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Volumn 896, Issue , 2016, Pages 351-368

Application of nuclear magnetic resonance and hybrid methods to structure determination of complex systems

Author keywords

Multidomain proteins; NMR; Protein protein interactions; SAXS; Structural biology

Indexed keywords

4 CARBOXYGLUTAMIC ACID; CAPSID PROTEIN; EPIDERMAL GROWTH FACTOR; FRATAXIN; IRON SULFUR PROTEIN; MALATE SYNTHASE; MALATE SYNTHASE G; UNCLASSIFIED DRUG; MULTIPROTEIN COMPLEX; PROTEIN BINDING; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

EID: 84979084493     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-3-319-27216-0_22     Document Type: Chapter
Times cited : (4)

References (97)
  • 1
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch MH, Vachette P, Svergun DI (2003) Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q Rev Biophys 36(2):147–227
    • (2003) Q Rev Biophys , vol.36 , Issue.2 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 3
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson CV, Sali A, Baumeister W (2007) The molecular sociology of the cell. Nature 450(7172):973–982
    • (2007) Nature , vol.450 , Issue.7172 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 4
    • 79951479408 scopus 로고    scopus 로고
    • Molecular biology. The eukaryotic ribosome
    • Ramakrishnan V (2011) Molecular biology. The eukaryotic ribosome. Science 331(6018):681–682
    • (2011) Science , vol.331 , Issue.6018 , pp. 681-682
    • Ramakrishnan, V.1
  • 6
    • 0007059875 scopus 로고    scopus 로고
    • Principles of nuclear magnetic resonance in one and two dimensions
    • Clarendon Press; Oxford University Press, Oxford
    • Ernst RR, Bodenhausen G, Wokaun A (1997) Principles of nuclear magnetic resonance in one and two dimensions. The international series of monographs on chemistry, vol 14. Clarendon Press; Oxford University Press, Oxford
    • (1997) The International Series of Monographs on Chemistry , vol.14
    • Ernst, R.R.1    Bodenhausen, G.2    Wokaun, A.3
  • 7
    • 0041930989 scopus 로고    scopus 로고
    • Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE (2003) Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc 125(34):10420–10428
    • (2003) J am Chem Soc , vol.125 , Issue.34 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 8
    • 0024351231 scopus 로고
    • Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy
    • Clore GM, Gronenborn AM (1989) Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. Crit Rev Biochem Mol Biol 24(5):479–564
    • (1989) Crit Rev Biochem Mol Biol , vol.24 , Issue.5 , pp. 479-564
    • Clore, G.M.1    Gronenborn, A.M.2
  • 9
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278(5340):1111–1114
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 10
    • 0034167156 scopus 로고    scopus 로고
    • Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings
    • Al-Hashimi HM, Valafar H, Terrell M, Zartler ER, Eidsness MK, Prestegard JH (2000) Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings. J Magn Reson 143(2):402–406
    • (2000) J Magn Reson , vol.143 , Issue.2 , pp. 402-406
    • Al-Hashimi, H.M.1    Valafar, H.2    Terrell, M.3    Zartler, E.R.4    Eidsness, M.K.5    Prestegard, J.H.6
  • 11
    • 0034254909 scopus 로고    scopus 로고
    • Accurate and rapid docking of protein- protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization
    • Clore GM (2000) Accurate and rapid docking of protein- protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization. Proc Natl Acad Sci U S A 97(16):9021–9025
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.16 , pp. 9021-9025
    • Clore, G.M.1
  • 12
    • 37849015942 scopus 로고    scopus 로고
    • Highresolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment
    • Rumpel S, Becker S, Zweckstetter M (2008) Highresolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment. J Biomol NMR 40(1):1–13
    • (2008) J Biomol NMR , vol.40 , Issue.1 , pp. 1-13
    • Rumpel, S.1    Becker, S.2    Zweckstetter, M.3
  • 13
    • 0037433504 scopus 로고    scopus 로고
    • Docking of proteinprotein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N- 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • Clore GM, Schwieters CD (2003) Docking of proteinprotein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N- 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics. J Am Chem Soc 125(10):2902–2912
    • (2003) J am Chem Soc , vol.125 , Issue.10 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 15
    • 80051492024 scopus 로고    scopus 로고
    • Oligomeric structure of the chemokine CCL5/RANTES from NMR, MS, and SAXS data
    • Wang X, Watson C, Sharp JS, Handel TM, Prestegard JH (2011) Oligomeric structure of the chemokine CCL5/RANTES from NMR, MS, and SAXS data. Structure 19(8):1138–1148
    • (2011) Structure , vol.19 , Issue.8 , pp. 1138-1148
    • Wang, X.1    Watson, C.2    Sharp, J.S.3    Handel, T.M.4    Prestegard, J.H.5
  • 16
    • 0033562633 scopus 로고    scopus 로고
    • Use of pair potentials across protein interfaces in screening predicted docked complexes
    • Moont G, Gabb HA, Sternberg MJ (1999) Use of pair potentials across protein interfaces in screening predicted docked complexes. Proteins 35(3):364–373
    • (1999) Proteins , vol.35 , Issue.3 , pp. 364-373
    • Moont, G.1    Gabb, H.A.2    Sternberg, M.J.3
  • 17
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, Kern D (2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450(7171):913–916
    • (2007) Nature , vol.450 , Issue.7171 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 18
    • 78650811435 scopus 로고    scopus 로고
    • Structural biology: Proteins in dynamic equilibrium
    • Bernado P, Blackledge M (2010) Structural biology: proteins in dynamic equilibrium. Nature 468(7327):1046–1048
    • (2010) Nature , vol.468 , Issue.7327 , pp. 1046-1048
    • Bernado, P.1    Blackledge, M.2
  • 20
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernado P, Mylonas E, Petoukhov MV, Blackledge M, Svergun DI (2007) Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc 129(17):5656–5664
    • (2007) J am Chem Soc , vol.129 , Issue.17 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 21
    • 0029840317 scopus 로고    scopus 로고
    • The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study
    • Sunnerhagen M, Olah GA, Stenflo J, Forsen S, Drakenberg T, Trewhella J (1996) The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. Biochemistry 35(36):11547–11559
    • (1996) Biochemistry , vol.35 , Issue.36 , pp. 11547-11559
    • Sunnerhagen, M.1    Olah, G.A.2    Stenflo, J.3    Forsen, S.4    Drakenberg, T.5    Trewhella, J.6
  • 22
    • 45449109207 scopus 로고    scopus 로고
    • Small angle neutron and X-ray scattering in structural biology: Recent examples from the literature
    • Neylon C (2008) Small angle neutron and X-ray scattering in structural biology: recent examples from the literature. Eur Biophys J 37(5):531–541
    • (2008) Eur Biophys J , vol.37 , Issue.5 , pp. 531-541
    • Neylon, C.1
  • 24
    • 3242861343 scopus 로고    scopus 로고
    • The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyanocytochrome c as an example
    • Banci L, Bertini I, Bren KL, Cremonini MA, Gray HB, Luchinat C, Turano P (1996) The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyanocytochrome c as an example. J Biol Inorg Chem 1:117–126
    • (1996) J Biol Inorg Chem , vol.1 , pp. 117-126
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Cremonini, M.A.4    Gray, H.B.5    Luchinat, C.6    Turano, P.7
  • 25
    • 0029185933 scopus 로고
    • CRYSOL –a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, Koch MH (1995) CRYSOL –a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28:768–773
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 26
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin’s flexibility allows for promiscuity in its interactions with target proteins and peptides
    • Yamniuk AP, Vogel HJ (2004) Calmodulin’s flexibility allows for promiscuity in its interactions with target proteins and peptides. Mol Biotechnol 27(1):33–57
    • (2004) Mol Biotechnol , vol.27 , Issue.1 , pp. 33-57
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 28
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu YS, Bugg CE, Cook WJ (1988) Structure of calmodulin refined at 2.2 A resolution. J Mol Biol 204(1):191–204
    • (1988) J Mol Biol , vol.204 , Issue.1 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 29
    • 0141594755 scopus 로고    scopus 로고
    • A closed compact structure of native Ca(2+)-calmodulin
    • Fallon JL, Quiocho FA (2003) A closed compact structure of native Ca(2+)-calmodulin. Structure 11(10):1303–1307
    • (2003) Structure , vol.11 , Issue.10 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 30
    • 33749246223 scopus 로고    scopus 로고
    • Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode
    • Maximciuc AA, Putkey JA, Shamoo Y, Mackenzie KR (2006) Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode. Structure 14(10):1547–1556
    • (2006) Structure , vol.14 , Issue.10 , pp. 1547-1556
    • Maximciuc, A.A.1    Putkey, J.A.2    Shamoo, Y.3    Mackenzie, K.R.4
  • 31
    • 77951648455 scopus 로고    scopus 로고
    • Molecular basis of the death- associated protein kinase-calcium/calmodulin regulator complex
    • de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M (2010) Molecular basis of the death- associated protein kinase-calcium/calmodulin regulator complex. Sci Signal 3(106):ra6
    • (2010) Sci Signal , vol.3 , Issue.106
    • De Diego, I.1    Kuper, J.2    Bakalova, N.3    Kursula, P.4    Wilmanns, M.5
  • 32
    • 0037450635 scopus 로고    scopus 로고
    • Structural basis for endothelial nitric oxide synthase binding to calmodulin
    • Aoyagi M, Arvai AS, Tainer JA, Getzoff ED (2003) Structural basis for endothelial nitric oxide synthase binding to calmodulin. EMBO J 22(4):766–775
    • (2003) EMBO J , vol.22 , Issue.4 , pp. 766-775
    • Aoyagi, M.1    Arvai, A.S.2    Tainer, J.A.3    Getzoff, E.D.4
  • 33
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures
    • Meador WE, Means AR, Quiocho FA (1993) Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Science 262(5140):1718–1721
    • (1993) Science , vol.262 , Issue.5140 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 34
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
    • Meador WE, Means AR, Quiocho FA (1992) Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257(5074):1251–1255
    • (1992) Science , vol.257 , Issue.5074 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 35
    • 0035823139 scopus 로고    scopus 로고
    • Target-induced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca(2+)/calmodulin-dependent kinase kinase peptide
    • Kurokawa H, Osawa M, Kurihara H, Katayama N, Tokumitsu H, Swindells MB, Kainosho M, Ikura M (2001) Target-induced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca(2+)/calmodulin-dependent kinase kinase peptide. J Mol Biol 312(1):59–68
    • (2001) J Mol Biol , vol.312 , Issue.1 , pp. 59-68
    • Kurokawa, H.1    Osawa, M.2    Kurihara, H.3    Katayama, N.4    Tokumitsu, H.5    Swindells, M.B.6    Kainosho, M.7    Ikura, M.8
  • 36
    • 0034753415 scopus 로고    scopus 로고
    • Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains
    • Chou JJ, Li S, Klee CB, Bax A (2001) Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains. Nat Struct Biol 8(11):990–997
    • (2001) Nat Struct Biol , vol.8 , Issue.11 , pp. 990-997
    • Chou, J.J.1    Li, S.2    Klee, C.B.3    Bax, A.4
  • 37
    • 0026536335 scopus 로고
    • Solution structure of a calmodulintarget peptide complex by multidimensional NMR
    • Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A (1992) Solution structure of a calmodulintarget peptide complex by multidimensional NMR. Science 256(5057):632–638
    • (1992) Science , vol.256 , Issue.5057 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 38
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich KP, Ikura M (2002) Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108(6):739–742
    • (2002) Cell , vol.108 , Issue.6 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 39
    • 84900828258 scopus 로고    scopus 로고
    • Transient electrostatic interactions dominate the conformational equilibrium sampled by multidomain splicing factor U2AF65: A combined NMR and SAXS study
    • Huang JR, Warner LR, Sanchez C, Gabel F, Madl T, Mackereth CD, Sattler M, Blackledge M (2014) Transient electrostatic interactions dominate the conformational equilibrium sampled by multidomain splicing factor U2AF65: a combined NMR and SAXS study. J Am Chem Soc 136(19):7068–7076
    • (2014) J am Chem Soc , vol.136 , Issue.19 , pp. 7068-7076
    • Huang, J.R.1    Warner, L.R.2    Sanchez, C.3    Gabel, F.4    Madl, T.5    Mackereth, C.D.6    Sattler, M.7    Blackledge, M.8
  • 43
    • 28444453002 scopus 로고    scopus 로고
    • Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data
    • Grishaev A, Wu J, Trewhella J, Bax A (2005) Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. J Am Chem Soc 127(47):16621–16628
    • (2005) J am Chem Soc , vol.127 , Issue.47 , pp. 16621-16628
    • Grishaev, A.1    Wu, J.2    Trewhella, J.3    Bax, A.4
  • 45
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80(6):2946–2953
    • (2001) Biophys J , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 46
    • 0031807272 scopus 로고    scopus 로고
    • Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm
    • Chacon P, Moran F, Diaz JF, Pantos E, Andreu JM (1998) Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm. Biophys J 74(6):2760–2775
    • (1998) Biophys J , vol.74 , Issue.6 , pp. 2760-2775
    • Chacon, P.1    Moran, F.2    Diaz, J.F.3    Pantos, E.4    Reu, J.M.5
  • 48
    • 38349018735 scopus 로고    scopus 로고
    • Refined solution structure of the 82- kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints
    • Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A (2008) Refined solution structure of the 82- kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. J Biomol NMR 40(2):95–106
    • (2008) J Biomol NMR , vol.40 , Issue.2 , pp. 95-106
    • Grishaev, A.1    Tugarinov, V.2    Kay, L.E.3    Trewhella, J.4    Bax, A.5
  • 49
    • 54049155019 scopus 로고    scopus 로고
    • Solution structure of tRNAVal from refinement of homology model against residual dipolar coupling and SAXS data
    • Grishaev A, Ying J, Canny MD, Pardi A, Bax A (2008) Solution structure of tRNAVal from refinement of homology model against residual dipolar coupling and SAXS data. J Biomol NMR 42(2):99–109
    • (2008) J Biomol NMR , vol.42 , Issue.2 , pp. 99-109
    • Grishaev, A.1    Ying, J.2    Canny, M.D.3    Pardi, A.4    Bax, A.5
  • 50
    • 77956641793 scopus 로고    scopus 로고
    • Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering
    • Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM (2010) Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. J Am Chem Soc 132(37):13026–13045
    • (2010) J am Chem Soc , vol.132 , Issue.37 , pp. 13026-13045
    • Schwieters, C.D.1    Suh, J.Y.2    Grishaev, A.3    Ghirlando, R.4    Takayama, Y.5    Clore, G.M.6
  • 51
    • 79851489016 scopus 로고    scopus 로고
    • Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid-body conformational transitions in a nonphosphorylatable active-site mutant of the 128 kDa enzyme I dimer
    • Takayama Y, Schwieters CD, Grishaev A, Ghirlando R, Clore GM (2011) Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid-body conformational transitions in a nonphosphorylatable active-site mutant of the 128 kDa enzyme I dimer. J Am Chem Soc 133(3):424–427
    • (2011) J am Chem Soc , vol.133 , Issue.3 , pp. 424-427
    • Takayama, Y.1    Schwieters, C.D.2    Grishaev, A.3    Ghirlando, R.4    Clore, G.M.5
  • 53
    • 0037449145 scopus 로고    scopus 로고
    • Highresolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract
    • Basak A, Bateman O, Slingsby C, Pande A, Asherie N, Ogun O, Benedek GB, Pande J (2003) Highresolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract. J Mol Biol 328(5):1137–1147
    • (2003) J Mol Biol , vol.328 , Issue.5 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Slingsby, C.3    Pande, A.4    Asherie, N.5    Ogun, O.6    Benedek, G.B.7    Pande, J.8
  • 55
    • 0034696680 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: Mechanistic implications
    • Howard BR, Endrizzi JA, Remington SJ (2000) Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Biochemistry 39(11):3156–3168
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 3156-3168
    • Howard, B.R.1    Endrizzi, J.A.2    Remington, S.J.3
  • 58
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • Ganser BK, Li S, Klishko VY, Finch JT, Sundquist WI (1999) Assembly and analysis of conical models for the HIV-1 core. Science 283(5398):80–83
    • (1999) Science , vol.283 , Issue.5398 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 60
    • 78751670547 scopus 로고    scopus 로고
    • Atomic-level modelling of the HIV capsid
    • Pornillos O, Ganser-Pornillos BK, Yeager M (2011) Atomic-level modelling of the HIV capsid. Nature 469(7330):424–427
    • (2011) Nature , vol.469 , Issue.7330 , pp. 424-427
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Yeager, M.3
  • 61
    • 0031680643 scopus 로고    scopus 로고
    • The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly
    • Borsetti A, Ohagen A, Gottlinger HG (1998) The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly. J Virol 72(11):9313–9317
    • (1998) J Virol , vol.72 , Issue.11 , pp. 9313-9317
    • Borsetti, A.1    Ohagen, A.2    Gottlinger, H.G.3
  • 62
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid- p2 and a late assembly domain
    • Accola MA, Strack B, Gottlinger HG (2000) Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid- p2 and a late assembly domain. J Virol 74(12):5395–5402
    • (2000) J Virol , vol.74 , Issue.12 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 64
    • 70350771279 scopus 로고    scopus 로고
    • Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function
    • Byeon IJ, Meng X, Jung J, Zhao G, Yang R, Ahn J, Shi J, Concel J, Aiken C, Zhang P, Gronenborn AM (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139(4):780–790
    • (2009) Cell , vol.139 , Issue.4 , pp. 780-790
    • Byeon, I.J.1    Meng, X.2    Jung, J.3    Zhao, G.4    Yang, R.5    Ahn, J.6    Shi, J.7    Concel, J.8    Aiken, C.9    Zhang, P.10    Gronenborn, A.M.11
  • 69
    • 33644825600 scopus 로고    scopus 로고
    • A target function for quaternary structural refinement from small angle scattering and NMR orientational restraints
    • Gabel F, Simon B, Sattler M (2006) A target function for quaternary structural refinement from small angle scattering and NMR orientational restraints. Eur Biophys J 35(4):313–327
    • (2006) Eur Biophys J , vol.35 , Issue.4 , pp. 313-327
    • Gabel, F.1    Simon, B.2    Sattler, M.3
  • 70
    • 50349088228 scopus 로고    scopus 로고
    • A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints
    • Gabel F, Simon B, Nilges M, Petoukhov M, Svergun D, Sattler M (2008) A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints. J Biomol NMR 41(4):199–208
    • (2008) J Biomol NMR , vol.41 , Issue.4 , pp. 199-208
    • Gabel, F.1    Simon, B.2    Nilges, M.3    Petoukhov, M.4    Svergun, D.5    Sattler, M.6
  • 71
    • 36348979305 scopus 로고    scopus 로고
    • A simple genetic algorithm for the optimization of multidomain protein homology models driven by NMR residual dipolar coupling and small angle X-ray scattering data
    • Mareuil F, Sizun C, Perez J, Schoenauer M, Lallemand JY, Bontems F (2007) A simple genetic algorithm for the optimization of multidomain protein homology models driven by NMR residual dipolar coupling and small angle X-ray scattering data. Eur Biophys J 37(1):95–104
    • (2007) Eur Biophys J , vol.37 , Issue.1 , pp. 95-104
    • Mareuil, F.1    Sizun, C.2    Perez, J.3    Schoenauer, M.4    Lallemand, J.Y.5    Bontems, F.6
  • 72
    • 82055161782 scopus 로고    scopus 로고
    • DADIMODO: A program for refining the structure of multidomain proteins and complexes against small-angle scattering data and NMR-derived restraints
    • Evrard G, Mareuil F, Bontems F, Sizun C, Perez J (2011) DADIMODO: a program for refining the structure of multidomain proteins and complexes against small-angle scattering data and NMR-derived restraints. J Appl Crystallogr 44:7
    • (2011) J Appl Crystallogr , vol.44 , pp. 7
    • Evrard, G.1    Mareuil, F.2    Bontems, F.3    Sizun, C.4    Perez, J.5
  • 73
    • 40549143036 scopus 로고    scopus 로고
    • The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data
    • Parsons LM, Grishaev A, Bax A (2008) The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data. Biochemistry 47(10):3131–3142
    • (2008) Biochemistry , vol.47 , Issue.10 , pp. 3131-3142
    • Parsons, L.M.1    Grishaev, A.2    Bax, A.3
  • 74
    • 0036180995 scopus 로고    scopus 로고
    • Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity
    • Cascales E, Bernadac A, Gavioli M, Lazzaroni JC, Lloubes R (2002) Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J Bacteriol 184(3):754–759
    • (2002) J Bacteriol , vol.184 , Issue.3 , pp. 754-759
    • Cascales, E.1    Bernadac, A.2    Gavioli, M.3    Lazzaroni, J.C.4    Lloubes, R.5
  • 75
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction
    • Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA (2007) The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol Microbiol 63(4):1008–1025
    • (2007) E. Coli. Mol Microbiol , vol.63 , Issue.4 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    De Boer, P.A.5
  • 76
    • 0033631450 scopus 로고    scopus 로고
    • Molecular symmetry as an aid to geometry determination in ligand protein complexes
    • Al-Hashimi HM, Bolon PJ, Prestegard JH (2000) Molecular symmetry as an aid to geometry determination in ligand protein complexes. J Magn Reson 142(1):153–158
    • (2000) J Magn Reson , vol.142 , Issue.1 , pp. 153-158
    • Al-Hashimi, H.M.1    Bolon, P.J.2    Prestegard, J.H.3
  • 77
    • 33747343901 scopus 로고    scopus 로고
    • Variable dimerization of the Ly49A natural killer cell receptor results in differential engagement of its MHC class I ligand
    • Dam J, Baber J, Grishaev A, Malchiodi EL, Schuck P, Bax A, Mariuzza RA (2006) Variable dimerization of the Ly49A natural killer cell receptor results in differential engagement of its MHC class I ligand. J Mol Biol 362(1):102–113
    • (2006) J Mol Biol , vol.362 , Issue.1 , pp. 102-113
    • Dam, J.1    Baber, J.2    Grishaev, A.3    Malchiodi, E.L.4    Schuck, P.5    Bax, A.6    Mariuzza, R.A.7
  • 79
    • 38349001213 scopus 로고    scopus 로고
    • Comparison of alignment tensors generated for native tRNA(Val) using magnetic fields and liquid crystalline media
    • Latham MP, Hanson P, Brown DJ, Pardi A (2008) Comparison of alignment tensors generated for native tRNA(Val) using magnetic fields and liquid crystalline media. J Biomol NMR 40(2):83–94
    • (2008) J Biomol NMR , vol.40 , Issue.2 , pp. 83-94
    • Latham, M.P.1    Hanson, P.2    Brown, D.J.3    Pardi, A.4
  • 80
    • 41449107849 scopus 로고    scopus 로고
    • Global molecular structure and interfaces: Refining an RNA:RNA complex structure using solution X-ray scattering data
    • Zuo X, Wang J, Foster TR, Schwieters CD, Tiede DM, Butcher SE, Wang YX (2008) Global molecular structure and interfaces: refining an RNA:RNA complex structure using solution X-ray scattering data. J Am Chem Soc 130(11):3292–3293
    • (2008) J am Chem Soc , vol.130 , Issue.11 , pp. 3292-3293
    • Zuo, X.1    Wang, J.2    Foster, T.R.3    Schwieters, C.D.4    Tiede, D.M.5    Butcher, S.E.6    Wang, Y.X.7
  • 81
    • 0028921811 scopus 로고
    • Frequent use of the same tertiary motif by self-folding RNAs
    • Costa M, Michel F (1995) Frequent use of the same tertiary motif by self-folding RNAs. EMBO J 14(6):1276–1285
    • (1995) EMBO J , vol.14 , Issue.6 , pp. 1276-1285
    • Costa, M.1    Michel, F.2
  • 82
    • 22444437410 scopus 로고    scopus 로고
    • RNA helical packing in solution: NMR structure of a 30 kDa GAAA tetraloopreceptor complex
    • Davis JH, Tonelli M, Scott LG, Jaeger L, Williamson JR, Butcher SE (2005) RNA helical packing in solution: NMR structure of a 30 kDa GAAA tetraloopreceptor complex. J Mol Biol 351(2):371–382
    • (2005) J Mol Biol , vol.351 , Issue.2 , pp. 371-382
    • Davis, J.H.1    Tonelli, M.2    Scott, L.G.3    Jaeger, L.4    Williamson, J.R.5    Butcher, S.E.6
  • 83
    • 33845874649 scopus 로고    scopus 로고
    • Role of metal ions in the tetraloop-receptor complex as analyzed by NMR
    • Davis JH, Foster TR, Tonelli M, Butcher SE (2007) Role of metal ions in the tetraloop-receptor complex as analyzed by NMR. RNA 13(1):76–86
    • (2007) RNA , vol.13 , Issue.1 , pp. 76-86
    • Davis, J.H.1    Foster, T.R.2    Tonelli, M.3    Butcher, S.E.4
  • 84
    • 62549093116 scopus 로고    scopus 로고
    • The pathogenesis of Friedreich ataxia and the structure and function of frataxin
    • Pandolfo M, Pastore A (2009) The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J Neurol 256(Suppl 1):9–17
    • (2009) J Neurol , vol.256 , pp. 9-17
    • Pandolfo, M.1    Pastore, A.2
  • 86
    • 0035977015 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • Urbina HD, Silberg JJ, Hoff KG, Vickery LE (2001) Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. J Biol Chem 276(48):44521–44526
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 44521-44526
    • Urbina, H.D.1    Silberg, J.J.2    Hoff, K.G.3    Vickery, L.E.4
  • 89
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C, Boelens R, Bonvin AM (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc 125(7):1731–1737
    • (2003) J am Chem Soc , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 91
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon T, Cowan JA (2003) Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J Am Chem Soc 125(20):6078–6084
    • (2003) J am Chem Soc , vol.125 , Issue.20 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 93
    • 69249084026 scopus 로고    scopus 로고
    • Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis
    • Li H, Gakh O, Smith DY, Isaya G (2009) Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis. J Biol Chem 284(33):21971–21980
    • (2009) J Biol Chem , vol.284 , Issue.33 , pp. 21971-21980
    • Li, H.1    Gakh, O.2    Smith, D.Y.3    Isaya, G.4
  • 96
    • 7944225865 scopus 로고    scopus 로고
    • Solution structure of the bacterial frataxin ortholog, CyaY: Mapping the iron binding sites
    • Nair M, Adinolfi S, Pastore C, Kelly G, Temussi P, Pastore A (2004) Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Structure 12(11):2037–2048
    • (2004) Structure , vol.12 , Issue.11 , pp. 2037-2048
    • Nair, M.1    Adinolfi, S.2    Pastore, C.3    Kelly, G.4    Temussi, P.5    Pastore, A.6
  • 97
    • 0038351831 scopus 로고    scopus 로고
    • Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
    • Cupp-Vickery JR, Urbina H, Vickery LE (2003) Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J Mol Biol 330(5):1049–1059
    • (2003) J Mol Biol , vol.330 , Issue.5 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3


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