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Volumn 107, Issue 8, 2014, Pages 1950-1961

Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE LIPID; MICELLE; OUTER MEMBRANE PROTEIN; PROTEIN BINDING;

EID: 84908240911     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.09.005     Document Type: Article
Times cited : (9)

References (79)
  • 1
    • 33847795359 scopus 로고    scopus 로고
    • Intrinsic disorder and functional proteomics
    • P. Radivojac, and L.M. Iakoucheva A.K. Dunker Intrinsic disorder and functional proteomics Biophys. J. 92 2007 1439 1456
    • (2007) Biophys. J. , vol.92 , pp. 1439-1456
    • Radivojac, P.1    Iakoucheva, L.M.2    Dunker, A.K.3
  • 2
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 3
    • 0030756675 scopus 로고    scopus 로고
    • Induced α helix in the VP16 activation domain upon binding to a human TAF
    • M. Uesugi, and O. Nyanguile G.L. Verdine Induced α helix in the VP16 activation domain upon binding to a human TAF Science 277 1997 1310 1313
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Verdine, G.L.3
  • 4
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions
    • I. Radhakrishnan, and G.C. Pérez-Alvarado P.E. Wright Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions Cell 91 1997 741 752
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Pérez-Alvarado, G.C.2    Wright, P.E.3
  • 5
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 6
    • 39749120473 scopus 로고    scopus 로고
    • How is protein aggregation in amyloidogenic diseases modulated by biological membranes?
    • C. Aisenbrey, and T. Borowik G. Gröbner How is protein aggregation in amyloidogenic diseases modulated by biological membranes? Eur. Biophys. J. 37 2008 247 255
    • (2008) Eur. Biophys. J. , vol.37 , pp. 247-255
    • Aisenbrey, C.1    Borowik, T.2    Gröbner, G.3
  • 7
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • D. Eliezer, and E. Kutluay G. Browne Conformational properties of α-synuclein in its free and lipid-associated states J. Mol. Biol. 307 2001 1061 1073
    • (2001) J. Mol. Biol. , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Browne, G.3
  • 8
    • 77957775523 scopus 로고    scopus 로고
    • Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins
    • J. Varkey, and J.M. Isas R. Langen Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins J. Biol. Chem. 285 2010 32486 32493
    • (2010) J. Biol. Chem. , vol.285 , pp. 32486-32493
    • Varkey, J.1    Isas, J.M.2    Langen, R.3
  • 9
    • 56249131479 scopus 로고    scopus 로고
    • Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli
    • P. Neumann, and A. Weidner K. Tittmann Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli Proc. Natl. Acad. Sci. USA 105 2008 17390 17395
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17390-17395
    • Neumann, P.1    Weidner, A.2    Tittmann, K.3
  • 10
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. USA 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 11
    • 45849131354 scopus 로고    scopus 로고
    • Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
    • O.F. Lange, and N.A. Lakomek B.L. de Groot Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution Science 320 2008 1471 1475
    • (2008) Science , vol.320 , pp. 1471-1475
    • Lange, O.F.1    Lakomek, N.A.2    De Groot, B.L.3
  • 12
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • J. Monod, J. Wyman, and J.P. Changeux On the nature of allosteric transitions: a plausible model J. Mol. Biol. 12 1965 88 118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 13
    • 84896336036 scopus 로고    scopus 로고
    • The binding mechanisms of intrinsically disordered proteins
    • J. Dogan, S. Gianni, and P. Jemth The binding mechanisms of intrinsically disordered proteins Phys. Chem. Chem. Phys. 16 2014 6323 6331
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 6323-6331
    • Dogan, J.1    Gianni, S.2    Jemth, P.3
  • 14
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • J.E. Galán, and H. Wolf-Watz Protein delivery into eukaryotic cells by type III secretion machines Nature 444 2006 567 573
    • (2006) Nature , vol.444 , pp. 567-573
    • Galán, J.E.1    Wolf-Watz, H.2
  • 15
    • 21344453525 scopus 로고    scopus 로고
    • The bacterial injection kit: Type III secretion systems
    • L.J. Mota, and G.R. Cornelis The bacterial injection kit: type III secretion systems Ann. Med. 37 2005 234 249
    • (2005) Ann. Med. , vol.37 , pp. 234-249
    • Mota, L.J.1    Cornelis, G.R.2
  • 16
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • G.R. Cornelis, and H. Wolf-Watz The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells Mol. Microbiol. 23 1997 861 867
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 18
    • 0033900964 scopus 로고    scopus 로고
    • Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching
    • T. Minamino, and R.M. Macnab Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching J. Bacteriol. 182 2000 4906 4914
    • (2000) J. Bacteriol. , vol.182 , pp. 4906-4914
    • Minamino, T.1    Macnab, R.M.2
  • 19
    • 0029989240 scopus 로고    scopus 로고
    • Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium
    • A.W. Williams, and S. Yamaguchi R.M. Macnab Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium J. Bacteriol. 178 1996 2960 2970
    • (1996) J. Bacteriol. , vol.178 , pp. 2960-2970
    • Williams, A.W.1    Yamaguchi, S.2    Macnab, R.M.3
  • 20
    • 0037379368 scopus 로고    scopus 로고
    • YscP and YscU regulate substrate specificity of the Yersinia type III secretion system
    • P.J. Edqvist, and J. Olsson S.A. Lloyd YscP and YscU regulate substrate specificity of the Yersinia type III secretion system J. Bacteriol. 185 2003 2259 2266
    • (2003) J. Bacteriol. , vol.185 , pp. 2259-2266
    • Edqvist, P.J.1    Olsson, J.2    Lloyd, S.A.3
  • 21
    • 67649400614 scopus 로고    scopus 로고
    • Autoproteolysis of YscU of Yersinia pseudotuberculosis is important for regulation of expression and secretion of Yop proteins
    • A.C. Björnfot, and M. Lavander H. Wolf-Watz Autoproteolysis of YscU of Yersinia pseudotuberculosis is important for regulation of expression and secretion of Yop proteins J. Bacteriol. 191 2009 4259 4267
    • (2009) J. Bacteriol. , vol.191 , pp. 4259-4267
    • Björnfot, A.C.1    Lavander, M.2    Wolf-Watz, H.3
  • 22
    • 43049127811 scopus 로고    scopus 로고
    • Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS
    • R. Zarivach, and W. Deng N.C. Strynadka Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS Nature 453 2008 124 127
    • (2008) Nature , vol.453 , pp. 124-127
    • Zarivach, R.1    Deng, W.2    Strynadka, N.C.3
  • 23
    • 59949084690 scopus 로고    scopus 로고
    • Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion
    • G.T. Lountos, and B.P. Austin D.S. Waugh Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion Protein Sci. 18 2009 467 474
    • (2009) Protein Sci. , vol.18 , pp. 467-474
    • Lountos, G.T.1    Austin, B.P.2    Waugh, D.S.3
  • 24
    • 84869809433 scopus 로고    scopus 로고
    • Autoproteolysis and intramolecular dissociation of Yersinia YscU precedes secretion of its C-terminal polypeptide YscU(CC)
    • S. Frost, and O. Ho M. Wolf-Watz Autoproteolysis and intramolecular dissociation of Yersinia YscU precedes secretion of its C-terminal polypeptide YscU(CC) PLoS ONE 7 2012 e49349
    • (2012) PLoS ONE , vol.7 , pp. 49349
    • Frost, S.1    Ho, O.2    Wolf-Watz, M.3
  • 25
    • 58149112120 scopus 로고    scopus 로고
    • Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica
    • U. Wiesand, and I. Sorg D.W. Heinz Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica J. Mol. Biol. 385 2009 854 866
    • (2009) J. Mol. Biol. , vol.385 , pp. 854-866
    • Wiesand, U.1    Sorg, I.2    Heinz, D.W.3
  • 26
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. 545-W549
    • Holm, L.1    Rosenström, P.2
  • 27
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • N.J. Greenfield Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 1 2006 2876 2890
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 29
    • 0034515845 scopus 로고    scopus 로고
    • Ansig for Windows: An interactive computer program for semiautomatic assignment of protein NMR spectra
    • M. Helgstrand, and P. Kraulis T. Härd Ansig for Windows: an interactive computer program for semiautomatic assignment of protein NMR spectra J. Biomol. NMR 18 2000 329 336
    • (2000) J. Biomol. NMR , vol.18 , pp. 329-336
    • Helgstrand, M.1    Kraulis, P.2    Härd, T.3
  • 30
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • W.F. Vranken, and W. Boucher E.D. Laue The CCPN data model for NMR spectroscopy: development of a software pipeline Proteins 59 2005 687 696
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Laue, E.D.3
  • 31
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • A.G. Palmer, and J. Cavanagh M. Rance Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy J. Magn. Reson. 93 1991 151 170
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer, A.G.1    Cavanagh, J.2    Rance, M.3
  • 32
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • L.E. Kay, P. Keifer, and T. Saarinen Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 114 1992 10663 10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 34
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • S. Grzesiek, and A. Bax Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein J. Magn. Reson. 96 1992 432 440
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 35
    • 84863112496 scopus 로고    scopus 로고
    • Identification of helix capping and b-turn motifs from NMR chemical shifts
    • Y. Shen, and A. Bax Identification of helix capping and b-turn motifs from NMR chemical shifts J. Biomol. NMR 52 2012 211 232
    • (2012) J. Biomol. NMR , vol.52 , pp. 211-232
    • Shen, Y.1    Bax, A.2
  • 36
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 37
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts J. Am. Chem. Soc. 113 1991 5490 5492
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 38
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects J. Biomol. NMR 5 1995 67 81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Sykes, B.D.3
  • 39
    • 34547563370 scopus 로고    scopus 로고
    • The RCI server: Rapid and accurate calculation of protein flexibility using chemical shifts
    • M.V. Berjanskii, and D.S. Wishart The RCI server: rapid and accurate calculation of protein flexibility using chemical shifts Nucleic Acids Res. 35 2007 W531 W537
    • (2007) Nucleic Acids Res. , vol.35 , pp. 531-W537
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 40
    • 0032352438 scopus 로고    scopus 로고
    • Pulsed-field gradient nuclear magnetic resonance as a tool for studying translational diffusion: Part II. Experimental aspects
    • W.S. Price Pulsed-field gradient nuclear magnetic resonance as a tool for studying translational diffusion: Part II. Experimental aspects Concepts Magn. Reson. 10 1998 197 237
    • (1998) Concepts Magn. Reson. , vol.10 , pp. 197-237
    • Price, W.S.1
  • 41
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time-dependent field gradient
    • E.O. Stejskal, and J.E. Tanner Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient J. Chem. Phys. 42 1965 288 292
    • (1965) J. Chem. Phys. , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.E.2
  • 42
    • 0031498272 scopus 로고    scopus 로고
    • Pulsed-field gradient nuclear magnetic resonance as a tool for studying translational diffusion. 1. Basic theory
    • W.S. Price Pulsed-field gradient nuclear magnetic resonance as a tool for studying translational diffusion. 1. Basic theory Concepts Magn. Reson. 9 1997 299 336
    • (1997) Concepts Magn. Reson. , vol.9 , pp. 299-336
    • Price, W.S.1
  • 43
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • J.L. Battiste, and G. Wagner Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data Biochemistry 39 2000 5355 5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 45
    • 79960654163 scopus 로고    scopus 로고
    • Structural characterization of AS1-membrane interactions from a subset of HAMP domains
    • S. Unnerståle, L. Mäler, and R.R. Draheim Structural characterization of AS1-membrane interactions from a subset of HAMP domains Biochim. Biophys. Acta 1808 2011 2403 2412
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2403-2412
    • Unnerståle, S.1    Mäler, L.2    Draheim, R.R.3
  • 46
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • S.H. White, and W.C. Wimley Hydrophobic interactions of peptides with membrane interfaces Biochim. Biophys. Acta 1376 1998 339 352
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 47
    • 1842650004 scopus 로고
    • Growth of sodium dodecyl sulfate micelles with detergent concentration
    • F.H. Quina, and P.M. Nassar B.L. Bales Growth of sodium dodecyl sulfate micelles with detergent concentration J. Phys. Chem. 99 1995 17028 17031
    • (1995) J. Phys. Chem. , vol.99 , pp. 17028-17031
    • Quina, F.H.1    Nassar, P.M.2    Bales, B.L.3
  • 49
    • 77954287478 scopus 로고    scopus 로고
    • Protein annotation and modelling servers at University College London
    • D.W. Buchan, and S.M. Ward D.T. Jones Protein annotation and modelling servers at University College London Nucleic Acids Res. 38 2010 W563 W568
    • (2010) Nucleic Acids Res. , vol.38 , pp. 563-W568
    • Buchan, D.W.1    Ward, S.M.2    Jones, D.T.3
  • 50
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 52
    • 0034723132 scopus 로고    scopus 로고
    • Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters
    • J.L. Goodman, M.D. Pagel, and M.J. Stone Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters J. Mol. Biol. 295 2000 963 978
    • (2000) J. Mol. Biol. , vol.295 , pp. 963-978
    • Goodman, J.L.1    Pagel, M.D.2    Stone, M.J.3
  • 53
    • 34547920308 scopus 로고    scopus 로고
    • Positioning of the Alzheimer Aβ(1-40) peptide in SDS micelles using NMR and paramagnetic probes
    • J. Jarvet, and J. Danielsson A. Gräslund Positioning of the Alzheimer Aβ(1-40) peptide in SDS micelles using NMR and paramagnetic probes J. Biomol. NMR 39 2007 63 72
    • (2007) J. Biomol. NMR , vol.39 , pp. 63-72
    • Jarvet, J.1    Danielsson, J.2    Gräslund, A.3
  • 54
    • 79251588504 scopus 로고    scopus 로고
    • Electrostatic contributions to the stabilities of native proteins and amyloid complexes
    • S.R. Sheftic, and R.L. Croke A.T. Atexandrescu Electrostatic contributions to the stabilities of native proteins and amyloid complexes Methods Enzymol 466 2009 233 258
    • (2009) Methods Enzymol , vol.466 , pp. 233-258
    • Sheftic, S.R.1    Croke, R.L.2    Atexandrescu, A.T.3
  • 55
    • 0031989849 scopus 로고    scopus 로고
    • Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme
    • T.L. Hwang, P.C. van Zijl, and S. Mori Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme J. Biomol. NMR 11 1998 221 226
    • (1998) J. Biomol. NMR , vol.11 , pp. 221-226
    • Hwang, T.L.1    Van Zijl, P.C.2    Mori, S.3
  • 56
    • 51049124329 scopus 로고    scopus 로고
    • The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE
    • L. Rodgers, and A. Gamez P. Ghosh The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE J. Biol. Chem. 283 2008 20857 20863
    • (2008) J. Biol. Chem. , vol.283 , pp. 20857-20863
    • Rodgers, L.1    Gamez, A.2    Ghosh, P.3
  • 57
    • 0038016732 scopus 로고    scopus 로고
    • Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB
    • G.M. Fraser, and T. Hirano R.M. Macnab Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB Mol. Microbiol. 48 2003 1043 1057
    • (2003) Mol. Microbiol. , vol.48 , pp. 1043-1057
    • Fraser, G.M.1    Hirano, T.2    Macnab, R.M.3
  • 59
    • 0013293280 scopus 로고    scopus 로고
    • The Xplor-NIH NMR molecular structure determination package
    • C.D. Schwieters, and J.J. Kuszewski G.M. Clore The Xplor-NIH NMR molecular structure determination package J. Magn. Reson. 160 2003 65 73
    • (2003) J. Magn. Reson. , vol.160 , pp. 65-73
    • Schwieters, C.D.1    Kuszewski, J.J.2    Clore, G.M.3
  • 60
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, and F. Delaglio A. Bax TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Bax, A.3
  • 61
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, and M.W. Macarthur J.M. Thornton Procheck: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26 1993 283 291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Thornton, J.M.3
  • 62
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 63
  • 64
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease Biochemistry 28 1989 8972 8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 65
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • S. Mori, and C. Abeygunawardana P.C. van Zijl Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation J. Magn. Reson. B. 108 1995 94 98
    • (1995) J. Magn. Reson. B. , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Van Zijl, P.C.3
  • 66
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Y. Bai, and J.S. Milne S.W. Englander Primary structure effects on peptide group hydrogen exchange Proteins 17 1993 75 86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Englander, S.W.3
  • 67
    • 0027169975 scopus 로고
    • Isotope effects in peptide group hydrogen exchange
    • G.P. Connelly, and Y. Bai S.W. Englander Isotope effects in peptide group hydrogen exchange Proteins 17 1993 87 92
    • (1993) Proteins , vol.17 , pp. 87-92
    • Connelly, G.P.1    Bai, Y.2    Englander, S.W.3
  • 68
    • 0032584781 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids
    • J.L. Markley, and A. Bax K. Wüthrich Recommendations for the presentation of NMR structures of proteins and nucleic acids J. Mol. Biol. 280 1998 933 952
    • (1998) J. Mol. Biol. , vol.280 , pp. 933-952
    • Markley, J.L.1    Bax, A.2    Wüthrich, K.3
  • 69
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • A.M. Mandel, M. Akke, and A.G. Palmer 3rd Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme J. Mol. Biol. 246 1995 144 163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 71
    • 0141502348 scopus 로고    scopus 로고
    • Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G
    • J.B. Hall, and D. Fushman Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G J. Biomol. NMR 27 2003 261 275
    • (2003) J. Biomol. NMR , vol.27 , pp. 261-275
    • Hall, J.B.1    Fushman, D.2
  • 72
    • 0002437070 scopus 로고
    • Nuclear magnetic relaxation induced by chemical exchange
    • H. Wennerst Nuclear magnetic relaxation induced by chemical exchange Mol. Phys. 24 1972 69 80
    • (1972) Mol. Phys. , vol.24 , pp. 69-80
    • Wennerst, H.1
  • 73
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity J. Am. Chem. Soc. 104 1982 4546 4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 74
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results J. Am. Chem. Soc. 104 1982 4559 4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 75
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • G.M. Clore, and A. Szabo A.M. Gronenborn Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins J. Am. Chem. Soc. 112 1990 4989 4991
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Gronenborn, A.M.3
  • 76
    • 0344236151 scopus 로고    scopus 로고
    • Hydrodynamic properties of rodlike and disklike particles in dilute solution
    • A. Ortega, and J.G. de la Torre Hydrodynamic properties of rodlike and disklike particles in dilute solution J. Chem. Phys. 119 2003 9914 9919
    • (2003) J. Chem. Phys. , vol.119 , pp. 9914-9919
    • Ortega, A.1    De La Torre, J.G.2
  • 77
    • 0033615301 scopus 로고    scopus 로고
    • a measurements of the β-peptide and mechanism of pH-induced amyloid formation
    • a measurements of the β-peptide and mechanism of pH-induced amyloid formation J. Am. Chem. Soc. 121 1999 8698 8706
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8698-8706
    • Ma, K.1    Clancy, E.L.2    Zagorski, M.G.3
  • 78
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F.W. Studier, and B.A. Moffatt Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J. Mol. Biol. 189 1986 113 130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 79
    • 0036334915 scopus 로고    scopus 로고
    • Proteolytic cleavage of the FlhB homologue YscU of Yersinia pseudotuberculosis is essential for bacterial survival but not for type III secretion
    • M. Lavander, and L. Sundberg A. Forsberg Proteolytic cleavage of the FlhB homologue YscU of Yersinia pseudotuberculosis is essential for bacterial survival but not for type III secretion J. Bacteriol. 184 2002 4500 4509
    • (2002) J. Bacteriol. , vol.184 , pp. 4500-4509
    • Lavander, M.1    Sundberg, L.2    Forsberg, A.3


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