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Volumn 6, Issue , 2015, Pages

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE III; TRANSCRIPTION FACTOR 3; TRANSCRIPTION FACTOR IIIC; TRANSFER RNA; UNCLASSIFIED DRUG; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR III; TRANSCRIPTION FACTOR TFIIIC;

EID: 84931275345     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8387     Document Type: Article
Times cited : (53)

References (51)
  • 1
    • 0037108150 scopus 로고    scopus 로고
    • Recruitment of RNA polymerase III to its target promoters
    • Schramm, L. & 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
  • 2
    • 0025055216 scopus 로고
    • Cerevisiae TFIIIB is the transcription initiation factor proper of RNA polymerase III, while TFIIIA and TFIIIC are assembly factors
    • Kassavetis, G. A., Braun, B. R., Nguyen, L. H. & Geiduschek, E. P. S. cerevisiae TFIIIB is the transcription initiation factor proper of RNA polymerase III, while TFIIIA and TFIIIC are assembly factors. Cell 60, 235-245 (1990).
    • (1990) Cell , vol.60 , pp. 235-245
    • Kassavetis, G.A.1    Braun, B.R.2    Nguyen, L.H.3    Geiduschek, E.P.S.4
  • 3
    • 0035967858 scopus 로고    scopus 로고
    • The RNA polymerase III transcription apparatus
    • Geiduschek, E. P. & Kassavetis, G. A. The RNA polymerase III transcription apparatus. J. Mol. Biol. 310, 1-26 (2001).
    • (2001) J. Mol. Biol. , vol.310 , pp. 1-26
    • Geiduschek, E.P.1    Kassavetis, G.A.2
  • 4
    • 0027295502 scopus 로고
    • On the subunit composition, stoichiometry, and phosphorylation of the yeast transcription factor TFIIIC/tau
    • Conesa, C., Swanson, R. N., Schultz, P., Oudet, P. & Sentenac, A. On the subunit composition, stoichiometry, and phosphorylation of the yeast transcription factor TFIIIC/tau. J. Biol. Chem. 268, 18047-18052 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 18047-18052
    • Conesa, C.1    Swanson, R.N.2    Schultz, P.3    Oudet, P.4    Sentenac, A.5
  • 5
    • 33744966027 scopus 로고    scopus 로고
    • Reconstitution of the yeast RNA polymerase III transcription system with all recombinant factors
    • Ducrot, C. et al. Reconstitution of the yeast RNA polymerase III transcription system with all recombinant factors. J. Biol. Chem. 281, 11685-11692 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 11685-11692
    • Ducrot, C.1
  • 6
    • 0021415340 scopus 로고
    • Differential binding of a S. Cerevisiae RNA polymerase III transcription factor to two promoter segments of a tRNA gene
    • Stillman, D. J. & Geiduschek, E. P. Differential binding of a S. cerevisiae RNA polymerase III transcription factor to two promoter segments of a tRNA gene. EMBO J. 3, 847-853 (1984).
    • (1984) EMBO J. , vol.3 , pp. 847-853
    • Stillman, D.J.1    Geiduschek, E.P.2
  • 7
    • 0023475623 scopus 로고
    • Gene size differentially affects the binding of yeast transcription factor tau to two intragenic regions
    • Baker, R. E., Camier, S., Sentenac, A. & Hall, B. D. Gene size differentially affects the binding of yeast transcription factor tau to two intragenic regions. Proc. Natl Acad. Sci. USA 84, 8768-8772 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8768-8772
    • Baker, R.E.1    Camier, S.2    Sentenac, A.3    Hall, B.D.4
  • 8
    • 84884962622 scopus 로고    scopus 로고
    • Global 'bootprinting' reveals the elastic architecture of the yeast TFIIIB-TFIIIC transcription complex in vivo
    • Nagarajavel, V., Iben, J. R., Howard, B. H., Maraia, R. J. & Clark, D. J. Global 'bootprinting' reveals the elastic architecture of the yeast TFIIIB-TFIIIC transcription complex in vivo. Nucleic Acids Res. 41, 8135-8143 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 8135-8143
    • Nagarajavel, V.1    Iben, J.R.2    Howard, B.H.3    Maraia, R.J.4    Clark, D.J.5
  • 9
    • 0023046997 scopus 로고
    • Selective proteolysis defines two DNA binding domains in yeast transcription factor tau
    • Marzouki, N., Camier, S., Ruet, A., Moenne, A. & Sentenac, A. Selective proteolysis defines two DNA binding domains in yeast transcription factor tau. Nature 323, 176-178 (1986).
    • (1986) Nature , vol.323 , pp. 176-178
    • Marzouki, N.1    Camier, S.2    Ruet, A.3    Moenne, A.4    Sentenac, A.5
  • 10
    • 0024840078 scopus 로고
    • The two DNA-binding domains of yeast transcription factor tau as observed by scanning transmission electron microscopy
    • Schultz, P. et al. The two DNA-binding domains of yeast transcription factor tau as observed by scanning transmission electron microscopy. EMBO J. 8, 3815-3824 (1989).
    • (1989) EMBO J. , vol.8 , pp. 3815-3824
    • Schultz, P.1
  • 11
    • 34447130248 scopus 로고    scopus 로고
    • Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC
    • Dumay-Odelot, H. et al. Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC. J. Biol. Chem. 282, 17179-17189 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 17179-17189
    • Dumay-Odelot, H.1
  • 12
    • 33750087881 scopus 로고    scopus 로고
    • Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: Insights into preinitiation complex assembly
    • Mylona, A. et al. Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: Insights into preinitiation complex assembly. Mol. Cell 24, 221-232 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 221-232
    • Mylona, A.1
  • 13
    • 84878228062 scopus 로고    scopus 로고
    • Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC
    • Taylor, N. M. et al. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. J. Biol. Chem. 288, 15110-15120 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 15110-15120
    • Taylor, N.M.1
  • 14
    • 84885990149 scopus 로고    scopus 로고
    • RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74
    • Taylor, N. M., Baudin, F., von Scheven, G. & Muller, C. W. RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74. Nucleic Acids Res. 41, 9183-9196 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 9183-9196
    • Taylor, N.M.1    Baudin, F.2    Von Scheven, G.3    Muller, C.W.4
  • 15
    • 0038532240 scopus 로고    scopus 로고
    • The tau95 subunit of yeast TFIIIC influences upstream and downstream functions of TFIIIC.DNA complexes
    • Jourdain, S., Acker, J., Ducrot, C., Sentenac, A. & Lefebvre, O. The tau95 subunit of yeast TFIIIC influences upstream and downstream functions of TFIIIC.DNA complexes. J. Biol. Chem. 278, 10450-10457 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 10450-10457
    • Jourdain, S.1    Acker, J.2    Ducrot, C.3    Sentenac, A.4    Lefebvre, O.5
  • 16
    • 0034893653 scopus 로고    scopus 로고
    • Genetic interactions within TFIIIC, the promoterbinding factor of yeast RNA polymerase III
    • Rozenfeld, S. & Thuriaux, P. Genetic interactions within TFIIIC, the promoterbinding factor of yeast RNA polymerase III. Mol. Genet. Genomics 265, 705-710 (2001).
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 705-710
    • Rozenfeld, S.1    Thuriaux, P.2
  • 17
    • 0025291547 scopus 로고
    • The subunit structure of Saccharomyces cerevisiae transcription factor IIIC probed with a novel photocrosslinking reagent
    • Bartholomew, B., Kassavetis, G. A., Braun, B. R. & Geiduschek, E. P. The subunit structure of Saccharomyces cerevisiae transcription factor IIIC probed with a novel photocrosslinking reagent. EMBO J. 9, 2197-2205 (1990).
    • (1990) EMBO J. , vol.9 , pp. 2197-2205
    • Bartholomew, B.1    Kassavetis, G.A.2    Braun, B.R.3    Geiduschek, E.P.4
  • 18
    • 0028016209 scopus 로고
    • A mutation in the largest subunit of yeast TFIIIC affects tRNA and 5 S RNA synthesis. Identification of two classes of suppressors
    • Lefebvre, O., Ruth, J. & Sentenac, A. A mutation in the largest subunit of yeast TFIIIC affects tRNA and 5 S RNA synthesis. Identification of two classes of suppressors. J. Biol. Chem. 269, 23374-23381 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 23374-23381
    • Lefebvre, O.1    Ruth, J.2    Sentenac, A.3
  • 19
    • 0036006513 scopus 로고    scopus 로고
    • Multiple roles of the tau131 subunit of yeast transcription factor IIIC (TFIIIC) in TFIIIB assembly
    • Dumay-Odelot, H., Acker, J., Arrebola, R., Sentenac, A. & Marck, C. Multiple roles of the tau131 subunit of yeast transcription factor IIIC (TFIIIC) in TFIIIB assembly. Mol. Cell. Biol. 22, 298-308 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 298-308
    • Dumay-Odelot, H.1    Acker, J.2    Arrebola, R.3    Sentenac, A.4    Marck, C.5
  • 20
    • 84857933257 scopus 로고    scopus 로고
    • Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module
    • Zeytuni, N. & Zarivach, R. Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module. Structure 20, 397-405 (2012).
    • (2012) Structure , vol.20 , pp. 397-405
    • Zeytuni, N.1    Zarivach, R.2
  • 21
    • 84882796823 scopus 로고    scopus 로고
    • The yeast ski complex: Crystal structure and RNA channeling to the exosome complex
    • Halbach, F., Reichelt, P., Rode, M. & Conti, E. The yeast ski complex: Crystal structure and RNA channeling to the exosome complex. Cell 154, 814-826 (2013).
    • (2013) Cell , vol.154 , pp. 814-826
    • Halbach, F.1    Reichelt, P.2    Rode, M.3    Conti, E.4
  • 22
    • 0242666313 scopus 로고    scopus 로고
    • The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to overlapping sites in the tetratricopeptide repeats of Tfc4
    • Liao, Y.,Willis, I. M. & Moir, R. D. The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to overlapping sites in the tetratricopeptide repeats of Tfc4. J. Biol. Chem. 278, 44467-44474 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 44467-44474
    • Liao, Y.1    Willis, I.M.2    Moir, R.D.3
  • 23
    • 0036337439 scopus 로고    scopus 로고
    • A gain-of-function mutation in the second tetratricopeptide repeat of TFIIIC131 relieves autoinhibition of Brf1 binding
    • Moir, R. D., Puglia, K. V. & Willis, I. M. A gain-of-function mutation in the second tetratricopeptide repeat of TFIIIC131 relieves autoinhibition of Brf1 binding. Mol. Cell. Biol. 22, 6131-6141 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6131-6141
    • Moir, R.D.1    Puglia, K.V.2    Willis, I.M.3
  • 24
    • 0037016692 scopus 로고    scopus 로고
    • Autoinhibition of TFIIIB70 binding by the tetratricopeptide repeat-containing subunit of TFIIIC
    • Moir, R. D., Puglia, K. V. & Willis, I. M. Autoinhibition of TFIIIB70 binding by the tetratricopeptide repeat-containing subunit of TFIIIC. J. Biol. Chem. 277, 694-701 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 694-701
    • Moir, R.D.1    Puglia, K.V.2    Willis, I.M.3
  • 25
    • 0034713936 scopus 로고    scopus 로고
    • Interactions between the tetratricopeptide repeat-containing transcription factor TFIIIC131 and its ligand TFIIIB70. Evidence for a conformational change in the complex
    • Moir, R. D., Puglia, K. V. & Willis, I. M. Interactions between the tetratricopeptide repeat-containing transcription factor TFIIIC131 and its ligand, TFIIIB70. Evidence for a conformational change in the complex. J. Biol. Chem. 275, 26591-26598 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26591-26598
    • Moir, R.D.1    Puglia, K.V.2    Willis, I.M.3
  • 26
    • 0030699094 scopus 로고    scopus 로고
    • A tetratricopeptide repeat mutation in yeast transcription factor IIIC131 (TFIIIC131) facilitates recruitment of TFIIB-related factor TFIIIB70
    • Moir, R. D., Sethy-Coraci, I., Puglia, K., Librizzi, M. D. & Willis, I. M. A tetratricopeptide repeat mutation in yeast transcription factor IIIC131 (TFIIIC131) facilitates recruitment of TFIIB-related factor TFIIIB70. Mol. Cell. Biol. 17, 7119-7125 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7119-7125
    • Moir, R.D.1    Sethy-Coraci, I.2    Puglia, K.3    Librizzi, M.D.4    Willis, I.M.5
  • 27
    • 33746970958 scopus 로고    scopus 로고
    • Interactions of Brf1 peptides with the tetratricopeptide repeat-containing subunit of TFIIIC inhibit and promote preinitiation complex assembly
    • Liao, Y., Moir, R. D. & Willis, I. M. Interactions of Brf1 peptides with the tetratricopeptide repeat-containing subunit of TFIIIC inhibit and promote preinitiation complex assembly. Mol. Cell. Biol. 26, 5946-5956 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5946-5956
    • Liao, Y.1    Moir, R.D.2    Willis, I.M.3
  • 28
    • 1242273884 scopus 로고    scopus 로고
    • Tetratricopeptide repeats of Tfc4 and a limiting step in the assembly of the initiation factor TFIIIB
    • Moir, R. D. & Willis, I. M. Tetratricopeptide repeats of Tfc4 and a limiting step in the assembly of the initiation factor TFIIIB. Adv. Protein Chem. 67, 93-121 (2004).
    • (2004) Adv. Protein Chem. , vol.67 , pp. 93-121
    • Moir, R.D.1    Willis, I.M.2
  • 29
    • 0026465666 scopus 로고
    • The role of the TATA-binding protein in the assembly and function of the multisubunit yeast RNA polymerase III transcription factor
    • Kassavetis, G. A. et al. The role of the TATA-binding protein in the assembly and function of the multisubunit yeast RNA polymerase III transcription factor, TFIIIB. Cell 71, 1055-1064 (1992).
    • (1992) TFIIIB. Cell , vol.71 , pp. 1055-1064
    • Kassavetis, G.A.1
  • 30
    • 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. & 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
  • 31
    • 0033584857 scopus 로고    scopus 로고
    • Interaction between yeast RNA polymerase III and transcription factor TFIIIC via ABC10alpha and tau131 subunits
    • Dumay, H., Rubbi, L., Sentenac, A. & Marck, C. Interaction between yeast RNA polymerase III and transcription factor TFIIIC via ABC10alpha and tau131 subunits. J. Biol. Chem. 274, 33462-33468 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 33462-33468
    • Dumay, H.1    Rubbi, L.2    Sentenac, A.3    Marck, C.4
  • 32
    • 0033038711 scopus 로고    scopus 로고
    • Cloning and characterization of two evolutionarily conserved subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their involvement in functional interactions with TFIIIB and RNA polymerase III
    • Hsieh, Y. J., Wang, Z., Kovelman, R. & Roeder, R. G. Cloning and characterization of two evolutionarily conserved subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their involvement in functional interactions with TFIIIB and RNA polymerase III. Mol. Cell. Biol. 19, 4944-4952 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4944-4952
    • Hsieh, Y.J.1    Wang, Z.2    Kovelman, R.3    Roeder, R.G.4
  • 33
    • 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. (2015).
    • (2015) J. Struct. Biol.
    • Kosinski, J.1
  • 34
    • 0031594706 scopus 로고    scopus 로고
    • Tau91, an essential subunit of yeast transcription factor IIIC, cooperates with tau138 in DNA binding
    • Arrebola, R. et al. Tau91, an essential subunit of yeast transcription factor IIIC, cooperates with tau138 in DNA binding. Mol. Cell. Biol. 18, 1-9 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1-9
    • Arrebola, R.1
  • 35
    • 0348111451 scopus 로고    scopus 로고
    • An extended winged helix domain in general transcription factor E/IIE alpha
    • Meinhart, A., Blobel, J. & Cramer, P. An extended winged helix domain in general transcription factor E/IIE alpha. J. Biol. Chem. 278, 48267-48274 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 48267-48274
    • Meinhart, A.1    Blobel, J.2    Cramer, P.3
  • 36
    • 27344446026 scopus 로고    scopus 로고
    • Reconfiguring the connectivity of a multiprotein complex: Fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB
    • Kassavetis, G. A., Soragni, E., Driscoll, R. & Geiduschek, E. P. Reconfiguring the connectivity of a multiprotein complex: Fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB. Proc. Natl Acad. Sci. USA 102, 15406-15411 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15406-15411
    • Kassavetis, G.A.1    Soragni, E.2    Driscoll, R.3    Geiduschek, E.P.4
  • 37
    • 0033508032 scopus 로고    scopus 로고
    • A subunit of yeast TFIIIC participates in the recruitment of TATA-binding protein
    • Deprez, E., Arrebola, R., Conesa, C. & Sentenac, A. A subunit of yeast TFIIIC participates in the recruitment of TATA-binding protein. Mol. Cell. Biol. 19, 8042-8051 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8042-8051
    • Deprez, E.1    Arrebola, R.2    Conesa, C.3    Sentenac, A.4
  • 38
    • 0028270310 scopus 로고
    • Encounters of Saccharomyces cerevisiae RNA polymerase III with its transcription factors during RNA chain elongation
    • Bardeleben, C., Kassavetis, G. A. & Geiduschek, E. P. Encounters of Saccharomyces cerevisiae RNA polymerase III with its transcription factors during RNA chain elongation. J. Mol. Biol. 235, 1193-1205 (1994).
    • (1994) J. Mol. Biol. , vol.235 , pp. 1193-1205
    • Bardeleben, C.1    Kassavetis, G.A.2    Geiduschek, E.P.3
  • 39
    • 84922748306 scopus 로고    scopus 로고
    • Identification of proteins associated with RNA polymerase III using a modified tandem chromatin affinity purification
    • Nguyen, N. T., Saguez, C., Conesa, C., Lefebvre, O. & Acker, J. Identification of proteins associated with RNA polymerase III using a modified tandem chromatin affinity purification. Gene 556, 51-60 (2015).
    • (2015) Gene , vol.556 , pp. 51-60
    • Nguyen, N.T.1    Saguez, C.2    Conesa, C.3    Lefebvre, O.4    Acker, J.5
  • 40
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • Leitner, A. et al. Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Mol. Cell. Proteomics 11, 014126 (2012).
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 014126
    • Leitner, A.1
  • 41
    • 84866118432 scopus 로고    scopus 로고
    • False discovery rate estimation for cross-linked peptides identified by mass spectrometry
    • Walzthoeni, T. et al. False discovery rate estimation for cross-linked peptides identified by mass spectrometry. Nat. Methods 9, 901-903 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 901-903
    • Walzthoeni, T.1
  • 42
    • 0026486967 scopus 로고
    • TFC3: Gene encoding the B-block binding subunit of the yeast transcription factor IIIC
    • Lefebvre, O. et al. TFC3: Gene encoding the B-block binding subunit of the yeast transcription factor IIIC. Proc. Natl Acad. Sci. USA 89, 10512-10516 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10512-10516
    • Lefebvre, O.1
  • 43
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D., LaCroute, F. & Fink, G. R. A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197, 345-346 (1984).
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 47
    • 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 Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 48
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 49
    • 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 Biol. Crystallogr. 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 50
    • 84926486138 scopus 로고    scopus 로고
    • XiNET: Cross-link network maps with residue resolution
    • Combe, C. W., Fischer, L. & Rappsilber, J. xiNET: Cross-link network maps with residue resolution. Mol. Cell. Proteomics 14, 1137-1147 (2015).
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1137-1147
    • Combe, C.W.1    Fischer, L.2    Rappsilber, J.3
  • 51
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A. & Diederichs, K. Linking crystallographic model and data quality. Science 336, 1030-1033 (2012).
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


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