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Volumn 26, Issue 46, 2014, Pages

Large, dynamic, multi-protein complexes: A challenge for structural biology

Author keywords

Hybrid methods of structural biology; Multi protein complexes; Protein structure

Indexed keywords

BIOLOGY; NUCLEIC ACIDS;

EID: 84908374097     PISSN: 09538984     EISSN: 1361648X     Source Type: Journal    
DOI: 10.1088/0953-8984/26/46/463103     Document Type: Article
Times cited : (26)

References (84)
  • 1
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Kruse A C et al 2013 Activation and allosteric modulation of a muscarinic acetylcholine receptor Nature 504 101-6
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1
  • 2
    • 84867840947 scopus 로고    scopus 로고
    • Structure of the agonist-bound neurotensin receptor
    • White J F et al 2012 Structure of the agonist-bound neurotensin receptor Nature 490 508-13
    • (2012) Nature , vol.490 , pp. 508-513
    • White, J.F.1
  • 3
    • 84861975966 scopus 로고    scopus 로고
    • Crystal structure of human enterovirus 71
    • Plevka P et al 2012 Crystal structure of human enterovirus 71 Science 336 1274
    • (2012) Science , vol.336 , pp. 1274
    • Plevka, P.1
  • 4
    • 84879067087 scopus 로고    scopus 로고
    • Overcoming mutation-based resistance to antiandrogens with rational drug design
    • Balbas M D et al 2013 Overcoming mutation-based resistance to antiandrogens with rational drug design eLife 2 e00499
    • (2013) ELife , vol.2
    • Balbas, M.D.1
  • 5
    • 84870810902 scopus 로고    scopus 로고
    • Biophysical and computational fragment-based approaches to targeting protein-protein interactions: Applications in structure-guided drug discovery
    • Winter A et al 2012 Biophysical and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery Q. Rev. Biophys. 45 383-426
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 383-426
    • Winter, A.1
  • 7
    • 84877778935 scopus 로고    scopus 로고
    • Super-resolution in solution x-ray scattering and its applications to structural systems biology
    • Rambo R P and Tainer J A 2013 Super-resolution in solution x-ray scattering and its applications to structural systems biology Annu. Rev. Biophys. 42 415-41
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 415-441
    • Rambo, R.P.1    Tainer, J.A.2
  • 8
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • Rozycki B, Kim Y C and Hummer G 2011 SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions Structure 19 109-16
    • (2011) Structure , vol.19 , pp. 109-116
    • Rozycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 9
    • 78651258167 scopus 로고    scopus 로고
    • EROS: Better than SAXS!
    • Yang S and Roux B 2011 EROS: Better than SAXS! Structure 19 3-4
    • (2011) Structure , vol.19 , pp. 3-4
    • Yang, S.1    Roux, B.2
  • 10
    • 84868097048 scopus 로고    scopus 로고
    • Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes
    • Rozycki B et al 2012 Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes PLoS Comput. Biol. 8 e1002736
    • (2012) PLoS Comput. Biol. , vol.8
    • Rozycki, B.1
  • 11
    • 84863115372 scopus 로고    scopus 로고
    • Assembly and architecture of biogenesis of lysosome-related organelles complex-1 (BLOC-1)
    • Lee H H et al 2012 Assembly and architecture of biogenesis of lysosome-related organelles complex-1 (BLOC-1) J. Biol. Chem. 287 5882-90
    • (2012) J. Biol. Chem. , vol.287 , pp. 5882-5890
    • Lee, H.H.1
  • 12
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai X C et al 2013 Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles eLife 2 e00461
    • (2013) ELife , vol.2
    • Bai, X.C.1
  • 13
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • Grigorieff N and Harrison S C 2011 Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy Curr. Opin. Struct. Biol. 21 265-73
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 265-273
    • Grigorieff, N.1    Harrison, S.C.2
  • 14
    • 84904560883 scopus 로고    scopus 로고
    • Three-dimensional structure of human gamma-secretase
    • Lu P et al 2014 Three-dimensional structure of human gamma-secretase Nature 512 166-70
    • (2014) Nature , vol.512 , pp. 166-170
    • Lu, P.1
  • 15
    • 84905911542 scopus 로고    scopus 로고
    • Structural biology. Beyond blob-ology
    • Smith M T and Rubinstein J L 2014 Structural biology. Beyond blob-ology Science 345 617-9
    • (2014) Science , vol.345 , pp. 617-619
    • Smith, M.T.1    Rubinstein, J.L.2
  • 18
    • 84885833311 scopus 로고    scopus 로고
    • NMR methods for structural studies of large monomeric and multimeric proteins
    • Frueh D P et al 2013 NMR methods for structural studies of large monomeric and multimeric proteins Curr. Opin. Struct. Biol. 23 734-9
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 734-739
    • Frueh, D.P.1
  • 20
    • 79958037883 scopus 로고    scopus 로고
    • Constructing ensembles for intrinsically disordered proteins
    • Fisher C K and Stultz C M 2011 Constructing ensembles for intrinsically disordered proteins Curr. Opin. Struct. Biol. 21 426-31
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 426-431
    • Fisher, C.K.1    Stultz, C.M.2
  • 21
    • 84860259978 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: From sequence and conformational properties toward drug discovery
    • Rezaei-Ghaleh N, Blackledge M and Zweckstetter M 2012 Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery ChemBioChem 13 930-50
    • (2012) ChemBioChem , vol.13 , pp. 930-950
    • Rezaei-Ghaleh, N.1    Blackledge, M.2    Zweckstetter, M.3
  • 22
    • 84879177976 scopus 로고    scopus 로고
    • Describing intrinsically disordered proteins at atomic resolution by NMR
    • Jensen M R, Ruigrok R W H and Blackledge M 2013 Describing intrinsically disordered proteins at atomic resolution by NMR Curr. Opin. Struct. Biol. 23 426-35
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 426-435
    • Jensen, M.R.1    Ruigrok, R.W.H.2    Blackledge, M.3
  • 23
    • 84865347103 scopus 로고    scopus 로고
    • Analysis of intrinsically disordered proteins by small-angle x-ray scattering
    • Bernado P and Svergun D I 2012 Analysis of intrinsically disordered proteins by small-angle x-ray scattering Methods Mol. Biol. 896 107-22
    • (2012) Methods Mol. Biol. , vol.896 , pp. 107-122
    • Bernado, P.1    Svergun, D.I.2
  • 24
    • 82655179912 scopus 로고    scopus 로고
    • Understanding the structural ensembles of a highly extended disordered protein
    • Daughdrill G W et al 2012 Understanding the structural ensembles of a highly extended disordered protein Mol. Biosyst. 8 308-19
    • (2012) Mol. Biosyst. , vol.8 , pp. 308-319
    • Daughdrill, G.W.1
  • 25
    • 79959371395 scopus 로고    scopus 로고
    • Solution structure of the ESCRT-I complex by small-angle x-ray scattering, EPR, and FRET spectroscopy
    • Boura E et al 2011 Solution structure of the ESCRT-I complex by small-angle x-ray scattering, EPR, and FRET spectroscopy Proc. Natl Acad. Sci. USA 108 9437-42
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9437-9442
    • Boura, E.1
  • 26
    • 84865035887 scopus 로고    scopus 로고
    • Endosomal sorting complex required for transport (ESCRT) complexes induce phase-separated microdomains in supported lipid bilayers
    • Boura E et al 2012 Endosomal sorting complex required for transport (ESCRT) complexes induce phase-separated microdomains in supported lipid bilayers J. Biol. Chem. 287 28144-51
    • (2012) J. Biol. Chem. , vol.287 , pp. 28144-28151
    • Boura, E.1
  • 27
    • 77951248675 scopus 로고    scopus 로고
    • Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9
    • Kloer D P et al 2010 Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9 J. Biol. Chem. 285 7794-804
    • (2010) J. Biol. Chem. , vol.285 , pp. 7794-7804
    • Kloer, D.P.1
  • 28
    • 84871581862 scopus 로고    scopus 로고
    • Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis
    • Ragusa M J, Stanley R E and Hurley J H 2012 Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis Cell 151 1501-12
    • (2012) Cell , vol.151 , pp. 1501-1512
    • Ragusa, M.J.1    Stanley, R.E.2    Hurley, J.H.3
  • 29
    • 84888042652 scopus 로고    scopus 로고
    • Bayesian analysis of individual electron microscopy images: Towards structures of dynamic and heterogeneous biomolecular assemblies
    • Cossio P and Hummer G 2013 Bayesian analysis of individual electron microscopy images: towards structures of dynamic and heterogeneous biomolecular assemblies J. Struct. Biol. 184 427-37
    • (2013) J. Struct. Biol. , vol.184 , pp. 427-437
    • Cossio, P.1    Hummer, G.2
  • 30
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle x-ray scattering
    • Bernado P et al 2007 Structural characterization of flexible proteins using small-angle x-ray scattering J. Am. Chem. Soc. 129 5656-64
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernado, P.1
  • 31
    • 77957655386 scopus 로고    scopus 로고
    • Multidomain assembled states of Hck tyrosine kinase in solution
    • Yang S et al 2010 Multidomain assembled states of Hck tyrosine kinase in solution Proc. Natl Acad. Sci. USA 107 15757-62
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 15757-15762
    • Yang, S.1
  • 32
    • 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 et al 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 1264-71
    • (2011) J. Appl. Crystallogr. , vol.44 , pp. 1264-1271
    • Evrard, G.1
  • 33
    • 84885861180 scopus 로고    scopus 로고
    • Impact and progress in small and wide angle x-ray scattering (SAXS and WAXS)
    • Graewert M A and Svergun D I 2013 Impact and progress in small and wide angle x-ray scattering (SAXS and WAXS) Curr. Opin. Struct. Biol. 23 748-54
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 748-754
    • Graewert, M.A.1    Svergun, D.I.2
  • 34
    • 84875982643 scopus 로고    scopus 로고
    • Small-angle x-ray scattering on biological macromolecules and nanocomposites in solution
    • Blanchet C E and Svergun D I 2013 Small-angle x-ray scattering on biological macromolecules and nanocomposites in solution Annu. Rev. Phys. Chem. 64 37-54
    • (2013) Annu. Rev. Phys. Chem. , vol.64 , pp. 37-54
    • Blanchet, C.E.1    Svergun, D.I.2
  • 35
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab initio shape determination in small-angle scattering
    • Franke D and Svergun D I 2009 DAMMIF, a program for rapid ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 342-6
    • (2009) J. Appl. Crystallogr. , vol.42 , Issue.2 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 36
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun D I, Petoukhov M V and Koch M H J 2001 Determination of domain structure of proteins from x-ray solution scattering Biophys. J. 80 2946-53
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 37
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov M V et al 2012 New developments in the ATSAS program package for small-angle scattering data analysis J. Appl. Crystallogr. 45 342-50
    • (2012) J. Appl. Crystallogr. , vol.45 , pp. 342-350
    • Petoukhov, M.V.1
  • 38
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C and Koch M H J 1995 CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 768-73
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 39
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M V and Svergun D I 2005 Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 1237-50
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 40
    • 77954627025 scopus 로고    scopus 로고
    • Free state conformational sampling of the SAM-I riboswitch aptamer domain
    • Stoddard C D et al 2010 Free state conformational sampling of the SAM-I riboswitch aptamer domain Structure 18 787-97
    • (2010) Structure , vol.18 , pp. 787-797
    • Stoddard, C.D.1
  • 41
    • 84055217520 scopus 로고    scopus 로고
    • Accurate flexible fitting of high-resolution protein structures to small-angle x-ray scattering data using a coarse-grained model with implicit hydration shell
    • Zheng W J and Tekpinar M 2011 Accurate flexible fitting of high-resolution protein structures to small-angle x-ray scattering data using a coarse-grained model with implicit hydration shell Biophys. J. 101 2981-91
    • (2011) Biophys. J. , vol.101 , pp. 2981-2991
    • Zheng, W.J.1    Tekpinar, M.2
  • 42
    • 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 et al 2008 Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints J. Biomol. NMR 40 95-106
    • (2008) J. Biomol. NMR , vol.40 , pp. 95-106
    • Grishaev, A.1
  • 43
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • Schneidman-Duhovny D, Hammel M and Sali A 2010 FoXS: a web server for rapid computation and fitting of SAXS profiles Nucl. Acids Res. 38 W540-4
    • (2010) Nucl. Acids Res. , vol.38 , pp. 540-W544
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 44
    • 78149240323 scopus 로고    scopus 로고
    • Improved fitting of solution x-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling
    • Grishaev A et al 2010 Improved fitting of solution x-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling J. Am. Chem. Soc. 132 15484-6
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15484-15486
    • Grishaev, A.1
  • 45
    • 79960029952 scopus 로고    scopus 로고
    • AquaSAXS: A web server for computation and fitting of SAXS profiles with non-uniformaly hydrated atomic models
    • Poitevin F et al 2011 AquaSAXS: a web server for computation and fitting of SAXS profiles with non-uniformaly hydrated atomic models Nucl. Acids Res. 39 W184-9
    • (2011) Nucl. Acids Res. , vol.39 , pp. 184-W189
    • Poitevin, F.1
  • 46
    • 84861503555 scopus 로고    scopus 로고
    • The small angle scattering ToolBox (SASTBX): An open-source software for biomolecular small-angle scattering
    • Liu H G, Hexemer A and Zwart P H 2012 The small angle scattering ToolBox (SASTBX): an open-source software for biomolecular small-angle scattering J. Appl. Crystallogr. 45 587-93
    • (2012) J. Appl. Crystallogr. , vol.45 , pp. 587-593
    • Liu, H.G.1    Hexemer, A.2    Zwart, P.H.3
  • 47
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo R P and Tainer J A 2011 Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law Biopolymers 95 559-71
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 48
    • 80054983091 scopus 로고    scopus 로고
    • Resting and active states of the ERK2:HePTP complex
    • Francis D M et al 2011 Resting and active states of the ERK2:HePTP complex J. Am. Chem. Soc. 133 17138-41
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17138-17141
    • Francis, D.M.1
  • 49
    • 51349101286 scopus 로고    scopus 로고
    • Replica exchange simulations of transient encounter complexes in protein-protein association
    • Kim Y C et al 2008 Replica exchange simulations of transient encounter complexes in protein-protein association Proc. Natl Acad. Sci. USA 105 12855-60
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12855-12860
    • Kim, Y.C.1
  • 50
    • 48749103296 scopus 로고    scopus 로고
    • Integrating diverse data for structure determination of macromolecular assemblies
    • Alber F et al 2008 Integrating diverse data for structure determination of macromolecular assemblies Annu. Rev. Biochem. 77 443-77
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 443-477
    • Alber, F.1
  • 51
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle x-ray scattering
    • Pelikan M, Hura G L and Hammel M 2009 Structure and flexibility within proteins as identified through small angle x-ray scattering Gen. Physiol. Biophys. 28 174-89
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 52
    • 84861083754 scopus 로고    scopus 로고
    • Solution structure of the ESCRT-I and -II supercomplex: Implications for membrane budding and scission
    • Boura E et al 2012 Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission Structure 20 874-86
    • (2012) Structure , vol.20 , pp. 874-886
    • Boura, E.1
  • 53
    • 85027955226 scopus 로고    scopus 로고
    • Protein structural dynamics revealed by site-directed spin labeling and multifrequency EPR
    • Nesmelov Y E and Thomas D D 2010 Protein structural dynamics revealed by site-directed spin labeling and multifrequency EPR Biophys. Rev. 2 91-9
    • (2010) Biophys. Rev. , vol.2 , pp. 91-99
    • Nesmelov, Y.E.1    Thomas, D.D.2
  • 54
    • 0028884014 scopus 로고
    • Fluorescence resonance energy-transfer spectroscopy is a reliable ruler for measuring structural-changes in proteins - Dispelling the problem of the unknown orientation factor
    • Dosremedios C G and Moens P D 1995 Fluorescence resonance energy-transfer spectroscopy is a reliable ruler for measuring structural-changes in proteins - dispelling the problem of the unknown orientation factor J. Struct. Biol. 115 175-85
    • (1995) J. Struct. Biol. , vol.115 , pp. 175-185
    • Dosremedios, C.G.1    Moens, P.D.2
  • 55
    • 84865294387 scopus 로고    scopus 로고
    • Mapping membrane protein structure with fluorescence
    • Taraska J W 2012 Mapping membrane protein structure with fluorescence Curr. Opin. Struct. Biol. 22 507-13
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 507-513
    • Taraska, J.W.1
  • 56
    • 79851509342 scopus 로고    scopus 로고
    • Three-dimensional molecular modeling with single molecule FRET
    • Brunger A T et al 2011 Three-dimensional molecular modeling with single molecule FRET J. Struct. Biol. 173 497-505
    • (2011) J. Struct. Biol. , vol.173 , pp. 497-505
    • Brunger, A.T.1
  • 57
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement
    • Jao C C et al 2008 Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement Proc. Natl Acad. Sci. USA 105 19666-71
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19666-19671
    • Jao, C.C.1
  • 58
    • 84877083091 scopus 로고    scopus 로고
    • Structural refinement from restrained-ensemble simulations based on EPR/DEER data: Application to T4 lysozyme
    • Islam S M et al 2013 Structural refinement from restrained-ensemble simulations based on EPR/DEER data: application to T4 lysozyme J. Phys. Chem. B 117 4740-54
    • (2013) J. Phys. Chem. , vol.117 , pp. 4740-4754
    • Islam, S.M.1
  • 59
    • 84870852782 scopus 로고    scopus 로고
    • A toolkit and benchmark study for FRET-restrained high-precision structural modeling
    • Kalinin S et al 2012 A toolkit and benchmark study for FRET-restrained high-precision structural modeling Natural Methods 9 1218-25
    • (2012) Natural Methods , vol.9 , pp. 1218-1225
    • Kalinin, S.1
  • 60
    • 84857510185 scopus 로고    scopus 로고
    • Single-molecule fluorescence experiments determine protein folding transition path times
    • Chung H S et al 2012 Single-molecule fluorescence experiments determine protein folding transition path times Science 335 981-4
    • (2012) Science , vol.335 , pp. 981-984
    • Chung, H.S.1
  • 61
    • 84886954019 scopus 로고    scopus 로고
    • Single-molecule fluorescence probes dynamics of barrier crossing
    • Chung H S and Eaton W A 2013 Single-molecule fluorescence probes dynamics of barrier crossing Nature 502 685-8
    • (2013) Nature , vol.502 , pp. 685-688
    • Chung, H.S.1    Eaton, W.A.2
  • 62
    • 77952583179 scopus 로고    scopus 로고
    • 14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)
    • Rezabkova L et al 2010 14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3) J. Struct. Biol. 170 451-61
    • (2010) J. Struct. Biol. , vol.170 , pp. 451-461
    • Rezabkova, L.1
  • 63
    • 84867084476 scopus 로고    scopus 로고
    • Improving FRET dynamic range with bright green and red fluorescent proteins
    • Lam A J et al 2012 Improving FRET dynamic range with bright green and red fluorescent proteins Natural Methods 9 1005-12
    • (2012) Natural Methods , vol.9 , pp. 1005-1012
    • Lam, A.J.1
  • 64
    • 34247267098 scopus 로고    scopus 로고
    • Both the N-terminal loop and wing W2 of the forkhead domain of transcription factor Foxo4 are important for DNA binding
    • Boura E et al 2007 Both the N-terminal loop and wing W2 of the forkhead domain of transcription factor Foxo4 are important for DNA binding J. Biol. Chem. 282 8265-75
    • (2007) J. Biol. Chem. , vol.282 , pp. 8265-8275
    • Boura, E.1
  • 65
    • 84883388081 scopus 로고    scopus 로고
    • Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin
    • Caron N S et al 2013 Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin Proc. Natl Acad. Sci. USA 110 14610-5
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 14610-14615
    • Caron, N.S.1
  • 66
    • 84888124729 scopus 로고    scopus 로고
    • Site-directed spin labeling EPR spectroscopy in protein research
    • Klare J P 2013 Site-directed spin labeling EPR spectroscopy in protein research Biol. Chem. 394 1281-300
    • (2013) Biol. Chem. , vol.394 , Issue.10 , pp. 1281-1300
    • Klare, J.P.1
  • 67
    • 77953415522 scopus 로고    scopus 로고
    • Detection of structural dynamics by FRET: A photon distribution and fluorescence lifetime analysis of systems with multiple states
    • Kalinin S et al 2010 Detection of structural dynamics by FRET: a photon distribution and fluorescence lifetime analysis of systems with multiple states J. Phys. Chem. B 114 7983-95
    • (2010) J. Phys. Chem. , vol.114 , pp. 7983-7995
    • Kalinin, S.1
  • 68
    • 84859899534 scopus 로고    scopus 로고
    • Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging
    • Ha T and Tinnefeld P 2012 Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging Annu. Rev. Phys. Chem. 63 595-617
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 595-617
    • Ha, T.1    Tinnefeld, P.2
  • 69
    • 84894235917 scopus 로고    scopus 로고
    • Protein-guided RNA dynamics during early ribosome assembly
    • Kim H et al 2014 Protein-guided RNA dynamics during early ribosome assembly Nature 506 334-8
    • (2014) Nature , vol.506 , pp. 334-338
    • Kim, H.1
  • 70
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney S A, Joo C and Ha T 2006 Analysis of single-molecule FRET trajectories using hidden Markov modeling Biophys. J. 91 1941-51
    • (2006) Biophys. J. , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 71
    • 37649015345 scopus 로고    scopus 로고
    • Effect of flexibility and cis residues in single-molecule FRET studies of polyproline
    • Best R B et al 2007 Effect of flexibility and cis residues in single-molecule FRET studies of polyproline Proc. Natl Acad. Sci. USA 104 18964-9
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18964-18969
    • Best, R.B.1
  • 72
    • 33846839535 scopus 로고    scopus 로고
    • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
    • Merchant K A et al 2007 Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations Proc. Natl Acad. Sci. USA 104 1528-33
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1528-1533
    • Merchant, K.A.1
  • 73
    • 2942627682 scopus 로고    scopus 로고
    • Sensitivity enhancement in pulse EPR distance measurements
    • Jeschke G et al 2004 Sensitivity enhancement in pulse EPR distance measurements J. Magn. Reson. 169 1-12
    • (2004) J. Magn. Reson. , vol.169 , pp. 1-12
    • Jeschke, G.1
  • 74
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Polyhach Y, Bordignon E and Jeschke G 2011 Rotamer libraries of spin labelled cysteines for protein studies Phys. Chem. Chem. Phys. 13 2356-66
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 75
    • 84891889778 scopus 로고    scopus 로고
    • Using cryoEM reconstruction and phase extension to determine crystal structure of bacteriophage varphi6 major capsid protein
    • Nemecek D, Plevka P and Boura E 2013 Using cryoEM reconstruction and phase extension to determine crystal structure of bacteriophage varphi6 major capsid protein Protein J. 32 635-40
    • (2013) Protein J. , vol.32 , pp. 635-640
    • Nemecek, D.1    Plevka, P.2    Boura, E.3
  • 76
    • 84881463246 scopus 로고    scopus 로고
    • Subunit folds and maturation pathway of a dsRNA virus capsid
    • Nemecek D et al 2013 Subunit folds and maturation pathway of a dsRNA virus capsid Structure 21 1374-83
    • (2013) Structure , vol.21 , pp. 1374-1383
    • Nemecek, D.1
  • 77
    • 33644676351 scopus 로고    scopus 로고
    • Structural basis of cellulosome efficiency explored by small angle x-ray scattering
    • Hammel M et al 2005 Structural basis of cellulosome efficiency explored by small angle x-ray scattering J. Biol. Chem. 280 38562-8
    • (2005) J. Biol. Chem. , vol.280 , pp. 38562-38568
    • Hammel, M.1
  • 78
    • 81355122666 scopus 로고    scopus 로고
    • Structural basis of p38alpha regulation by hematopoietic tyrosine phosphatase
    • Francis D M et al 2011 Structural basis of p38alpha regulation by hematopoietic tyrosine phosphatase Nature Chem. Biol. 7 916-24
    • (2011) Nature Chem. Biol. , vol.7 , pp. 916-924
    • Francis, D.M.1
  • 79
    • 37549009571 scopus 로고    scopus 로고
    • Coarse-grained models for simulations of multiprotein complexes: Application to ubiquitin binding
    • Kim Y C and Hummer G 2008 Coarse-grained models for simulations of multiprotein complexes: application to ubiquitin binding J. Mol. Biol. 375 1416-33
    • (2008) J. Mol. Biol. , vol.375 , pp. 1416-1433
    • Kim, Y.C.1    Hummer, G.2
  • 80
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor W et al 2006 HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes Acta Crystallogr. D 62 859-66
    • (2006) Acta Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1
  • 82
    • 84898741942 scopus 로고    scopus 로고
    • Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel
    • Wang Y et al 2014 Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel eLife 3 e01834
    • (2014) ELife , vol.3
    • Wang, Y.1
  • 83
    • 84881046157 scopus 로고    scopus 로고
    • Examining protein-lipid complexes using neutron scattering
    • Clifton L A, Neylon C and Lakey J H 2013 Examining protein-lipid complexes using neutron scattering Methods Mol. Biol. 974 119-50
    • (2013) Methods Mol. Biol. , vol.974 , pp. 119-150
    • Clifton, L.A.1    Neylon, C.2    Lakey, J.H.3
  • 84
    • 84908086364 scopus 로고    scopus 로고
    • The crystal structure of the phosphatidylinositol 4-kinase II-alpha
    • Baumlova A et al 2014 The crystal structure of the phosphatidylinositol 4-kinase II-alpha EMBO Reports 15 1085-92
    • (2014) EMBO Reports , vol.15 , pp. 1085-1092
    • Baumlova, A.1


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