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Volumn , Issue , 2012, Pages 1-31

Spatial and temporal organisation of multiprotein systems of cell regulation and signalling: What can we learn from NHEJ system of double-strand break repair?

Author keywords

AUC; Cell regulation; Cell signalling; Circular dichroism; Crosslinking; Crystallisation; DLS; DNA ligase IV; DNA repair; DNA PKcs; EM; ITC; Ku70 80; Multiprotein assemblies; Nanospray MS; NHEJ; SAXS; SPR; Structural determination; X ray diffraction; XLF; XRCC4; Yeast two hybrid

Indexed keywords


EID: 84858756788     PISSN: 18746489     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-2530-0_1     Document Type: Article
Times cited : (2)

References (89)
  • 1
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA Ligase IV complex to promote DNA nonhomologous end-joining
    • DOI 10.1016/j.cell.2005.12.031, PII S0092867406000031
    • Ahnesorg P, Smith P, Jackson SP (2006) XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA Non-homologous End-joining. Cell 124(2):301-313 (Pubitemid 43121979)
    • (2006) Cell , vol.124 , Issue.2 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 2
    • 37349113779 scopus 로고    scopus 로고
    • Crystal Structure of Human XLF: A Twist in Nonhomologous DNA End-Joining
    • DOI 10.1016/j.molcel.2007.10.024, PII S1097276507007319
    • Andres S, Modesti M, Tsai CJ, Chu G, Junop MS (2007) Crystal structure of human XLF: a twist in nonhomologous DNA End-joining. Mol Cell 28(6):1093-1101 (Pubitemid 350297023)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 1093-1101
    • Andres, S.N.1    Modesti, M.2    Tsai, C.J.3    Chu, G.4    Junop, M.S.5
  • 3
    • 61649100307 scopus 로고    scopus 로고
    • The FGF family: Biology, pathophysiology and therapy
    • Beenken A, Mohammadi M (2010) The FGF family: biology, pathophysiology and therapy. Nat Rev Drug Discov 8:235-253
    • (2010) Nat Rev Drug Discov , vol.8 , pp. 235-253
    • Beenken, A.1    Mohammadi, M.2
  • 6
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell TL, Jhoti H, Abell C (2002) High-throughput crystallography for lead discovery in drug design. Nat Rev Drug Discov 1:45-54 (Pubitemid 37361403)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 8
    • 0242576857 scopus 로고    scopus 로고
    • Visualization of DNA-induced conformational changes in the DNA repair kinase DNA-PKcs
    • DOI 10.1093/emboj/cdg555
    • Boskovic J, Rivera-Calzada A, Maman JD, Chacón P, Willison KR, Pearl LH, Llorca O (2003) Visualization of dna-induced conformational changes in the DNA repair kinase dna-pkcs. EMBO J 22(21):5875-5882 (Pubitemid 37419925)
    • (2003) EMBO Journal , vol.22 , Issue.21 , pp. 5875-5882
    • Boskovic, J.1    Rivera-Calzada, A.2    Maman, J.D.3    Chacon, P.4    Willison, K.R.5    Pearl, L.H.6    Llorca, O.7
  • 9
    • 0026499357 scopus 로고
    • Has negative staining still a place in biomacromolecular electron microscopy?
    • DOI 10.1016/0304-3991(92)90040-Q
    • Bremer A, Henn C, Engel A, Baumeister W, Aebi U (1992) Has negative staining still a place in biomacromolecular electron microscopy? Ultramicroscopy 46(1-4):85-111 (Pubitemid 23600813)
    • (1992) Ultramicroscopy , vol.45 , Issue.1-4 , pp. 85-111
    • Bremer Andreas1    Henn Christian2    Engel Andreas3    Baumeister Wolfgang4    Aebi Ueli5
  • 10
    • 0031015166 scopus 로고    scopus 로고
    • Fluorescence spectroscopy as a tool to investigate protein interactions
    • DOI 10.1016/S0958-1669(97)80156-5
    • Brown M, Royer C (1997) Fluorescence spectroscopy as a tool to investigate protein interactions. Curr Opin Biotechnol 8(1):45-49 (Pubitemid 27067464)
    • (1997) Current Opinion in Biotechnology , vol.8 , Issue.1 , pp. 45-49
    • Brown, M.P.1    Royer, C.2
  • 11
    • 0032971199 scopus 로고    scopus 로고
    • Absence of DNA ligase IV protein in XR-1 cells: Evidence for stabilization by XRCC4
    • DOI 10.1016/S0921-8777(98)00063-9, PII S0921877798000639
    • Bryans M, Valenzano MC, Stamato TD (1999) Absence of DNA ligase IV protein in xr-1 cells: evidence for stabilization by xrcc4. Mutat Res/DNA Repair 433(1):53-58 (Pubitemid 29073670)
    • (1999) Mutation Research - DNA Repair , vol.433 , Issue.1 , pp. 53-58
    • Bryans, M.1    Valenzano, M.C.2    Stamato, T.D.3
  • 13
    • 3142765336 scopus 로고    scopus 로고
    • Class-switch recombination: Interplay of transcription, DNA deamination and DNA repair
    • Chaudhuri J, Alt FW (2004) Class-switch recombination: interplay of transcription, DNA deamination and DNA repair. Nat Rev Immunol 4:541-552 (Pubitemid 38931769)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.7 , pp. 541-552
    • Chaudhuri, J.1    Alt, F.W.2
  • 14
    • 0032509097 scopus 로고    scopus 로고
    • Cryo-EM imaging of the catalytic subunit of the DNA-dependent protein kinase
    • DOI 10.1006/jmbi.1998.2212
    • Chiu CY, Cary RB, Chen DJ, Peterson SR, Stewart PL (1998) Cryo-EM imaging of the catalytic subunit of the DNA-dependent protein kinase. J Mol Biol 284:1075-1081 (Pubitemid 28558557)
    • (1998) Journal of Molecular Biology , vol.284 , Issue.4 , pp. 1075-1081
    • Chiu, C.Y.1    Cary, R.B.2    Chen, D.J.3    Peterson, S.R.4    Stewart, P.L.5
  • 16
    • 34247602569 scopus 로고    scopus 로고
    • Interaction of the Ku heterodimer with the DNA ligase IV/Xrcc4 complex and its regulation by DNA-PK
    • DOI 10.1016/j.dnarep.2006.12.007, PII S1568786406004046
    • Costantini S, Woodbine L, Andreoli L, Jeggo PA, Vindigni A (2007) Interaction of the ku heterodimer with the dna ligase iv/xrcc4 complex and its regulation by dna-pk. DNA Repair 6(6):712-722 (Pubitemid 46670084)
    • (2007) DNA Repair , vol.6 , Issue.6 , pp. 712-722
    • Costantini, S.1    Woodbine, L.2    Andreoli, L.3    Jeggo, P.A.4    Vindigni, A.5
  • 17
    • 0031214080 scopus 로고    scopus 로고
    • Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV
    • Critchlow SE, Bowater RP, Jackson SP (1997) Mammalian dna double-strand break repair protein xrcc4 interacts with dna ligase iv. Curr Biol 7(8):588-598 (Pubitemid 27335654)
    • (1997) Current Biology , vol.7 , Issue.8 , pp. 588-598
    • Critchlow, S.E.1    Bowater, R.P.2    Jackson, S.P.3
  • 18
    • 1842428822 scopus 로고    scopus 로고
    • Calculating Sedimentation Coefficient Distributions by Direct Modeling of Sedimentation Velocity Concentration Profiles
    • DOI 10.1016/S0076-6879(04)84012-6
    • Dam J, Schuck P (2004) Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles. Methods Enzymol 384:185-212. doi: 10.1016/S0076-6879(04)84012-6 (Pubitemid 38420481)
    • (2004) Methods in Enzymology , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 19
    • 34548567192 scopus 로고    scopus 로고
    • Modes of interaction among yeast Nej1, Lif1 and Dnl4 proteins and comparison to human XLF, XRCC4 and Lig4
    • DOI 10.1016/j.dnarep.2007.04.014, PII S1568786407001814
    • Deshpande R, Wilson T (2007) Modes of interaction among yeast Nej1, Lif1 and Dnl4 proteins and comparison to human XLF, XRCC4 and Lig4. DNA Repair 6(10):1507-1516 (Pubitemid 47386045)
    • (2007) DNA Repair , vol.6 , Issue.10 , pp. 1507-1516
    • Deshpande, R.A.1    Wilson, T.E.2
  • 20
    • 32644480115 scopus 로고    scopus 로고
    • Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode
    • DOI 10.1016/j.dnarep.2005.11.004, PII S1568786405003125
    • Doré AS, Furnham N, Davies OR, Sibanda BL, Chirgadze DY, Jackson SP, Pellegrini L, Blundell TL (2006) Structure of an xrcc4-dna ligase iv yeast ortholog complex reveals a novel brct interaction mode. DNA Repair 5(3):362-368 (Pubitemid 43247602)
    • (2006) DNA Repair , vol.5 , Issue.3 , pp. 362-368
    • Dore, A.S.1    Furnham, N.2    Davies, O.R.3    Sibanda, B.L.4    Chirgadze, D.Y.5    Jackson, S.P.6    Pellegrini, L.7    Blundell, T.L.8
  • 22
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197-208 (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 23
    • 51249118082 scopus 로고    scopus 로고
    • Integration of smallangle x-ray scattering data into structural modeling of proteins and their assemblies
    • Förster F, Webb B, Krukenberg KA, Tsuruta H, Agard DA, Sali A (2008) Integration of smallangle x-ray scattering data into structural modeling of proteins and their assemblies. J Mol Biol 382(4):1089-1106
    • (2008) J Mol Biol , vol.382 , Issue.4 , pp. 1089-1106
    • Förster, F.1    Webb, B.2    Krukenberg, K.A.3    Tsuruta, H.4    Agard, D.A.5    Sali, A.6
  • 24
    • 0019877067 scopus 로고
    • A gel electrophoresis method for quantifying the binding of proteins to specific dna regions: Application to components of the escherichia coli lactose operon regulatory system
    • Garner MM, Revzin A (1981) A gel electrophoresis method for quantifying the binding of proteins to specific dna regions: application to components of the escherichia coli lactose operon regulatory system. Nucleic Acids Res 9(13):3047-3060
    • (1981) Nucleic Acids Res , vol.9 , Issue.13 , pp. 3047-3060
    • Garner, M.M.1    Revzin, A.2
  • 25
    • 0033198709 scopus 로고    scopus 로고
    • Mapping of protein-protein interactions within the DNA-dependent protein kinase complex
    • DOI 10.1093/nar/27.17.3494
    • Gell D, Jackson SP (1999) Mapping of protein-protein interactions within the dna-dependent protein kinase complex. Nucleic Acids Res 27(17):3494-3502 (Pubitemid 29414677)
    • (1999) Nucleic Acids Research , vol.27 , Issue.17 , pp. 3494-3502
    • Gell, D.1    Jackson, S.P.2
  • 26
    • 0035997348 scopus 로고    scopus 로고
    • V(D)J recombination: RAG proteins, repair factors, and regulation
    • DOI 10.1146/annurev.biochem.71.090501.150203
    • Gellert M (2002) V(d)j recombination: Rag proteins, repair factors, and regulation. Annu Rev Biochem 71:101-132 (Pubitemid 34800216)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 101-132
    • Gellert, M.1
  • 28
    • 0030743386 scopus 로고    scopus 로고
    • Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
    • DOI 10.1038/41358
    • Grawunder U, Wilm M, Wu X, Kulesza P, Wilson TE, Mann M, Lieber MR (1997) Activity of dna ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature 388(6641):492-495 (Pubitemid 27328929)
    • (1997) Nature , vol.388 , Issue.6641 , pp. 492-495
    • Grawunder, U.1    Wilm, M.2    Wu, X.3    Kulesza, P.4    Wilson, T.E.5    Mann, M.6    Lieber, M.R.7
  • 29
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • DOI 10.1006/abio.1996.0084
    • Greenfield NJ (1996) Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal Biochem 235(1):1-10 (Pubitemid 26065191)
    • (1996) Analytical Biochemistry , vol.235 , Issue.1 , pp. 1-10
    • Greenfield, N.J.1
  • 32
    • 2942623745 scopus 로고    scopus 로고
    • Protein-nucleic acid interactions and the expanding role of mass spectrometry
    • DOI 10.1074/jbc.R300037200
    • Hanson CL, Robinson CV (2004) Protein-nucleic acid interactions and the expanding role of mass spectrometry. J Biol Chem 279(24):24907-24910. doi: 10.1074/jbc.R300037200 (Pubitemid 38756735)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 24907-24910
    • Hanson, C.L.1    Robinson, C.V.2
  • 33
    • 2542482608 scopus 로고    scopus 로고
    • Towards a resolution of the stoichiometry of the fibroblast growth factor (FGF)-FGF receptor-heparin complex
    • DOI 10.1016/j.jmb.2004.04.031, PII S002228360400467X
    • Harmer NJ, Ilag LL, Mulloy B, Pellegrini L, Robinson CV, Blundell TL (2004) Towards a resolution of the stoichiometry of the fibroblast growth factor (FGF)-FGF receptor-heparin complex. J Mol Biol 339:821-834 (Pubitemid 38686347)
    • (2004) Journal of Molecular Biology , vol.339 , Issue.4 , pp. 821-834
    • Harmer, N.J.1    Ilag, L.L.2    Mulloy, B.3    Pellegrini, L.4    Robinson, C.V.5    Blundell, T.L.6
  • 35
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • DOI 10.1038/nprot.2007.73, PII NPROT.2007.73
    • Hernandez H, Robinson C (2007) Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat Protoc 2(3):715-726 (Pubitemid 47040033)
    • (2007) Nature Protocols , vol.2 , Issue.3 , pp. 715-726
    • Hernandez, H.1    Robinson, C.V.2
  • 36
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • DOI 10.1016/j.cbpa.2006.08.017, PII S1367593106001244, Analytical Techniques/Mechanisms
    • Howlett GJ, Minton AP, Rivas G (2006) Analytical ultracentrifugation for the study of protein association and assembly. Curr Opin Chem Biol 10(5):430-436. doi: 10.1016/j.cbpa.2006.08.017 (Pubitemid 44375070)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3
  • 38
    • 0026045194 scopus 로고
    • Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology
    • Jönsson U, Fägerstam L, Ivarsson B, Johnsson B, Karlsson R, Lundh K et al (1991) Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology. Biotechniques 11(5):620-627
    • (1991) Biotechniques , vol.11 , Issue.5 , pp. 620-627
    • Jönsson, U.1    Fägerstam, L.2    Ivarsson, B.3    Johnsson, B.4    Karlsson, R.5    Lundh, K.6
  • 39
    • 0034669204 scopus 로고    scopus 로고
    • Crystal structure of the xrcc4 dna repair protein and implications for end joining
    • Junop MS, Modesti M, Guarné A, Ghirlando R, Gellert M, Yang W (2000) Crystal structure of the xrcc4 dna repair protein and implications for end joining. EMBO J 19(22):5962-5970
    • (2000) EMBO J , vol.19 , Issue.22 , pp. 5962-5970
    • Junop, M.S.1    Modesti, M.2    Guarné, A.3    Ghirlando, R.4    Gellert, M.5    Yang, W.6
  • 42
    • 0035093737 scopus 로고    scopus 로고
    • DNA double-strand breaks: Signaling, repair and the cancer connection
    • DOI 10.1038/85798
    • Khanna KK, Jackson SP (2001) Dna double-strand breaks: signaling, repair and the cancer connection. Nat Genet 27(3):247-254 (Pubitemid 32201842)
    • (2001) Nature Genetics , vol.27 , Issue.3 , pp. 247-254
    • Khanna, K.K.1    Jackson, S.P.2
  • 43
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • DOI 10.1016/S0959-440X(00)00248-7
    • Leavitt S (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr Opin Struct Biol 11(5):560-566. doi: 10.1016/S0959-440X(00)00248-7 (Pubitemid 32972017)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 45
    • 3242879122 scopus 로고    scopus 로고
    • The mechanism of vertebrate nonhomologous DNA end joining and its role in V(D)J recombination
    • DOI 10.1016/j.dnarep.2004.03.015, PII S1568786404000746
    • Lieber MR, Ma Y, Pannicke U, Schwarz K (2004) The mechanism of vertebrate nonhomologous dna end joining and its role in v(d)j recombination. DNA Repair 3(8-9):817-826 (Pubitemid 39004089)
    • (2004) DNA Repair , vol.3 , Issue.8-9 , pp. 817-826
    • Lieber, M.R.1    Ma, Y.2    Pannicke, U.3    Schwarz, K.4
  • 46
    • 64549095890 scopus 로고    scopus 로고
    • Hybrid approaches: Applying computational methods in cryo-electron microscopy
    • Lindert S, Stewart PL, Meiler J (2009) Hybrid approaches: applying computational methods in cryo-electron microscopy. Curr Opin Struct Biol 19(2):218-225
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.2 , pp. 218-225
    • Lindert, S.1    Stewart, P.L.2    Meiler, J.3
  • 47
    • 34249685474 scopus 로고    scopus 로고
    • Length-dependent binding of human XLF to DNA and stimulation of XRCC4·DNA ligase IV activity
    • DOI 10.1074/jbc.M609904200
    • Lu H, Pannicke U, Schwarz K, Lieber M (2007) Length-dependent binding of human XLF to DNA and stimulation of XRCC4-DNA ligase IV activity. J Biol Chem 282(15):11155-11162 (Pubitemid 47100736)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11155-11162
    • Lu, H.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 48
    • 26644444577 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human artemis
    • DOI 10.1074/jbc.M507113200
    • Ma Y, Pannicke U, Lu H, Niewolik D, Schwarz K, Lieber MR (2005) The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human Artemis. J Biol Chem 280(40):33839-33846 (Pubitemid 41443103)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 33839-33846
    • Ma, Y.1    Pannicke, U.2    Lu, H.3    Niewolik, D.4    Schwarz, K.5    Lieber, M.R.6
  • 49
    • 0242289356 scopus 로고    scopus 로고
    • Tetramerization and DNA ligase IV interaction of the DNA double-strand break repair protein XRCC4 are mutually exclusive
    • DOI 10.1016/j.jmb.2003.09.031
    • Modesti M, Junop MS, Ghirlando R, van de Rakt M, Gellert M, Yang W, Kanaar R (2003) Tetramerization and dna ligase iv interaction of the dna double-strand break repair protein xrcc4 are mutually exclusive. J Mol Biol 334(2):215-228 (Pubitemid 37357262)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.2 , pp. 215-228
    • Modesti, M.1    Junop, M.S.2    Ghirlando, R.3    Van De Rakt, M.4    Gellert, M.5    Yang, W.6    Kanaar, R.7
  • 51
    • 37349034299 scopus 로고    scopus 로고
    • Combining X-ray and electron-microscopy data to solve crystal structures
    • Navaza J (2008) Combining X-ray and electron-microscopy data to solve crystal structures. Acta Crystallogr D 64(1):70-75
    • (2008) Acta Crystallogr D , vol.64 , Issue.1 , pp. 70-75
    • Navaza, J.1
  • 52
    • 29244437908 scopus 로고    scopus 로고
    • The role of double-strand break repair - Insights from human genetics
    • O'Driscoll M, Jeggo PA (2005) The role of double-strand break repair - insights from human genetics. Nat Rev Genet 7(1):45-54
    • (2005) Nat Rev Genet , vol.7 , Issue.1 , pp. 45-54
    • O'Driscoll, M.1    Jeggo, P.A.2
  • 53
    • 79960616484 scopus 로고    scopus 로고
    • Structural biology of DNA repair: Spatial organisation of the multicomponent complexes of nonhomologous End joining
    • Ochi T, Sibanda BL, Wu Q, Chirgadze DY, Bolanos-Garcia VM, Blundell TL (2010) Structural biology of DNA repair: spatial organisation of the multicomponent complexes of nonhomologous End joining, J Nucleic Acids 2010:1-19
    • (2010) J Nucleic Acids , vol.2010 , pp. 1-19
    • Ochi, T.1    Sibanda, B.L.2    Wu, Q.3    Chirgadze, D.Y.4    Bolanos-Garcia, V.M.5    Blundell, T.L.6
  • 54
    • 9644289536 scopus 로고    scopus 로고
    • Human DNA ligase I completely encircles and partially unwinds nicked DNA
    • DOI 10.1038/nature03082
    • Pascal JM, O'Brien PJ, Tomkinson AE, Ellenberger T (2004) Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature 432(7016):473-478 (Pubitemid 39576523)
    • (2004) Nature , vol.432 , Issue.7016 , pp. 473-478
    • Pascal, J.M.1    O'Brien, P.J.2    Tomkinson, A.E.3    Ellenberger, T.4
  • 55
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle x-ray scattering
    • Pelikan M, Hura GL, Hammel M (2009) Structure and flexibility within proteins as identified through small angle x-ray scattering. Gen Physiol Biophys 28(2):174-189
    • (2009) Gen Physiol Biophys , vol.28 , Issue.2 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 56
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407:1029-1034
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 58
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • DOI 10.1529/biophysj.105.064154
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89(2):1237-1250 (Pubitemid 41099005)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 60
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • DOI 10.1006/meth.1999.0852
    • Pierce M, Raman C, Nall B (1999) Isothermal titration calorimetry of protein-protein interactions. Methods (San Diego, Calif) 19(2):213-221. doi: 10.1006/meth.1999.0852 (Pubitemid 29515856)
    • (1999) Methods: A Companion to Methods in Enzymology , vol.19 , Issue.2 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 61
    • 0023257807 scopus 로고
    • Universal calibration of gel permeation chromatography and determination of molecular shape in solution
    • DOI 10.1016/0003-2697(87)90009-1
    • Potschka M (1987) Universal calibration of gel permeation chromatography and determination of molecular shape in solution. Anal Biochem 162(1):47-64 (Pubitemid 17064301)
    • (1987) Analytical Biochemistry , vol.162 , Issue.1 , pp. 47-64
    • Potschka, M.1
  • 62
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam CD, Hammel M, Hura GL, Tainer JA (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q Rev Biophys 40(03):191-285 (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 63
    • 67651241140 scopus 로고    scopus 로고
    • Circular dichroism techniques: Biomolecular and nanostructural analyses- a review
    • Ranjbar B, Gill P (2009) Circular dichroism techniques: Biomolecular and nanostructural analyses- a review. Chem Biol Drug Des 74(2):101-120
    • (2009) Chem Biol Drug des , vol.74 , Issue.2 , pp. 101-120
    • Ranjbar, B.1    Gill, P.2
  • 66
    • 13844253934 scopus 로고    scopus 로고
    • Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs)
    • DOI 10.1016/j.str.2004.12.006
    • Rivera-Calzada A, Maman JD, Spagnolo L, Pearl LH, Llorca O (2005) Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). Structure 13:243-255 (Pubitemid 40247700)
    • (2005) Structure , vol.13 , Issue.2 , pp. 243-255
    • Rivera-Calzada, A.1    Maman, J.P.2    Spagnolo, L.3    Pearl, L.H.4    Llorca, O.5
  • 67
    • 0029817836 scopus 로고    scopus 로고
    • DNA ligase IV from HeLa cell nuclei
    • DOI 10.1074/jbc.271.39.24257
    • Robins P, Lindahl T (1996) Dna ligase iv from hela cell nuclei. J Biol Chem 271(39): 24257-24261 (Pubitemid 26327414)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.39 , pp. 24257-24261
    • Robins, P.1    Lindahl, T.2
  • 68
    • 14844338484 scopus 로고    scopus 로고
    • Combining X-ray crystallography and electron microscopy
    • DOI 10.1016/j.str.2005.01.005
    • Rossmann M, Morais M, Leiman P, Zhang W (2005) Combining x-ray crystallography and electron microscopy. Structure 13(3):355-362 (Pubitemid 40342874)
    • (2005) Structure , vol.13 , Issue.3 , pp. 355-362
    • Rossmann, M.G.1    Morais, M.C.2    Leiman, P.G.3    Zhang, W.4
  • 70
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379 (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 71
    • 35448971602 scopus 로고    scopus 로고
    • A brief introduction to the analytical ultracentrifugation of proteins for beginners
    • David RAS, Harding SE (eds). The Royal Society of Chemistry, Cambridge. doi: 10.1039/ 9781847552617
    • Scott D, Harding SE, Rowe A (2005) A brief introduction to the analytical ultracentrifugation of proteins for beginners. In: David RAS, Harding SE (eds) Analytical ultracentrifugation: technique and methods. The Royal Society of Chemistry, Cambridge. doi: 10.1039/ 9781847552617
    • (2005) Analytical Ultracentrifugation: Technique and Methods
    • Scott, D.1    Harding, S.E.2    Rowe, A.3
  • 72
    • 33747347236 scopus 로고    scopus 로고
    • Structural organization of the 19 S proteasome lid: Insights from MS of intact complexes
    • doi: 10.1371/journal.pbio.0040267
    • Sharon M, Taverner T, Ambroggio XI, Deshaies RJ, Robinson CV (2006) Structural organization of the 19 S proteasome lid: insights from MS of intact complexes. PLoS Biol 4(8):doi: 10.1371/journal.pbio.0040267
    • (2006) PLoS Biol , vol.4 , Issue.8
    • Sharon, M.1    Taverner, T.2    Ambroggio, X.I.3    Deshaies, R.J.4    Robinson, C.V.5
  • 74
    • 73849140503 scopus 로고    scopus 로고
    • Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats
    • Sibanda BL, Chirgadze D, Blundell TL (2010) Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats. Nature 463(7277):118-121
    • (2010) Nature , vol.463 , Issue.7277 , pp. 118-121
    • Sibanda, B.L.1    Chirgadze, D.2    Blundell, T.L.3
  • 76
    • 0033560796 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase
    • Smith GCM, Jackson SP (1999) The dna-dependent protein kinase. Genes Dev 13(8):916-934 (Pubitemid 29200976)
    • (1999) Genes and Development , vol.13 , Issue.8 , pp. 916-934
    • Smith, G.C.M.1    Jackson, S.P.2
  • 77
    • 33646714595 scopus 로고    scopus 로고
    • Three-Dimensional Structure of the Human DNA-PKcs/Ku70/Ku80 Complex Assembled on DNA and Its Implications for DNA DSB Repair
    • DOI 10.1016/j.molcel.2006.04.013, PII S1097276506002619
    • Spagnolo L, Rivera-Calzada A, Pearl LH, Llorca O (2006) Three-dimensional structure of the human dna-pkcs/ku70/ku80 complex assembled on DNA and its implications for DNA dsb repair. Mol Cell 22(4):511-519 (Pubitemid 43740469)
    • (2006) Molecular Cell , vol.22 , Issue.4 , pp. 511-519
    • Spagnolo, L.1    Rivera-Calzada, A.2    Pearl, L.H.3    Llorca, O.4
  • 78
    • 18744389180 scopus 로고    scopus 로고
    • Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells
    • DOI 10.1038/nmeth752
    • Suchanek M, Radzikowska A, Thiele C (2005) Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. Nat Methods 2(4):261-267. doi: 10.1038/nmeth752 (Pubitemid 41131007)
    • (2005) Nature Methods , vol.2 , Issue.4 , pp. 261-267
    • Suchanek, M.1    Radzikowska, A.2    Thiele, C.3
  • 79
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • DOI 10.1088/0034-4885/66/10/R05, PII S0034488503126887
    • Svergun DI, Koch MHJ (2003) Small-angle scattering studies of biological macromolecules in solution. Rep Prog Phys 66(10):1735-1782 (Pubitemid 37365734)
    • (2003) Reports on Progress in Physics , vol.66 , Issue.10 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 80
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MHJ (2001) Determination of domain structure of proteins from x-ray solution scattering. Biophys J 80(6):2946-2953 (Pubitemid 32521666)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 81
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • DOI 10.1093/emboj/17.18.5497
    • Takata M, Sasaki MS, Sonoda E, Morrison C, Hashimoto M, Utsumi H, Yamaguchi-Iwai Y, Shinohara A, Takeda S (1998) Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in verterbrate cells. EMBO J 17:5497-5508 (Pubitemid 28427063)
    • (1998) EMBO Journal , vol.17 , Issue.18 , pp. 5497-5508
    • Takata, M.1    Sasaki, M.S.2    Sonoda, E.3    Morrison, C.4    Hashimoto, M.5    Utsumi, H.6    Yamaguchi-Iwai, Y.7    Shinohara, A.8    Takeda, S.9
  • 82
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to dna and its implications for double-strand break repair
    • DOI 10.1038/35088000
    • Walker JR, Corpina RA, Goldberg J (2001) Structure of the ku heterodimer bound to dna and its implications for double-strand break repair. Nature 412(6847):607-614 (Pubitemid 32772267)
    • (2001) Nature , vol.412 , Issue.6847 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 83
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells J, McClendon C (2007) Reaching for high-hanging fruit in drug discovery at protein, Aìprotein interfaces. Nature 450:1001-1009 (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 84
    • 38049125555 scopus 로고    scopus 로고
    • The endless tale of non-homologous end-joining
    • Weterings E, Chen DJ (2008) The endless tale of non-homologous end-joining. Cell Res 18(1):114-124
    • (2008) Cell Res , vol.18 , Issue.1 , pp. 114-124
    • Weterings, E.1    Chen, D.J.2
  • 85
    • 40049096125 scopus 로고    scopus 로고
    • Cryo-EM Structure of the DNA-Dependent Protein Kinase Catalytic Subunit at Subnanometer Resolution Reveals α Helices and Insight into DNA Binding
    • DOI 10.1016/j.str.2007.12.014, PII S0969212608000208
    • Williams DR, Lee KJ, Chen DJ, Shi J, Stewart PL (2008) Cryo-EM structure of the DNAdependent protein kinase catalytic subunit at subnanometer resolution reveals alpha helices and insight into DNA binding. Structure 16:468-477 (Pubitemid 351324109)
    • (2008) Structure , vol.16 , Issue.3 , pp. 468-477
    • Williams, D.R.1    Lee, K.-J.2    Shi, J.3    Chen, D.J.4    Stewart, P.L.5
  • 87
    • 80053358977 scopus 로고    scopus 로고
    • Nonhomologous end-joining partners in a helical dance: Structural studies of XLF-XRCC4 interactions
    • Wu Q, Ochi T, Matak-Vinkovic D, Robinson CV, Chirgadze DY, Blundell TL (2011) Nonhomologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions. Biochem Soc Trans 39(5):1387-1392
    • (2011) Biochem Soc Trans , vol.39 , Issue.5 , pp. 1387-1392
    • Wu, Q.1    Ochi, T.2    Matak-Vinkovic, D.3    Robinson, C.V.4    Chirgadze, D.Y.5    Blundell, T.L.6
  • 88
    • 37349121808 scopus 로고    scopus 로고
    • From electron microscopy to X-ray crystallography: Molecular-replacement case studies
    • Xiong Y (2008) From electron microscopy to X-ray crystallography: molecular-replacement case studies. Acta Crystallogr D 64(1):76-82
    • (2008) Acta Crystallogr D , vol.64 , Issue.1 , pp. 76-82
    • Xiong, Y.1
  • 89
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 A cryoem structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Hui WH, Zhou ZH (2010) 3.3 A cryo-em structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141(3):472-482
    • (2010) Cell , vol.141 , Issue.3 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zh, Z.5


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