메뉴 건너뛰기




Volumn 112, Issue 30, 2015, Pages E4036-E4045

Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1

Author keywords

Phosphorylation; Protein protein interaction inhibitor; Structure; Translation initiation

Indexed keywords

INITIATION FACTOR 4E; INITIATION FACTOR 4E BINDING PROTEIN 1; INITIATION FACTOR 4G; ANTINEOPLASTIC AGENT; EIF4E PROTEIN, MOUSE; EIF4EBP1 PROTEIN, HUMAN; EIF4ENIF1 PROTEIN, HUMAN; EIF4G1 PROTEIN, HUMAN; EIF4G1 PROTEIN, MOUSE; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN; PHOSPHOPROTEIN; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84938149443     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1512118112     Document Type: Article
Times cited : (86)

References (57)
  • 1
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: Mechanisms and biological targets. Cell 136(4):731-745.
    • (2009) Cell , vol.136 , Issue.4 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 2
    • 0021921587 scopus 로고
    • mRNA cap binding proteins: Essential factors for initiating translation
    • Shatkin AJ (1985) mRNA cap binding proteins: Essential factors for initiating translation. Cell 40(2):223-224.
    • (1985) Cell , vol.40 , Issue.2 , pp. 223-224
    • Shatkin, A.J.1
  • 3
    • 0032834055 scopus 로고    scopus 로고
    • EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N (1999) eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 68:913-963.
    • (1999) Annu Rev Biochem , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 4
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation
    • Beretta L, Gingras AC, Svitkin YV, Hall MN, Sonenberg N (1996) Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation. EMBO J 15(3):658-664.
    • (1996) EMBO J , vol.15 , Issue.3 , pp. 658-664
    • Beretta, L.1    Gingras, A.C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 5
    • 0035498939 scopus 로고    scopus 로고
    • Hierarchical phosphorylation of the translation inhibitor 4E-BP1
    • Gingras AC, et al. (2001) Hierarchical phosphorylation of the translation inhibitor 4E-BP1. Genes Dev 15(21):2852-2864.
    • (2001) Genes Dev , vol.15 , Issue.21 , pp. 2852-2864
    • Gingras, A.C.1
  • 6
    • 27744569843 scopus 로고    scopus 로고
    • MTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz MK, Ballif BA, Gygi SP, Blenis J (2005) mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123(4):569-580.
    • (2005) Cell , vol.123 , Issue.4 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 7
    • 84892685362 scopus 로고    scopus 로고
    • Casein kinase 1ε promotes cell proliferation by regulating mRNA translation
    • Shin S, Wolgamott L, Roux PP, Yoon SO (2014) Casein kinase 1ε promotes cell proliferation by regulating mRNA translation. Cancer Res 74(1):201-211.
    • (2014) Cancer Res , vol.74 , Issue.1 , pp. 201-211
    • Shin, S.1    Wolgamott, L.2    Roux, P.P.3    Yoon, S.O.4
  • 8
    • 84898014860 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β positively regulates protein synthesis and cell proliferation through the regulation of translation initiation factor 4E-binding protein 1
    • Shin S, et al. (2014) Glycogen synthase kinase-3β positively regulates protein synthesis and cell proliferation through the regulation of translation initiation factor 4E-binding protein 1. Oncogene 33(13):1690-1699.
    • (2014) Oncogene , vol.33 , Issue.13 , pp. 1690-1699
    • Shin, S.1
  • 9
    • 84879367394 scopus 로고    scopus 로고
    • Prion formation correlates with activation of translation-regulating protein 4E-BP and neuronal transcription factor Elk1
    • Allard EK, Grujic M, Fisone G, Kristensson K (2013) Prion formation correlates with activation of translation-regulating protein 4E-BP and neuronal transcription factor Elk1. Neurobiol Dis 58:116-122.
    • (2013) Neurobiol Dis , vol.58 , pp. 116-122
    • Allard, E.K.1    Grujic, M.2    Fisone, G.3    Kristensson, K.4
  • 10
    • 84872595085 scopus 로고    scopus 로고
    • Autism-related deficits via dysregulated eIF4E-dependent translational control
    • Gkogkas CG, et al. (2013) Autism-related deficits via dysregulated eIF4E-dependent translational control. Nature 493(7432):371-377.
    • (2013) Nature , vol.493 , Issue.7432 , pp. 371-377
    • Gkogkas, C.G.1
  • 12
    • 2942544833 scopus 로고    scopus 로고
    • Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells
    • Avdulov S, et al. (2004) Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells. Cancer Cell 5(6):553-563.
    • (2004) Cancer Cell , vol.5 , Issue.6 , pp. 553-563
    • Avdulov, S.1
  • 13
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap
    • Lazaris-Karatzas A, Montine KS, Sonenberg N (1990) Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap. Nature 345(6275):544-547.
    • (1990) Nature , vol.345 , Issue.6275 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 14
    • 2342489456 scopus 로고    scopus 로고
    • EIF-4E expression and its role in malignancies and metastases
    • De Benedetti A, Graff JR (2004) eIF-4E expression and its role in malignancies and metastases. Oncogene 23(18):3189-3199.
    • (2004) Oncogene , vol.23 , Issue.18 , pp. 3189-3199
    • De Benedetti, A.1    Graff, J.R.2
  • 15
    • 2342584183 scopus 로고    scopus 로고
    • EIF4E-from translation to transformation
    • Mamane Y, et al. (2004) eIF4E-from translation to transformation. Oncogene 23(18):3172-3179.
    • (2004) Oncogene , vol.23 , Issue.18 , pp. 3172-3179
    • Mamane, Y.1
  • 16
    • 84865116634 scopus 로고    scopus 로고
    • Translation regulation as a therapeutic target in cancer
    • Grzmil M, Hemmings BA (2012) Translation regulation as a therapeutic target in cancer. Cancer Res 72(16):3891-3900.
    • (2012) Cancer Res , vol.72 , Issue.16 , pp. 3891-3900
    • Grzmil, M.1    Hemmings, B.A.2
  • 17
    • 77952967459 scopus 로고    scopus 로고
    • MTORC1-mediated cell proliferation, but not cell growth, controlled by the 4E-BPs
    • Dowling RJ, et al. (2010) mTORC1-mediated cell proliferation, but not cell growth, controlled by the 4E-BPs. Science 328(5982):1172-1176.
    • (2010) Science , vol.328 , Issue.5982 , pp. 1172-1176
    • Dowling, R.J.1
  • 18
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • Mader S, Lee H, Pause A, Sonenberg N (1995) The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mol Cell Biol 15(9):4990-4997.
    • (1995) Mol Cell Biol , vol.15 , Issue.9 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 19
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK (1999) Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol Cell 3(6):707-716.
    • (1999) Mol Cell , vol.3 , Issue.6 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 20
    • 67649302863 scopus 로고    scopus 로고
    • Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site
    • Brown CJ, Verma CS, Walkinshaw MD, Lane DP (2009) Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site. Cell Cycle 8(12):1905-1911.
    • (2009) Cell Cycle , vol.8 , Issue.12 , pp. 1905-1911
    • Brown, C.J.1    Verma, C.S.2    Walkinshaw, M.D.3    Lane, D.P.4
  • 21
    • 0347281686 scopus 로고    scopus 로고
    • Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E
    • Gross JD, et al. (2003) Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. Cell 115(6):739-750.
    • (2003) Cell , vol.115 , Issue.6 , pp. 739-750
    • Gross, J.D.1
  • 22
    • 27844576586 scopus 로고    scopus 로고
    • Structural basis for mRNA Cap-Binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods
    • Tomoo K, et al. (2005) Structural basis for mRNA Cap-Binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods. Biochim Biophys Acta 1753(2):191-208.
    • (2005) Biochim Biophys Acta , vol.1753 , Issue.2 , pp. 191-208
    • Tomoo, K.1
  • 23
    • 0030826444 scopus 로고    scopus 로고
    • Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein
    • Matsuo H, et al. (1997) Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein. Nat Struct Biol 4(9):717-724.
    • (1997) Nat Struct Biol , vol.4 , Issue.9 , pp. 717-724
    • Matsuo, H.1
  • 24
    • 79955596590 scopus 로고    scopus 로고
    • The translational repressor 4E-BP called to order by eIF4E: New structural insights by SAXS
    • Gosselin P, et al. (2011) The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS. Nucleic Acids Res 39(8):3496-3503.
    • (2011) Nucleic Acids Res , vol.39 , Issue.8 , pp. 3496-3503
    • Gosselin, P.1
  • 25
    • 53049087996 scopus 로고    scopus 로고
    • Importance of C-terminal flexible region of 4E-binding protein in binding with eukaryotic initiation factor 4E
    • Mizuno A, et al. (2008) Importance of C-terminal flexible region of 4E-binding protein in binding with eukaryotic initiation factor 4E. FEBS Lett 582(23-24):3439-3444.
    • (2008) FEBS Lett , vol.582 , Issue.23-24 , pp. 3439-3444
    • Mizuno, A.1
  • 26
    • 80054911203 scopus 로고    scopus 로고
    • Identification and function of the second eIF4E-binding region in N-terminal domain of eIF4G: Comparison with eIF4E-binding protein
    • Umenaga Y, Paku KS, In Y, Ishida T, Tomoo K (2011) Identification and function of the second eIF4E-binding region in N-terminal domain of eIF4G: Comparison with eIF4E-binding protein. Biochem Biophys Res Commun 414(3):462-467.
    • (2011) Biochem Biophys Res Commun , vol.414 , Issue.3 , pp. 462-467
    • Umenaga, Y.1    Paku, K.S.2    In, Y.3    Ishida, T.4    Tomoo, K.5
  • 27
    • 84055178150 scopus 로고    scopus 로고
    • A conserved motif within the flexible C-terminus of the translational regulator 4E-BP is required for tight binding to the mRNA cap-binding protein eIF4E
    • Paku KS, et al. (2012) A conserved motif within the flexible C-terminus of the translational regulator 4E-BP is required for tight binding to the mRNA cap-binding protein eIF4E. Biochem J 441(1):237-245.
    • (2012) Biochem J , vol.441 , Issue.1 , pp. 237-245
    • Paku, K.S.1
  • 28
    • 84889564693 scopus 로고    scopus 로고
    • Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface
    • Lukhele S, Bah A, Lin H, Sonenberg N, Forman-Kay JD (2013) Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface. Structure 21(12):2186-2196.
    • (2013) Structure , vol.21 , Issue.12 , pp. 2186-2196
    • Lukhele, S.1    Bah, A.2    Lin, H.3    Sonenberg, N.4    Forman-Kay, J.D.5
  • 29
    • 33846449110 scopus 로고    scopus 로고
    • Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G
    • Moerke NJ, et al. (2007) Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell 128(2):257-267.
    • (2007) Cell , vol.128 , Issue.2 , pp. 257-267
    • Moerke, N.J.1
  • 30
    • 84868622977 scopus 로고    scopus 로고
    • Tumor suppression by small molecule inhibitors of translation initiation
    • Chen L, et al. (2012) Tumor suppression by small molecule inhibitors of translation initiation. Oncotarget 3(8):869-881.
    • (2012) Oncotarget , vol.3 , Issue.8 , pp. 869-881
    • Chen, L.1
  • 31
    • 84906265523 scopus 로고    scopus 로고
    • 4EGI-1 targets breast cancer stem cells by selective inhibition of translation that persists in CSC maintenance, proliferation and metastasis
    • Yi T, Kabha E, Papadopoulos E, Wagner G (2014) 4EGI-1 targets breast cancer stem cells by selective inhibition of translation that persists in CSC maintenance, proliferation and metastasis. Oncotarget 5(15):6028-6037.
    • (2014) Oncotarget , vol.5 , Issue.15 , pp. 6028-6037
    • Yi, T.1    Kabha, E.2    Papadopoulos, E.3    Wagner, G.4
  • 32
    • 84905653296 scopus 로고    scopus 로고
    • Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G
    • Papadopoulos E, et al. (2014) Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G. Proc Natl Acad Sci USA 111(31):E3187-E3195.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.31 , pp. E3187-E3195
    • Papadopoulos, E.1
  • 33
    • 0032577691 scopus 로고    scopus 로고
    • 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family
    • Poulin F, Gingras AC, Olsen H, Chevalier S, Sonenberg N (1998) 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family. J Biol Chem 273(22):14002-14007.
    • (1998) J Biol Chem , vol.273 , Issue.22 , pp. 14002-14007
    • Poulin, F.1    Gingras, A.C.2    Olsen, H.3    Chevalier, S.4    Sonenberg, N.5
  • 34
    • 84873739231 scopus 로고    scopus 로고
    • Anti-oncogenic potential of the eIF4E-binding proteins
    • Martineau Y, Azar R, Bousquet C, Pyronnet S (2013) Anti-oncogenic potential of the eIF4E-binding proteins. Oncogene 32(6):671-677.
    • (2013) Oncogene , vol.32 , Issue.6 , pp. 671-677
    • Martineau, Y.1    Azar, R.2    Bousquet, C.3    Pyronnet, S.4
  • 35
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK (1997) Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89(6):951-961.
    • (1997) Cell , vol.89 , Issue.6 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 36
    • 84925269956 scopus 로고    scopus 로고
    • Molecular architecture of 4E-BP translational inhibitors bound to eIF4E
    • Peter D, et al. (2015) Molecular architecture of 4E-BP translational inhibitors bound to eIF4E. Mol Cell 57(6):1074-1087.
    • (2015) Mol Cell , vol.57 , Issue.6 , pp. 1074-1087
    • Peter, D.1
  • 37
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372(3):774-797.
    • (2007) J Mol Biol , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 84925538272 scopus 로고    scopus 로고
    • Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch
    • Bah A, et al. (2015) Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. Nature 519(7541):106-109.
    • (2015) Nature , vol.519 , Issue.7541 , pp. 106-109
    • Bah, A.1
  • 39
    • 84907303445 scopus 로고    scopus 로고
    • 4E-BPs require non-canonical 4E-binding motifs and a lateral surface of eIF4E to repress translation
    • Igreja C, Peter D, Weiler C, Izaurralde E (2014) 4E-BPs require non-canonical 4E-binding motifs and a lateral surface of eIF4E to repress translation. Nat Commun 5:4790.
    • (2014) Nat Commun , vol.5 , pp. 4790
    • Igreja, C.1    Peter, D.2    Weiler, C.3    Izaurralde, E.4
  • 40
    • 84865118901 scopus 로고    scopus 로고
    • Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression
    • Kinkerlin K, Veith K, Grunwald M, Bono F (2012) Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression. RNA 18(9):1624-1634.
    • (2012) RNA , vol.18 , Issue.9 , pp. 1624-1634
    • Kinkerlin, K.1    Veith, K.2    Grunwald, M.3    Bono, F.4
  • 41
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
    • Gingras AC, et al. (1999) Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism. Genes Dev 13(11):1422-1437.
    • (1999) Genes Dev , vol.13 , Issue.11 , pp. 1422-1437
    • Gingras, A.C.1
  • 42
    • 0035827592 scopus 로고    scopus 로고
    • A quantitative molecular model for modulation of mammalian translation by the eIF4E-binding protein 1
    • Karim MM, et al. (2001) A quantitative molecular model for modulation of mammalian translation by the eIF4E-binding protein 1. J Biol Chem 276(23):20750-20757.
    • (2001) J Biol Chem , vol.276 , Issue.23 , pp. 20750-20757
    • Karim, M.M.1
  • 43
    • 0034057277 scopus 로고    scopus 로고
    • Multiple mechanisms control phosphorylation of PHAS-I in five (S/T) P sites that govern translational repression
    • Mothe-Satney I, Yang D, Fadden P, Haystead TA, Lawrence JC, Jr (2000) Multiple mechanisms control phosphorylation of PHAS-I in five (S/T) P sites that govern translational repression. Mol Cell Biol 20(10):3558-3567.
    • (2000) Mol Cell Biol , vol.20 , Issue.10 , pp. 3558-3567
    • Mothe-Satney, I.1    Yang, D.2    Fadden, P.3    Haystead, T.A.4    Lawrence, J.C.5
  • 44
    • 33646596978 scopus 로고    scopus 로고
    • Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization
    • Bao WJ, et al. (2006) Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization. Protein Expr Purif 47(2):599-606.
    • (2006) Protein Expr Purif , vol.47 , Issue.2 , pp. 599-606
    • Bao, W.J.1
  • 45
    • 0024238770 scopus 로고
    • High-level synthesis in Escherichia coli of functional cap-binding eukaryotic initiation factor eIF-4E and affinity purification using a simplified cap-analog resin
    • Edery I, Altmann M, Sonenberg N (1988) High-level synthesis in Escherichia coli of functional cap-binding eukaryotic initiation factor eIF-4E and affinity purification using a simplified cap-analog resin. Gene 74(2):517-525.
    • (1988) Gene , vol.74 , Issue.2 , pp. 517-525
    • Edery, I.1    Altmann, M.2    Sonenberg, N.3
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds Carter CW, Jr, Sweet RM Academic, New York
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Methods in Enzymology, eds Carter CW, Jr, Sweet RM (Academic, New York), Vol 276, pp 307-326.
    • (1997) Macromolecular Crystallography, Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 47
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63(Pt 1):32-41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 48
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 49
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58(Pt 11):1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 50
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 52
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA (2001) Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc Natl Acad Sci USA 98(18):10037-10041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.18 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 53
    • 77950835733 scopus 로고    scopus 로고
    • Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data
    • Hyberts SG, Takeuchi K, Wagner G (2010) Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data. J Am Chem Soc 132(7):2145-2147.
    • (2010) J Am Chem Soc , vol.132 , Issue.7 , pp. 2145-2147
    • Hyberts, S.G.1    Takeuchi, K.2    Wagner, G.3
  • 54
    • 84863114255 scopus 로고    scopus 로고
    • Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling
    • Hyberts SG, Milbradt AG, Wagner AB, Arthanari H, Wagner G (2012) Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling. J Biomol NMR 52(4):315-327.
    • (2012) J Biomol NMR , vol.52 , Issue.4 , pp. 315-327
    • Hyberts, S.G.1    Milbradt, A.G.2    Wagner, A.B.3    Arthanari, H.4    Wagner, G.5
  • 55
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, et al. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277-293.
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1
  • 56
    • 14844299785 scopus 로고    scopus 로고
    • Software extensions to UCSF chimera for interactive visualization of large molecular assemblies
    • Goddard TD, Huang CC, Ferrin TE (2005) Software extensions to UCSF chimera for interactive visualization of large molecular assemblies. Structure 13(3):473-482.
    • (2005) Structure , vol.13 , Issue.3 , pp. 473-482
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 57
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin MA, et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23(21):2947-2948.
    • (2007) Bioinformatics , vol.23 , Issue.21 , pp. 2947-2948
    • Larkin, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.