 scopus 로고    scopus 로고
    • Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation
    • Bousset, L. et al. Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation. RNA 20, 1955-1962 (2014).
    • (2014) RNA , vol.20 , pp. 1955-1962
    • Bousset, L.1
  • 10
    • 0021645935 scopus 로고
    • The 4.5 S RNA gene of Escherichia coli is essential for cell growth
    • Brown, S. &Fournier, M.J. The 4.5 S RNA gene of Escherichia coli is essential for cell growth. J. Mol. Biol. 178, 533-550 (1984).
    • (1984) J. Mol. Biol , vol.178 , pp. 533-550
    • Brown, S.1    Fournier, M.J.2
  • 11
    • 0026517258 scopus 로고
    • Small cytoplasmic RNA of Bacillus subtilis: Functional-relationship with human signal recognition particle 7s RNA and Escherichia coli 4.5s RNA
    • Nakamura, K., Imai, Y., Nakamura, A. &Yamane, K. Small cytoplasmic RNA of Bacillus subtilis: functional-relationship with human signal recognition particle 7s RNA and Escherichia coli 4.5s RNA. J. Bacteriol. 174, 2185-2192 (1992).
    • (1992) J. Bacteriol , vol.174 , pp. 2185-2192
    • Nakamura, K.1    Imai, Y.2    Nakamura, A.3    Yamane, K.4
  • 12
    • 0028818093 scopus 로고
    • Small cytoplasmic RNA (Scrna) gene from Clostridium perfringens can replace the gene for the Bacillus subtilis Scrna in both growth and sporulation
    • Nakamura, K. et al. Small cytoplasmic RNA (Scrna) gene from Clostridium perfringens can replace the gene for the Bacillus subtilis Scrna in both growth and sporulation. Microbiology 141, 2965-2975 (1995).
    • (1995) Microbiology , vol.141 , pp. 2965-2975
    • Nakamura, K.1
  • 13
    • 0026032190 scopus 로고
    • Genes for 7S RNAs can replace the gene for 4.5S RNA in growth of Escherichia coli
    • Brown, S. Genes for 7S RNAs can replace the gene for 4.5S RNA in growth of Escherichia coli. J. Bacteriol. 173, 1835-1837 (1991).
    • (1991) J. Bacteriol , vol.173 , pp. 1835-1837
    • Brown, S.1
  • 14
    • 0025260974 scopus 로고
    • Escherichia coli 4.5S RNA gene function can be complemented by heterologous bacterial RNA genes
    • Struck, J.C., Lempicki, R.A., Toschka, H.Y., Erdmann, V.A. &Fournier, M.J. Escherichia coli 4.5S RNA gene function can be complemented by heterologous bacterial RNA genes. J. Bacteriol. 172, 1284-1288 (1990).
    • (1990) J. Bacteriol , vol.172 , pp. 1284-1288
    • Struck, J.C.1    Lempicki, R.A.2    Toschka, H.Y.3    Erdmann, V.A.4    Fournier, M.J.5
  • 15
    • 0036427575 scopus 로고    scopus 로고
    • Evolution of signalling in the sporulation phosphorelay
    • Stephenson, K. &Hoch, J.A. Evolution of signalling in the sporulation phosphorelay. Mol. Microbiol. 46, 297-304 (2002).
    • (2002) Mol. Microbiol , vol.46 , pp. 297-304
    • Stephenson, K.1    Hoch, J.A.2
  • 16
    • 0033531944 scopus 로고    scopus 로고
    • Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA
    • Nakamura, K., Yahagi, S., Yamazaki, T. &Yamane, K. Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA. J. Biol. Chem. 274, 13569-13576 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 13569-13576
    • Nakamura, K.1    Yahagi, S.2    Yamazaki, T.3    Yamane, K.4
  • 17
    • 0033614458 scopus 로고    scopus 로고
    • Depletion of Bacillus subtilis histone-like protein, HBsu, causes defective protein translocation and induces upregulation of small cytoplasmic RNA
    • Yamazaki, T., Yahagi, S., Nakamura, K. &Yamane, K. Depletion of Bacillus subtilis histone-like protein, HBsu, causes defective protein translocation and induces upregulation of small cytoplasmic RNA. Biochem. Biophys. Res. Commun. 258, 211-214 (1999).
    • (1999) Biochem. Biophys. Res. Commun , vol.258 , pp. 211-214
    • Yamazaki, T.1    Yahagi, S.2    Nakamura, K.3    Yamane, K.4
  • 18
    • 84866857051 scopus 로고    scopus 로고
    • Multisite ribosomal stalling: A unique mode of regulatory nascent chain action revealed for MifM
    • Chiba, S. &Ito, K. Multisite ribosomal stalling: a unique mode of regulatory nascent chain action revealed for MifM. Mol. Cell 47, 863-872 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 863-872
    • Chiba, S.1    Ito, K.2
  • 19
    • 84928475949 scopus 로고    scopus 로고
    • Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling
    • Sohmen, D. et al. Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling. Nat. Commun. 6, 6941 (2015).
    • (2015) Nat. Commun , vol.6 , pp. 6941
    • Sohmen, D.1
  • 20
    • 2942561968 scopus 로고    scopus 로고
    • Proteomics of protein secretion by Bacillus subtilis: Separating the "secrets" of the secretome
    • Tjalsma, H. et al. Proteomics of protein secretion by Bacillus subtilis: separating the "secrets" of the secretome. Microbiol. Mol. Biol. Rev. 68, 207-233 (2004).
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 207-233
    • Tjalsma, H.1
  • 21
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H., Bolhuis, A., Jongbloed, J.D., Bron, S. &van Dijl, J.M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64, 515-547 (2000).
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    Van Dijl, J.M.5
  • 22
    • 0024571667 scopus 로고
    • Species-specific variation in signal peptide design Implications for protein secretion in foreign hosts
    • von Heijne, G. &Abrahmsen, L. Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts. FEBS Lett. 244, 439-446 (1989).
    • (1989) FEBS Lett , vol.244 , pp. 439-446
    • Von Heijne, G.1    Abrahmsen, L.2
  • 23
    • 33745683590 scopus 로고    scopus 로고
    • Proteomic dissection of potential signal recognition particle dependence in protein secretion by Bacillus subtilis
    • Zanen, G. et al. Proteomic dissection of potential signal recognition particle dependence in protein secretion by Bacillus subtilis. Proteomics 6, 3636-3648 (2006).
    • (2006) Proteomics , vol.6 , pp. 3636-3648
    • Zanen, G.1
  • 24
    • 0027523180 scopus 로고
    • Titration of protein-transport activity by incremental changes in signal peptide hydrophobicity
    • Doud, S.K., Chou, M.M. &Kendall, D.A. Titration of protein-transport activity by incremental changes in signal peptide hydrophobicity. Biochemistry 32, 1251-1256 (1993).
    • (1993) Biochemistry , vol.32 , pp. 1251-1256
    • Doud, S.K.1    Chou, M.M.2    Kendall, D.A.3
  • 25
    • 84870817496 scopus 로고    scopus 로고
    • Dynamic switch of the signal recognition particle from scanning to targeting
    • Holtkamp, W. et al. Dynamic switch of the signal recognition particle from scanning to targeting. Nat. Struct. Mol. Biol. 19, 1332-1337 (2012).
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 1332-1337
    • Holtkamp, W.1
  • 26
    • 0025260974 scopus 로고
    • Escherichia coli 4.5s RNA gene-function can be complemented by heterologous bacterial RNA genes
    • Struck, J.C.R., Lempicki, R.A., Toschka, H.Y., Erdmann, V.A. &Fournier, M.J. Escherichia coli 4.5s RNA gene-function can be complemented by heterologous bacterial RNA genes. J. Bacteriol. 172, 1284-1288 (1990).
    • (1990) J. Bacteriol , vol.172 , pp. 1284-1288
    • Struck, J.C.R.1    Lempicki, R.A.2    Toschka, H.Y.3    Erdmann, V.A.4    Fournier, M.J.5
  • 27
    • 0028009958 scopus 로고
    • Structural Requirements of Bacillus subtilis small cytoplasmic RNA for cell-growth, sporulation, and extracellular enzyme-production
    • Nishiguchi, M., Honda, K., Amikura, R., Nakamura, K. &Yamane, K. Structural Requirements of Bacillus subtilis small cytoplasmic RNA for cell-growth, sporulation, and extracellular enzyme-production. J. Bacteriol. 176, 157-165 (1994).
    • (1994) J. Bacteriol , vol.176 , pp. 157-165
    • Nishiguchi, M.1    Honda, K.2    Amikura, R.3    Nakamura, K.4    Yamane, K.5
  • 28
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason, N., Ciufo, L.F. &Brown, J.D. Elongation arrest is a physiologically important function of signal recognition particle. EMBO J. 19, 4164-4174 (2000).
    • (2000) EMBO J , vol.19 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, J.D.3
  • 29
    • 0019822645 scopus 로고
    • Translocation of proteins across the endoplasmic-reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal-membranes
    • Walter, P. &Blobel, G. Translocation of proteins across the endoplasmic-reticulum. III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal-membranes. J. Cell Biol. 91, 557-561 (1981).
    • (1981) J. Cell Biol , vol.91 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 30
    • 0019817924 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein
    • Walter, P. &Blobel, G. Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein. J. Cell Biol. 91, 551-556 (1981).
    • (1981) J. Cell Biol , vol.91 , pp. 551-556
    • Walter, P.1    Blobel, G.2
  • 31
    • 0019849075 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein
    • Walter, P., Ibrahimi, I. &Blobel, G. 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, 545-550 (1981).
    • (1981) J. Cell Biol , vol.91 , pp. 545-550
    • Walter, P.1    Ibrahimi, I.2    Blobel, G.3
  • 32
    • 0024817509 scopus 로고
    • Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate
    • Wolin, S.L. &Walter, P. Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J. Cell Biol. 109, 2617-2622 (1989).
    • (1989) J. Cell Biol , vol.109 , pp. 2617-2622
    • Wolin, S.L.1    Walter, P.2
  • 33
    • 84869216020 scopus 로고    scopus 로고
    • Both YidC and SecYEG are required for translocation of the periplasmic loops 1 and 2 of the multispanning membrane protein TatC
    • Zhu, L., Klenner, C., Kuhn, A. &Dalbey, R.E. Both YidC and SecYEG are required for translocation of the periplasmic loops 1 and 2 of the multispanning membrane protein TatC. J. Mol. Biol. 424, 354-367 (2012).
    • (2012) J. Mol. Biol , vol.424 , pp. 354-367
    • Zhu, L.1    Klenner, C.2    Kuhn, A.3    Dalbey, R.E.4
  • 34
    • 79951826865 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle in complex with its receptor
    • Ataide, S.F. et al. The crystal structure of the signal recognition particle in complex with its receptor. Science 331, 881-886 (2011).
    • (2011) Science , vol.331 , pp. 881-886
    • Ataide, S.F.1
  • 35
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey, R.T., Rambo, R.P., Lucast, L., Rha, B. &Doudna, J.A. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287, 1232-1239 (2000).
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 36
    • 77955405123 scopus 로고    scopus 로고
    • Assemble: An interactive graphical tool to analyze and build RNA architectures at the 2D and 3D levels
    • Jossinet, F., Ludwig, T.E. &Westhof, E. Assemble: an interactive graphical tool to analyze and build RNA architectures at the 2D and 3D levels. Bioinformatics 26, 2057-2059 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 2057-2059
    • Jossinet, F.1    Ludwig, T.E.2    Westhof, E.3
  • 37
    • 33646442605 scopus 로고    scopus 로고
    • Signal recognition particle receptor exposes the ribosomal translocon binding site
    • Halic, M. et al. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science 312, 745-747 (2006).
    • (2006) Science , vol.312 , pp. 745-747
    • Halic, M.1
  • 38
    • 84897545031 scopus 로고    scopus 로고
    • SRP RNA remodeling by SRP68 explains its role in protein translocation
    • Grotwinkel, J.T., Wild, K., Segnitz, B. &Sinning, I. SRP RNA remodeling by SRP68 explains its role in protein translocation. Science 344, 101-104 (2014).
    • (2014) Science , vol.344 , pp. 101-104
    • Grotwinkel, J.T.1    Wild, K.2    Segnitz, B.3    Sinning, I.4
  • 39
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • Halic, M. et al. Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 444, 507-511 (2006).
    • (2006) Nature , vol.444 , pp. 507-511
    • Halic, M.1
  • 40
    • 77953025666 scopus 로고    scopus 로고
    • Recognition of a signal peptide by the signal recognition particle
    • Janda, C.Y. et al. Recognition of a signal peptide by the signal recognition particle. Nature 465, 507-510 (2010).
    • (2010) Nature , vol.465 , pp. 507-510
    • Janda, C.Y.1
  • 42
    • 84890165372 scopus 로고    scopus 로고
    • The structural basis of FtsY recruitment and GTPase activation by SRP RNA
    • Voigts-Hoffmann, F. et al. The structural basis of FtsY recruitment and GTPase activation by SRP RNA. Mol. Cell 52, 643-654 (2013).
    • (2013) Mol. Cell , vol.52 , pp. 643-654
    • Voigts-Hoffmann, F.1
  • 43
    • 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
  • 44
    • 84902330606 scopus 로고    scopus 로고
    • Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting
    • Saraogi, I., Akopian, D. &Shan, S.O. Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting. J. Cell Biol. 205, 693-706 (2014).
    • (2014) J. Cell Biol , vol.205 , pp. 693-706
    • Saraogi, I.1    Akopian, D.2    Shan, S.O.3
  • 45
    • 79955005771 scopus 로고    scopus 로고
    • Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting
    • Shen, K., Zhang, X. &Shan, S.O. Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting. RNA 17, 892-902 (2011).
    • (2011) RNA , vol.17 , pp. 892-902
    • Shen, K.1    Zhang, X.2    Shan, S.O.3
  • 46
    • 84890165372 scopus 로고    scopus 로고
    • The structural basis of FtsY recruitment and GTPase activation by SRP RNA
    • Voigts-Hoffmann, F. et al. The structural basis of FtsY recruitment and GTPase activation by SRP RNA. Mol. Cell 52, 643-654 (2013).
    • (2013) Mol. Cell , vol.52 , pp. 643-654
    • Voigts-Hoffmann, F.1
  • 47
    • 77952127782 scopus 로고    scopus 로고
    • Sequential checkpoints govern substrate selection during cotranslational protein targeting
    • Zhang, X., Rashid, R., Wang, K. &Shan, S.O. Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science 328, 757-760 (2010).
    • (2010) Science , vol.328 , pp. 757-760
    • Zhang, X.1    Rashid, R.2    Wang, K.3    Shan, S.O.4
  • 48
    • 60549083291 scopus 로고    scopus 로고
    • Multiple conformational switches in a GTPase complex control co-translational protein targeting
    • Zhang, X., Schaffitzel, C., Ban, N. &Shan, S.O. Multiple conformational switches in a GTPase complex control co-translational protein targeting. Proc. Natl. Acad. Sci. USA 106, 1754-1759 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1754-1759
    • Zhang, X.1    Schaffitzel, C.2    Ban, N.3    Shan, S.O.4
  • 49
    • 80053594659 scopus 로고    scopus 로고
    • RNase y in Bacillus subtilis: A natively disordered protein that is the functional equivalent of RNase e from Escherichia coli
    • Lehnik-Habrink, M. et al. RNase Y in Bacillus subtilis: a natively disordered protein that is the functional equivalent of RNase E from Escherichia coli. J. Bacteriol. 193, 5431-5441 (2011).
    • (2011) J. Bacteriol , vol.193 , pp. 5431-5441
    • Lehnik-Habrink, M.1
  • 50
    • 85003044155 scopus 로고    scopus 로고
    • A structural model of the active ribosome-bound membrane protein insertase YidC
    • Wickles, S. et al. A structural model of the active ribosome-bound membrane protein insertase YidC. eLife 3, e03035 (2014).
    • (2014) ELife , vol.3 , pp. e03035
    • Wickles, S.1
  • 51
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., Rasband, W.S. &Eliceiri, K.W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 52
    • 33845449481 scopus 로고    scopus 로고
    • SIGNATURE: A single-particle selection system for molecular electron microscopy
    • Chen, J.Z. &Grigorieff, N. SIGNATURE: a single-particle selection system for molecular electron microscopy. J. Struct. Biol. 157, 168-173 (2007).
    • (2007) J. Struct. Biol , vol.157 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 53
    • 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
  • 54
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S.H. &Chen, S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 9, 853-854 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 55
    • 51549084591 scopus 로고    scopus 로고
    • Sharpening high resolution information in single particle electron cryomicroscopy
    • Fernández, J.J., Luque, D., Caston, J.R. &Carrascosa, J.L. Sharpening high resolution information in single particle electron cryomicroscopy. J. Struct. Biol. 164, 170-175 (2008).
    • (2008) J. Struct. Biol , vol.164 , pp. 170-175
    • Fernández, J.J.1    Luque, D.2    Caston, J.R.3    Carrascosa, J.L.4
  • 56
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 57
    • 84899967993 scopus 로고    scopus 로고
    • 2dx-automator: Implementation of a semiautomatic high-throughput high-resolution cryo-electron crystallography pipeline
    • Scherer, S. et al. 2dx-automator: implementation of a semiautomatic high-throughput high-resolution cryo-electron crystallography pipeline. J. Struct. Biol. 186, 302-307 (2014).
    • (2014) J. Struct. Biol , vol.186 , pp. 302-307
    • Scherer, S.1
  • 58
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera: a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.