메뉴 건너뛰기




Volumn 528, Issue 7581, 2015, Pages 231-236

Molecular structures of unbound and transcribing RNA polymerase III

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE III; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84949797800     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature16143     Document Type: Article
Times cited : (141)

References (73)
  • 2
    • 56649105133 scopus 로고    scopus 로고
    • RNA polymerases i and III, non-coding RNAs and cancer
    • White, R. J. RNA polymerases I and III, non-coding RNAs and cancer. Trends Genet. 24, 622-629 (2008).
    • (2008) Trends Genet. , vol.24 , pp. 622-629
    • White, R.J.1
  • 3
    • 84857423235 scopus 로고    scopus 로고
    • Conservation between the RNA polymerase I, II, and III transcription initiation machineries
    • Vannini, A. and Cramer, P. Conservation between the RNA polymerase I, II, and III transcription initiation machineries. Mol. Cell 45, 439-446 (2012).
    • (2012) Mol. Cell , vol.45 , pp. 439-446
    • Vannini, A.1    Cramer, P.2
  • 4
    • 84937596472 scopus 로고    scopus 로고
    • Mechanism of transcription termination by RNA polymerase III utilizes a non-template strand sequence-specific signal element
    • Arimbasseri, A. G. and Maraia, R. J. Mechanism of transcription termination by RNA polymerase III utilizes a non-template strand sequence-specific signal element. Mol. Cell 58, 1124-1132 (2015).
    • (2015) Mol. Cell , vol.58 , pp. 1124-1132
    • Arimbasseri, A.G.1    Maraia, R.J.2
  • 5
    • 0032535546 scopus 로고    scopus 로고
    • The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination
    • Chedin, S., Riva, M., Schultz, P., Sentenac, A. and Carles, C. The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev. 12, 3857-3871 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3857-3871
    • Chedin, S.1    Riva, M.2    Schultz, P.3    Sentenac, A.4    Carles, C.5
  • 6
    • 70549090264 scopus 로고    scopus 로고
    • Structure-function analysis of RNA polymerases i and III
    • Werner, M., Thuriaux, P. and Soutourina, J. Structure-function analysis of RNA polymerases I and III. Curr. Opin. Struct. Biol. 19, 740-745 (2009).
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 740-745
    • Werner, M.1    Thuriaux, P.2    Soutourina, J.3
  • 7
    • 33745499068 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: Subcomplex C17/25 X-ray structure and 11 subunit enzyme model
    • Jasiak, A. J., Armache, K. J., Martens, B., Jansen, R. P. and Cramer, P. Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model. Mol. Cell 23, 71-81 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 71-81
    • Jasiak, A.J.1    Armache, K.J.2    Martens, B.3    Jansen, R.P.4    Cramer, P.5
  • 8
    • 77449109937 scopus 로고    scopus 로고
    • The C53/C37 subcomplex of RNA polymerase III lies near the active site and participates in promoter opening
    • Kassavetis, G. A., Prakash, P. and Shim, E. The C53/C37 subcomplex of RNA polymerase III lies near the active site and participates in promoter opening. J. Biol. Chem. 285, 2695-2706 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 2695-2706
    • Kassavetis, G.A.1    Prakash, P.2    Shim, E.3
  • 9
    • 30444450804 scopus 로고    scopus 로고
    • A subcomplex of RNA polymerase III subunits involved in transcription termination and reinitiation
    • Landrieux, E. et al. A subcomplex of RNA polymerase III subunits involved in transcription termination and reinitiation. EMBO J. 25, 118-128 (2006).
    • (2006) EMBO J. , vol.25 , pp. 118-128
    • Landrieux, E.1
  • 10
    • 77951608945 scopus 로고    scopus 로고
    • The increase in the number of subunits in eukaryotic RNA polymerase III relative to RNA polymerase II is due to the permanent recruitment of general transcription factors
    • Carter, R. and Drouin, G. The increase in the number of subunits in eukaryotic RNA polymerase III relative to RNA polymerase II is due to the permanent recruitment of general transcription factors. Mol. Biol. Evol. 27, 1035-1043 (2010).
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 1035-1043
    • Carter, R.1    Drouin, G.2
  • 11
    • 77955993009 scopus 로고    scopus 로고
    • RNA polymerase i contains a TFIIF-related DNA-binding subcomplex
    • Geiger, S. R. et al. RNA polymerase I contains a TFIIF-related DNA-binding subcomplex. Mol. Cell 39, 583-594 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 583-594
    • Geiger, S.R.1
  • 12
    • 33947369108 scopus 로고    scopus 로고
    • Insights into transcription initiation and termination from the electron microscopy structure of yeast RNA polymerase III
    • Fernandez-Tornero, C. et al. Insights into transcription initiation and termination from the electron microscopy structure of yeast RNA polymerase III. Mol. Cell 25, 813-823 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 813-823
    • Fernandez-Tornero, C.1
  • 13
    • 79959407310 scopus 로고    scopus 로고
    • The TFIIF-like Rpc37/53 dimer lies at the center of a protein network to connect TFIIIC, Bdp1, and the RNA polymerase III active center
    • Wu, C. C., Lin, Y. C. and Chen, H. T. The TFIIF-like Rpc37/53 dimer lies at the center of a protein network to connect TFIIIC, Bdp1, and the RNA polymerase III active center. Mol. Cell. Biol. 31, 2715-2728 (2011).
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2715-2728
    • Wu, C.C.1    Lin, Y.C.2    Chen, H.T.3
  • 14
    • 78651245123 scopus 로고    scopus 로고
    • Mass spectrometry reveals stable modules in holo and apo RNA polymerases i and III
    • Lane, L. A. et al. Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III. Structure 19, 90-100 (2011).
    • (2011) Structure , vol.19 , pp. 90-100
    • Lane, L.A.1
  • 15
    • 0030998344 scopus 로고    scopus 로고
    • Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation
    • Wang, Z. and Roeder, R. G. Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation. Genes Dev. 11, 1315-1326 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 1315-1326
    • Wang, Z.1    Roeder, R.G.2
  • 16
    • 84869830300 scopus 로고    scopus 로고
    • RNA polymerase III subunit architecture and implications for open promoter complex formation
    • Wu, C. C. et al. RNA polymerase III subunit architecture and implications for open promoter complex formation. Proc. Natl Acad. Sci. USA 109, 19232-19237 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 19232-19237
    • Wu, C.C.1
  • 17
    • 0028872606 scopus 로고
    • A mutation in the C31 subunit of Saccharomyces cerevisiae RNA polymerase III affects transcription initiation
    • Thuillier, V., Stettler, S., Sentenac, A., Thuriaux, P. and Werner, M. A mutation in the C31 subunit of Saccharomyces cerevisiae RNA polymerase III affects transcription initiation. EMBO J. 14, 351-359 (1995).
    • (1995) EMBO J. , vol.14 , pp. 351-359
    • Thuillier, V.1    Stettler, S.2    Sentenac, A.3    Thuriaux, P.4    Werner, M.5
  • 18
    • 0030766849 scopus 로고    scopus 로고
    • Dual role of the C34 subunit of RNA polymerase III in transcription initiation
    • Brun, I., Sentenac, A. and Werner, M. Dual role of the C34 subunit of RNA polymerase III in transcription initiation. EMBO J. 16, 5730-5741 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5730-5741
    • Brun, I.1    Sentenac, A.2    Werner, M.3
  • 19
    • 84892456826 scopus 로고    scopus 로고
    • Mapping the protein interaction network for TFIIB-related factor Brf1 in the RNA polymerase III preinitiation complex
    • Khoo, S. K., Wu, C. C., Lin, Y. C., Lee, J. C. and Chen, H. T. Mapping the protein interaction network for TFIIB-related factor Brf1 in the RNA polymerase III preinitiation complex. Mol. Cell. Biol. 34, 551-559 (2014).
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 551-559
    • Khoo, S.K.1    Wu, C.C.2    Lin, Y.C.3    Lee, J.C.4    Chen, H.T.5
  • 20
    • 84875236968 scopus 로고    scopus 로고
    • Maf1, a general negative regulator of RNA polymerase III in yeast
    • Boguta, M. Maf1, a general negative regulator of RNA polymerase III in yeast. Biochim. Biophys. Acta 1829, 376-384 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 376-384
    • Boguta, M.1
  • 21
    • 77957222055 scopus 로고    scopus 로고
    • Molecular basis of RNA polymerase III transcription repression by Maf1
    • Vannini, A. et al. Molecular basis of RNA polymerase III transcription repression by Maf1. Cell 143, 59-70 (2010).
    • (2010) Cell , vol.143 , pp. 59-70
    • Vannini, A.1
  • 22
    • 84923804845 scopus 로고    scopus 로고
    • Structural basis of transcription initiation by RNA polymerase II
    • Sainsbury, S., Bernecky, C. and Cramer, P. Structural basis of transcription initiation by RNA polymerase II. Nature Rev. Mol. Cell Biol. 16, 129-143 (2015).
    • (2015) Nature Rev. Mol. Cell Biol. , vol.16 , pp. 129-143
    • Sainsbury, S.1    Bernecky, C.2    Cramer, P.3
  • 23
    • 84872376551 scopus 로고    scopus 로고
    • Basic mechanism of transcription by RNA polymerase II
    • Svetlov, V. and Nudler, E. Basic mechanism of transcription by RNA polymerase II. Biochim. Biophys. Acta 1829, 20-28 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 20-28
    • Svetlov, V.1    Nudler, E.2
  • 24
    • 84886947664 scopus 로고    scopus 로고
    • Crystal structure of the 14-subunit RNA polymerase i
    • Fernandez-Tornero, C. et al. Crystal structure of the 14-subunit RNA polymerase I. Nature 502, 644-649 (2013).
    • (2013) Nature , vol.502 , pp. 644-649
    • Fernandez-Tornero, C.1
  • 25
    • 84886948058 scopus 로고    scopus 로고
    • RNA polymerase i structure and transcription regulation
    • Engel, C., Sainsbury, S., Cheung, A. C., Kostrewa, D. and Cramer, P. RNA polymerase I structure and transcription regulation. Nature 502, 650-655 (2013).
    • (2013) Nature , vol.502 , pp. 650-655
    • Engel, C.1    Sainsbury, S.2    Cheung, A.C.3    Kostrewa, D.4    Cramer, P.5
  • 26
    • 78449300336 scopus 로고    scopus 로고
    • Conformational flexibility of RNA polymerase III during transcriptional elongation
    • Fernandez-Tornero, C. et al. Conformational flexibility of RNA polymerase III during transcriptional elongation. EMBO J. 29, 3762-3772 (2010).
    • (2010) EMBO J. , vol.29 , pp. 3762-3772
    • Fernandez-Tornero, C.1
  • 27
    • 84907811433 scopus 로고    scopus 로고
    • Solving the RNA polymerase i structural puzzle
    • Moreno-Morcillo, M. et al. Solving the RNA polymerase I structural puzzle. Acta Crystallogr. D 70, 2570-2582 (2014).
    • (2014) Acta Crystallogr. D , vol.70 , pp. 2570-2582
    • Moreno-Morcillo, M.1
  • 28
    • 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
  • 29
    • 84937422854 scopus 로고    scopus 로고
    • Crystal structure of a transcribing RNA polymerase II complex reveals a complete transcription bubble
    • Barnes, C. O. et al. Crystal structure of a transcribing RNA polymerase II complex reveals a complete transcription bubble. Mol. Cell 59, 258-269 (2015).
    • (2015) Mol. Cell , vol.59 , pp. 258-269
    • Barnes, C.O.1
  • 30
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3A resolution
    • Gnatt, A. L., Cramer, P., Fu, J., Bushnell, D. A. and Kornberg, R. D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3A resolution. Science 292, 1876-1882 (2001).
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 31
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • Kettenberger, H., Armache, K. J. and Cramer, P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol. Cell 16, 955-965 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 32
    • 79952360458 scopus 로고    scopus 로고
    • Structure-function analysis of hRPC62 provides insights into RNA polymerase III transcription initiation
    • Lefevre, S. et al. Structure-function analysis of hRPC62 provides insights into RNA polymerase III transcription initiation. Nature Struct. Mol. Biol. 18, 352-358 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 352-358
    • Lefevre, S.1
  • 33
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: Transcription regulation and beyond
    • Aravind, L., Anantharaman, V., Balaji, S., Babu, M. M. and Iyer, L. M. The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol. Rev. 29, 231-262 (2005).
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 231-262
    • Aravind, L.1    Anantharaman, V.2    Balaji, S.3    Babu, M.M.4    Iyer, L.M.5
  • 34
    • 84875613843 scopus 로고    scopus 로고
    • Structural visualization of key steps in human transcription initiation
    • He, Y., Fang, J., Taatjes, D. J. and Nogales, E. Structural visualization of key steps in human transcription initiation. Nature 495, 481-486 (2013).
    • (2013) Nature , vol.495 , pp. 481-486
    • He, Y.1    Fang, J.2    Taatjes, D.J.3    Nogales, E.4
  • 35
    • 0037108150 scopus 로고    scopus 로고
    • Recruitment of RNA polymerase III to its target promoters
    • Schramm, L. and Hernandez, N. Recruitment of RNA polymerase III to its target promoters. Genes Dev. 16, 2593-2620 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2593-2620
    • Schramm, L.1    Hernandez, N.2
  • 36
    • 0033970934 scopus 로고    scopus 로고
    • A novel subunit of yeast RNA polymerase III interacts with the TFIIB-related domain of TFIIIB70
    • Ferri, M. L. et al. A novel subunit of yeast RNA polymerase III interacts with the TFIIB-related domain of TFIIIB70. Mol. Cell. Biol. 20, 488-495 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 488-495
    • Ferri, M.L.1
  • 37
    • 84923358406 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-Mediator core initiation complex
    • Plaschka, C. et al. Architecture of the RNA polymerase II-Mediator core initiation complex. Nature 518, 376-380 (2015).
    • (2015) Nature , vol.518 , pp. 376-380
    • Plaschka, C.1
  • 38
    • 84900405636 scopus 로고    scopus 로고
    • Comparative overview of RNA polymerase II and III transcription cycles, with focus on RNA polymerase III termination and reinitiation
    • Arimbasseri, A. G., Rijal, K. and Maraia, R. J. Comparative overview of RNA polymerase II and III transcription cycles, with focus on RNA polymerase III termination and reinitiation. Transcription 5, e27369 (2014).
    • (2014) Transcription , vol.5 , pp. e27369
    • Arimbasseri, A.G.1    Rijal, K.2    Maraia, R.J.3
  • 39
    • 84937948775 scopus 로고    scopus 로고
    • A region of Bdp1 necessary for transcription initiation that is located within the RNA polymerase III active site cleft
    • Hu, H. L., Wu, C. C., Lee, J. C. and Chen, H. T. A region of Bdp1 necessary for transcription initiation that is located within the RNA polymerase III active site cleft. Mol. Cell. Biol. 35, 2831-2840 (2015).
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 2831-2840
    • Hu, H.L.1    Wu, C.C.2    Lee, J.C.3    Chen, H.T.4
  • 40
    • 84871727963 scopus 로고    scopus 로고
    • RNA polymerase III mutants in TFIIFα -like C37 that cause terminator readthrough with no decrease in transcription output
    • Rijal, K. and Maraia, R. J. RNA polymerase III mutants in TFIIFα -like C37 that cause terminator readthrough with no decrease in transcription output. Nucleic Acids Res. 41, 139-155 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 139-155
    • Rijal, K.1    Maraia, R.J.2
  • 41
    • 0028804625 scopus 로고
    • Termination-altering mutations in the second-largest subunit of yeast RNA polymerase III
    • Shaaban, S. A., Krupp, B. M. and Hall, B. D. Termination-altering mutations in the second-largest subunit of yeast RNA polymerase III. Mol. Cell. Biol. 15, 1467-1478 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1467-1478
    • Shaaban, S.A.1    Krupp, B.M.2    Hall, B.D.3
  • 42
    • 66149187105 scopus 로고    scopus 로고
    • Transcription termination by nuclear RNA polymerases
    • Richard, P. and Manley, J. L. Transcription termination by nuclear RNA polymerases. Genes Dev. 23, 1247-1269 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 1247-1269
    • Richard, P.1    Manley, J.L.2
  • 43
    • 0028144691 scopus 로고
    • Hydrolytic cleavage of nascent RNA in RNA polymerase III ternary transcription complexes
    • Whitehall, S. K., Bardeleben, C. and Kassavetis, G. A. Hydrolytic cleavage of nascent RNA in RNA polymerase III ternary transcription complexes. J. Biol. Chem. 269, 2299-2306 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 2299-2306
    • Whitehall, S.K.1    Bardeleben, C.2    Kassavetis, G.A.3
  • 44
    • 80051763224 scopus 로고    scopus 로고
    • Point mutations in the Rpb9-homologous domain of Rpc11 that impair transcription termination by RNA polymerase III
    • Iben, J. R. et al. Point mutations in the Rpb9-homologous domain of Rpc11 that impair transcription termination by RNA polymerase III. Nucleic Acids Res. 39, 6100-6113 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6100-6113
    • Iben, J.R.1
  • 45
    • 84860408300 scopus 로고    scopus 로고
    • Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA polymerase III
    • Ehara, H., Sekine, S. and Yokoyama, S. Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA polymerase III. Protein Sci. 20, 1558-1565 (2011).
    • (2011) Protein Sci. , vol.20 , pp. 1558-1565
    • Ehara, H.1    Sekine, S.2    Yokoyama, S.3
  • 46
    • 84864770299 scopus 로고    scopus 로고
    • Opening and closing of the bacterial RNA polymerase clamp
    • Chakraborty, A. et al. Opening and closing of the bacterial RNA polymerase clamp. Science 337, 591-595 (2012).
    • (2012) Science , vol.337 , pp. 591-595
    • Chakraborty, A.1
  • 47
    • 84938592009 scopus 로고    scopus 로고
    • The X-ray crystal structure of the euryarchaeal RNA polymerase in an open-clamp configuration
    • Jun, S. H. et al. The X-ray crystal structure of the euryarchaeal RNA polymerase in an open-clamp configuration. Nature Commun. 5, 5132 (2014).
    • (2014) Nature Commun. , vol.5 , pp. 5132
    • Jun, S.H.1
  • 48
    • 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. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 49
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J. A. and Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 50
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R. and Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 51
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S. H. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 3, e03665 (2014).
    • (2014) ELife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 52
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel, M. and Schatz, M. Fourier shell correlation threshold criteria. J. Struct. Biol. 151, 250-262 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 53
    • 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
  • 54
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. and Henderson, R. Optimal determination of particle orientation, absolute hand, and 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
  • 55
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. and Tagare, H. 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, F.J.2    Tagare, H.D.3
  • 56
    • 84875627549 scopus 로고    scopus 로고
    • MODexplorer: An integrated tool for exploring protein sequence, structure and function relationships
    • Kosinski, J., Barbato, A. and Tramontano, A. MODexplorer: an integrated tool for exploring protein sequence, structure and function relationships. Bioinformatics 29, 953-954 (2013).
    • (2013) Bioinformatics , vol.29 , pp. 953-954
    • Kosinski, J.1    Barbato, A.2    Tramontano, A.3
  • 57
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding, J. Protein homology detection by HMM-HMM comparison. Bioinformatics 21, 951-960 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 58
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 59
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 60
    • 84923290002 scopus 로고    scopus 로고
    • Xlink Analyzer: Software for analysis and visualization of cross-linking data in the context of three-dimensional structures
    • Kosinski, J. et al. Xlink Analyzer: software for analysis and visualization of cross-linking data in the context of three-dimensional structures. J. Struct. Biol. 189, 177-183 (2015).
    • (2015) J. Struct. Biol. , vol.189 , pp. 177-183
    • Kosinski, J.1
  • 61
    • 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
  • 62
    • 84890101190 scopus 로고    scopus 로고
    • Integrated structural analysis of the human nuclear pore complex scaffold
    • Bui, K. H. et al. Integrated structural analysis of the human nuclear pore complex scaffold. Cell 155, 1233-1243 (2013).
    • (2013) Cell , vol.155 , pp. 1233-1243
    • Bui, K.H.1
  • 63
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T. and Ben-Tal, N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 64
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 65
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 66
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding, M. M. Geometry of metal-ligand interactions in proteins. Acta Crystallogr. D 57, 401-411 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 67
    • 33744502092 scopus 로고    scopus 로고
    • Small revisions to predicted distances around metal sites in proteins
    • Harding, M. M. Small revisions to predicted distances around metal sites in proteins. Acta Crystallogr. D 62, 678-682 (2006).
    • (2006) Acta Crystallogr. D , vol.62 , pp. 678-682
    • Harding, M.M.1
  • 68
    • 84880584062 scopus 로고    scopus 로고
    • (ed Prince, E.) (International Union of Crystallography
    • Colliex, C. et al. in International Tables of Crystallography Vol. C (ed Prince, E.), 259-429 (International Union of Crystallography, 2006).
    • (2006) International Tables of Crystallography , vol.C , pp. 259-429
    • Colliex, C.1
  • 69
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: A fresh look at tobacco mosaic virus
    • Sachse, C. et al. High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J. Mol. Biol. 371, 812-835 (2007).
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1
  • 70
    • 84881282403 scopus 로고    scopus 로고
    • Cryo-EM model validation using independent map reconstructions
    • DiMaio, F., Zhang, J., Chiu, W. and Baker, D. Cryo-EM model validation using independent map reconstructions. Protein Sci. 22, 865-868 (2013).
    • (2013) Protein Sci. , vol.22 , pp. 865-868
    • DiMaio, F.1    Zhang, J.2    Chiu, W.3    Baker, D.4
  • 71
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J. S. and Brunger, A. T. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115 (1994).
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 72
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.