메뉴 건너뛰기




Volumn 66, Issue 5, 2007, Pages 1123-1135

Solution structure of the novel dispersin protein of enteroaggregative Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DISPERSIN; LIPOPOLYSACCHARIDE; UNCLASSIFIED DRUG;

EID: 36148966931     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05985.x     Document Type: Article
Times cited : (38)

References (82)
  • 1
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. Davis, D.G. (1985) MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J Mag Reson 65 : 355 360.
    • (1985) J Mag Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0001594959 scopus 로고
    • Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients
    • Bax, A. Pochapsky, S.S. (1992) Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients. J Magn Reson 99 : 638 643.
    • (1992) J Magn Reson , vol.99 , pp. 638-643
    • Bax, A.1    Pochapsky, S.S.2
  • 3
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • Bax, A., Kontaxis, G. Tjandra, N. (2001) Dipolar couplings in macromolecular structure determination. Methods Enzymol 339 : 127 174.
    • (2001) Methods Enzymol , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 5
    • 0038609651 scopus 로고    scopus 로고
    • Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex
    • Boulanger, M.J., Chow, D.C., Brevnova, E.E. Garcia, K.C. (2003) Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex. Science 300 : 2101 2104.
    • (2003) Science , vol.300 , pp. 2101-2104
    • Boulanger, M.J.1    Chow, D.C.2    Brevnova, E.E.3    Garcia, K.C.4
  • 7
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • Chou, J.J., Gaemers, S., Howder, B., Louis, J.M. Bax, A. (2001) A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J Biomol NMR 21 : 377 382.
    • (2001) J Biomol NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 8
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • Chou, J.J., Kaufman, J.D., Stahl, S.J., Wingfield, P.T. Bax, A. (2002) Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J Am Chem Soc 124 : 2450 2451.
    • (2002) J Am Chem Soc , vol.124 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 9
    • 0000939457 scopus 로고
    • The three-dimensional structure of alpha1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore, G.M., Nilges, M., Sukumaran, D.K., Brunger, A.T., Karplus, M. Gronenborn, A.M. (1986) The three-dimensional structure of alpha1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J 5 : 2729 2735.
    • (1986) EMBO J , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Sukumaran, D.K.3    Brunger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 10
    • 0023475020 scopus 로고
    • Three-dimensional structure of potato carboxypeptidase inhibitor in solution. a study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G.M., Gronenborn, A.M., Nilges, M. Ryan, C.A. (1987) Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 26 : 8012 8023.
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 11
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13 : 289 302.
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 12
    • 0030793821 scopus 로고    scopus 로고
    • Aggregative adherence fimbria II, a second fimbrial antigen mediating aggregative adherence in enteroaggregative Escherichia coli
    • Czeczulin, J.R., Balepur, S., Hicks, S., Phillips, A., Hall, R., Kothary, M.H., et al. (1997) Aggregative adherence fimbria II, a second fimbrial antigen mediating aggregative adherence in enteroaggregative Escherichia coli. Infect Immun 65 : 4135 4145.
    • (1997) Infect Immun , vol.65 , pp. 4135-4145
    • Czeczulin, J.R.1    Balepur, S.2    Hicks, S.3    Phillips, A.4    Hall, R.5    Kothary, M.H.6
  • 14
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6 : 277 293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 16
    • 0032939805 scopus 로고    scopus 로고
    • The use of dipolar couplings for determining the solution structure of rat apo-S100B (betabeta)
    • Drohat, A.C., Tjandra, N., Baldisseri, D.M. Weber, D.J. (1999) The use of dipolar couplings for determining the solution structure of rat apo-S100B (betabeta). Protein Sci 8 : 800 809.
    • (1999) Protein Sci , vol.8 , pp. 800-809
    • Drohat, A.C.1    Tjandra, N.2    Baldisseri, D.M.3    Weber, D.J.4
  • 17
    • 0028672866 scopus 로고
    • Practical introduction to theory and implementation of multinuclear, multidimensional nuclear magnetic resonance experiments
    • Edison, A.S., Abildgaard, F., Westler, W.M., Mooberry, E.S. Markley, J.L. (1994) Practical introduction to theory and implementation of multinuclear, multidimensional nuclear magnetic resonance experiments. Methods Enzymol 239 : 3 79.
    • (1994) Methods Enzymol , vol.239 , pp. 3-79
    • Edison, A.S.1    Abildgaard, F.2    Westler, W.M.3    Mooberry, E.S.4    Markley, J.L.5
  • 18
    • 0021864803 scopus 로고
    • Metabolism of mixed human colonic bacteria in a continuous culture mimicking the human cecal contents
    • Edwards, C.A., Duerden, B.I. Read, N.W. (1985) Metabolism of mixed human colonic bacteria in a continuous culture mimicking the human cecal contents. Astroenterology 88 : 1903 1909.
    • (1985) Astroenterology , vol.88 , pp. 1903-1909
    • Edwards, C.A.1    Duerden, B.I.2    Read, N.W.3
  • 19
    • 0345313627 scopus 로고    scopus 로고
    • Organization of biogenesis genes for aggregative adherence fimbria II defines a virulence gene cluster in enteroaggregative Escherichia coli
    • Elias, W.P., Czeczulin, J.R., Henderson, I.R., Trabulsi, L.R. Nataro, J.P. (1999) Organization of biogenesis genes for aggregative adherence fimbria II defines a virulence gene cluster in enteroaggregative Escherichia coli. J Bacteriol 181 : 1779 1785.
    • (1999) J Bacteriol , vol.181 , pp. 1779-1785
    • Elias, W.P.1    Czeczulin, J.R.2    Henderson, I.R.3    Trabulsi, L.R.4    Nataro, J.P.5
  • 21
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR pectroscopy. a strategy for the simplification of homonuclear two-dimensional NMR spectra
    • Fesik, S.W. Zuiderweg, E.R. (1988) Heteronuclear three-dimensional NMR pectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra. J Magn Reson 78 : 588 593.
    • (1988) J Magn Reson , vol.78 , pp. 588-593
    • Fesik, S.W.1    Zuiderweg, E.R.2
  • 23
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D.S., Powers, R., Gronenborn, A.M. Clore, G.M. (1991) A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. J Magn Reson 95 : 214 220.
    • (1991) J Magn Reson , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 24
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization
    • Grzesiek, S., Anglister, J. Bax, A. (1993) Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J Mag Reson B 101 : 114 119.
    • (1993) J Mag Reson B , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 25
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. Bax, A. (1992a) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114 : 6291 6293.
    • (1992) J Am Chem Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 26
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek, S. Bax, A. (1992b) An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J Mag Reson 99 : 201 207.
    • (1992) J Mag Reson , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 28
    • 0001269119 scopus 로고
    • Detection of nuclear overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy
    • Ikura, M., Bax, A., Clore, G.M. Gronenborn, A.M. (1990) Detection of nuclear overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J Am Chem Soc 112 : 9020 9022.
    • (1990) J Am Chem Soc , vol.112 , pp. 9020-9022
    • Ikura, M.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4
  • 29
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensioinal NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. Ernst, R.R. (1979) Investigation of exchange processes by two-dimensioinal NMR spectroscopy. J Chem Phys 71 : 4546 4553.
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 30
    • 0029787464 scopus 로고    scopus 로고
    • Adhesion of the positively charged bacterium Stenotrophomonas (Xanthomonas) maltophilia 70401 to glass and Teflon
    • Jucker, B.A., Harms, H. Zehnder, A.J. (1996) Adhesion of the positively charged bacterium Stenotrophomonas (Xanthomonas) maltophilia 70401 to glass and Teflon. J Bacteriol 178 : 5472 5479.
    • (1996) J Bacteriol , vol.178 , pp. 5472-5479
    • Jucker, B.A.1    Harms, H.2    Zehnder, A.J.3
  • 31
    • 0003026536 scopus 로고
    • Practical aspects of 3D heteronuclear NMR of proteins
    • Kay, L.E., Marion, D. Bax, A. (1989) Practical aspects of 3D heteronuclear NMR of proteins. J Magn Reson 84 : 72 84.
    • (1989) J Magn Reson , vol.84 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 32
    • 34447505016 scopus 로고
    • Enhanced sensitivity triple-resonance spectroscopy with minimal H2O saturation
    • Kay, L.E., Xu, G.Y. Yamazaki, T. (1994) Enhanced sensitivity triple-resonance spectroscopy with minimal H2O saturation. J Magn Reson A 109 : 129 133.
    • (1994) J Magn Reson a , vol.109 , pp. 129-133
    • Kay, L.E.1    Xu, G.Y.2    Yamazaki, T.3
  • 33
    • 0000935584 scopus 로고    scopus 로고
    • Molecular and cellular biology of interleukin-6 and its receptor
    • Keller, E.T., Wanagat, J. Ershler, W.B. (1996) Molecular and cellular biology of interleukin-6 and its receptor. Front Biosci 1 : d340 357.
    • (1996) Front Biosci , vol.1
    • Keller, E.T.1    Wanagat, J.2    Ershler, W.B.3
  • 34
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B. Hughes, C. (2000) Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 : 914 919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 35
    • 0028545648 scopus 로고
    • Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • Kuboniwa, H., Grzesiek, S., Delaglio, F. Bax, A. (1994) Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J Biomol NMR 4 : 871 878.
    • (1994) J Biomol NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 36
    • 0026676167 scopus 로고
    • Sampling and efficiency of metric matrix distance geometry: A novel partial metrization algorithm
    • Kuszewski, J., Nilges, M. Brunger, A.T. (1992) Sampling and efficiency of metric matrix distance geometry: a novel partial metrization algorithm. J Biomol NMR 2 : 33 56.
    • (1992) J Biomol NMR , vol.2 , pp. 33-56
    • Kuszewski, J.1    Nilges, M.2    Brunger, A.T.3
  • 37
    • 0029314335 scopus 로고
    • The impact of direct refinement against proton chemical shifts on protein structure determination by NMR
    • Kuszewski, J., Gronenborn, A.M. Clore, G.M. (1995) The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. J Magn Reson B 107 : 293 297.
    • (1995) J Magn Reson B , vol.107 , pp. 293-297
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 38
    • 0031083293 scopus 로고    scopus 로고
    • Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
    • Kuszewski, J., Gronenborn, A.M. Clore, G.M. (1997) Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J Magn Reson 125 : 171 177.
    • (1997) J Magn Reson , vol.125 , pp. 171-177
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 39
    • 0000243829 scopus 로고
    • PROCHECK, a program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. Thornton, J.M. (1993) PROCHECK, a program to check the stereochemical quality of protein structures. J Appl Crystallog 319 : 823 837.
    • (1993) J Appl Crystallog , vol.319 , pp. 823-837
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0021754853 scopus 로고
    • Long range hydrogen bond mediated effects in peptides: 15N NMR study of Gramicidin S in water and organic solvents
    • Live, D.H., Davis, D.G., Agosta, W.C. Cowburn, D. (1984) Long range hydrogen bond mediated effects in peptides: 15N NMR study of Gramicidin S in water and organic solvents. J Am Chem Soc 106 : 1939 1941.
    • (1984) J Am Chem Soc , vol.106 , pp. 1939-1941
    • Live, D.H.1    Davis, D.G.2    Agosta, W.C.3    Cowburn, D.4
  • 41
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R. Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 85 : 393 399.
    • (1989) J Magn Reson , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 42
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D, photorealistic molecular graphics
    • Merritt, E.A. Bacon, D.J. (1997) Raster3D, photorealistic molecular graphics. Methods Enzymol 277 : 505 524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 43
    • 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
    • Mori, S., Abeygunawardana, C., Johnson, M.O. van Zijl, P.C. (1995) 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 : 94 98.
    • (1995) J Magn Reson B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Van Zijl, P.C.4
  • 44
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D.R. Kay, L.E. (1994) Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B 103 : 203 216.
    • (1994) J Magn Reson B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 45
    • 0000045562 scopus 로고
    • An enhanced-sensitivity pure absorption gradient 4D, 15N, 13C-edited NOESY experiment
    • Muhandiram, D.R., Xu, G.Y. Kay, L.E. (1993) An enhanced-sensitivity pure absorption gradient 4D, 15N, 13C-edited NOESY experiment. J Biomol NMR 3 : 463 470.
    • (1993) J Biomol NMR , vol.3 , pp. 463-470
    • Muhandiram, D.R.1    Xu, G.Y.2    Kay, L.E.3
  • 47
    • 0026729493 scopus 로고
    • Aggregative adherence fimbriae I of enteroaggregative Escherichia coli mediate adherence to HEp-2 cells and hemagglutination of human erythrocytes
    • Nataro, J.P., Deng, Y., Maneval, D.R., German, A.L., Martin, W.C. Levine, M.M. (1992) Aggregative adherence fimbriae I of enteroaggregative Escherichia coli mediate adherence to HEp-2 cells and hemagglutination of human erythrocytes. Infect Immun 60 : 2297 2304.
    • (1992) Infect Immun , vol.60 , pp. 2297-2304
    • Nataro, J.P.1    Deng, Y.2    Maneval, D.R.3    German, A.L.4    Martin, W.C.5    Levine, M.M.6
  • 48
    • 0027522630 scopus 로고
    • Aggregative adherence fimbria I expression in enteroaggregative Escherichia coli requires two unlinked plasmid regions
    • Nataro, J.P., Yikang, D., Giron, J.A., Savarino, S.J., Kothary, M.H. Hall, R. (1993) Aggregative adherence fimbria I expression in enteroaggregative Escherichia coli requires two unlinked plasmid regions. Infect Immun 61 : 1126 1131.
    • (1993) Infect Immun , vol.61 , pp. 1126-1131
    • Nataro, J.P.1    Yikang, D.2    Giron, J.A.3    Savarino, S.J.4    Kothary, M.H.5    Hall, R.6
  • 49
    • 0027933197 scopus 로고
    • AggR, a transcriptional activator of aggregative adherence fimbria I expression in enteroaggregative Escherichia coli
    • Nataro, J.P., Yikang, D., Yingkang, D. Walker, K. (1994) AggR, a transcriptional activator of aggregative adherence fimbria I expression in enteroaggregative Escherichia coli. J Bacteriol 176 : 4691 4699.
    • (1994) J Bacteriol , vol.176 , pp. 4691-4699
    • Nataro, J.P.1    Yikang, D.2    Yingkang, D.3    Walker, K.4
  • 50
    • 0028894779 scopus 로고
    • Heterogeneity of enteroaggregative Escherichia coli virulence demonstrated in volunteers
    • Nataro, J.P., Deng, Y., Cookson, S., Cravioto, A., Savarino, S.J., Guers, L.D., et al. (1995) Heterogeneity of enteroaggregative Escherichia coli virulence demonstrated in volunteers. J Infect Dis 171 : 465 468.
    • (1995) J Infect Dis , vol.171 , pp. 465-468
    • Nataro, J.P.1    Deng, Y.2    Cookson, S.3    Cravioto, A.4    Savarino, S.J.5    Guers, L.D.6
  • 51
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 : 281 296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 52
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges, M., Clore, G.M. Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett 229 : 317 324.
    • (1988) FEBS Lett , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 54
    • 0242664748 scopus 로고    scopus 로고
    • The export of coat protein from enteroaggregative Escherichia coli by a specific ATP-binding cassette transporter system
    • Nishi, J., Sheikh, J., Mizuguchi, K., Luisi, B., Burland, V., Boutin, A., et al. (2003) The export of coat protein from enteroaggregative Escherichia coli by a specific ATP-binding cassette transporter system. J Biol Chem 278 : 45680 45689.
    • (2003) J Biol Chem , vol.278 , pp. 45680-45689
    • Nishi, J.1    Sheikh, J.2    Mizuguchi, K.3    Luisi, B.4    Burland, V.5    Boutin, A.6
  • 55
    • 0030758958 scopus 로고    scopus 로고
    • An empirical correlation between amide deuterium isotope effects on 13C-alpha chemical shifts and protein backbone conformation
    • Ottiger, M. Bax, A. (1997) An empirical correlation between amide deuterium isotope effects on 13C-alpha chemical shifts and protein backbone conformation. J Am Chem Soc 119 : 8070 8075.
    • (1997) J Am Chem Soc , vol.119 , pp. 8070-8075
    • Ottiger, M.1    Bax, A.2
  • 56
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger, M., Delaglio, F. Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson 131 : 373 378.
    • (1998) J Magn Reson , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 57
    • 0031885909 scopus 로고    scopus 로고
    • Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice
    • Pei, Z., Burucoa, C., Grignon, B., Baqar, S., Huang, X.Z., Kopecko, D.J., et al. (1998) Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice. Infect Immun 66 : 938 943.
    • (1998) Infect Immun , vol.66 , pp. 938-943
    • Pei, Z.1    Burucoa, C.2    Grignon, B.3    Baqar, S.4    Huang, X.Z.5    Kopecko, D.J.6
  • 58
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2 : 661 665.
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 60
    • 0035742163 scopus 로고    scopus 로고
    • The VMD-XPLOR visualization package for NMR structure refinement
    • Schwieters, C.D. Clore, G.M. (2001) The VMD-XPLOR visualization package for NMR structure refinement. J Magn Reson 149 : 239 244.
    • (2001) J Magn Reson , vol.149 , pp. 239-244
    • Schwieters, C.D.1    Clore, G.M.2
  • 62
    • 0026223896 scopus 로고
    • A relational database for sequence-specific protein NMR data
    • Seavey, B.R., Farr, E.A., Westler, W.M. Markley, J.C. (1991) A relational database for sequence-specific protein NMR data. J Biomol NMR 1 : 217 236.
    • (1991) J Biomol NMR , vol.1 , pp. 217-236
    • Seavey, B.R.1    Farr, E.A.2    Westler, W.M.3    Markley, J.C.4
  • 64
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle, D. Ackerman, M.S. (2001) Persistence of native-like topology in a denatured protein in 8 M urea. Science 293 : 487 489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 65
    • 0035057564 scopus 로고    scopus 로고
    • Neutrophil-epithelial crosstalk at the intestinal lumenal surface mediated by reciprocal secretion of adenosine and IL-6
    • Sitaraman, S.V., Merlin, D., Wang, L., Wong, M., Gewirtz, A.T., Si-Tahar, M. Madara, J.L. (2001) Neutrophil-epithelial crosstalk at the intestinal lumenal surface mediated by reciprocal secretion of adenosine and IL-6. J Clin Invest 107 : 861 869.
    • (2001) J Clin Invest , vol.107 , pp. 861-869
    • Sitaraman, S.V.1    Merlin, D.2    Wang, L.3    Wong, M.4    Gewirtz, A.T.5    Si-Tahar, M.6    Madara, J.L.7
  • 66
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and C (alpha) and C (beta) 13C nuclear magnetic resonance chemical shifts
    • Spera, S. Bax, A. (1991) Empirical correlation between protein backbone conformation and C (alpha) and C (beta) 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113 : 5490 5492.
    • (1991) J Am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 67
    • 0031010519 scopus 로고    scopus 로고
    • Identification and characterization of a basic cell surface-located protein from Lactobacillus fermentum BR11
    • Turner, M.S., Timms, P., Hafner, L.M. Giffard, P.M. (1997) Identification and characterization of a basic cell surface-located protein from Lactobacillus fermentum BR11. J Bacteriol 179 : 3310 3316.
    • (1997) J Bacteriol , vol.179 , pp. 3310-3316
    • Turner, M.S.1    Timms, P.2    Hafner, L.M.3    Giffard, P.M.4
  • 68
    • 0034721465 scopus 로고    scopus 로고
    • Alignment of biopolymers in strained gels: A new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR
    • Tycko, R., Blanco, F.J. Ishii, Y. (2000) Alignment of biopolymers in strained gels: a new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR. J Am Chem Soc 122 : 9340 9341.
    • (2000) J Am Chem Soc , vol.122 , pp. 9340-9341
    • Tycko, R.1    Blanco, F.J.2    Ishii, Y.3
  • 70
  • 71
    • 12044259775 scopus 로고
    • Quantitative J correlation: A new approach for measuring homonuclear three-bond J (HNHa) coupling constants in 15N-enriched proteins
    • Vuister, G.W. Bax, A. (1993) Quantitative J correlation: a new approach for measuring homonuclear three-bond J (HNHa) coupling constants in 15N-enriched proteins. J Am Chem Soc 115 : 7772 7777.
    • (1993) J Am Chem Soc , vol.115 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 72
    • 0013498057 scopus 로고
    • Increased resolution and improved spectral quality in four-dimensional 13C/13C-separated HMQC-NOESY-HMQC spectra using pulsed field gradients
    • Vuister, G.W., Clore, G.M., Gronenborn, A.M., Powers, R., Garrett, D.S., Tschudin, R. Bax, A. (1993) Increased resolution and improved spectral quality in four-dimensional 13C/13C-separated HMQC-NOESY-HMQC spectra using pulsed field gradients. J Mag Reson B 101 : 210 213.
    • (1993) J Mag Reson B , vol.101 , pp. 210-213
    • Vuister, G.W.1    Clore, G.M.2    Gronenborn, A.M.3    Powers, R.4    Garrett, D.S.5    Tschudin, R.6    Bax, A.7
  • 73
    • 0034923356 scopus 로고    scopus 로고
    • Use of chemical shifts in macromolecular structure determination
    • Wishart, D.S. Case, D.A. (2001) Use of chemical shifts in macromolecular structure determination. Methods Enzymol 338 : 3 34.
    • (2001) Methods Enzymol , vol.338 , pp. 3-34
    • Wishart, D.S.1    Case, D.A.2
  • 75
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind, M. Mueller, L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J Magn Reson B 101 : 201 205.
    • (1993) J Magn Reson B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 77
    • 0028119538 scopus 로고
    • An HNCA pulse scheme for the backbone assignment of 15N, 13C, 2H-labeled proteins: Application to a 37-kDa epressor-DNA complex
    • Yamazaki, T., Lee, W., Revington, M., Mattiello, D.L., Dahlquist, F.W., Arrowsmith, C.H. Kay, L.E. (1994a) An HNCA pulse scheme for the backbone assignment of 15N, 13C, 2H-labeled proteins: application to a 37-kDa epressor-DNA complex. J Am Chem Soc 116 : 6464 6465.
    • (1994) J Am Chem Soc , vol.116 , pp. 6464-6465
    • Yamazaki, T.1    Lee, W.2    Revington, M.3    Mattiello, D.L.4    Dahlquist, F.W.5    Arrowsmith, C.H.6    Kay, L.E.7
  • 78
    • 0028578764 scopus 로고
    • A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity
    • Yamazaki, T., Lee, W., Arrowsmith, C.H., Muhandiram, D.R. Kay, L.E. (1994b) A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity. J Am Chem Soc 116 : 11655 11666.
    • (1994) J Am Chem Soc , vol.116 , pp. 11655-11666
    • Yamazaki, T.1    Lee, W.2    Arrowsmith, C.H.3    Muhandiram, D.R.4    Kay, L.E.5
  • 79
    • 0028541866 scopus 로고
    • Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • Zhang, O., Kay, L.E., Olivier, J.P. Forman-Kay, J.D. (1994) Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4 : 845 858.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 80
    • 0000517056 scopus 로고
    • Improved linear prediction for truncated signals of known phase
    • Zhu, G. Bax, A. (1990) Improved linear prediction for truncated signals of known phase. J Magn Reson 90 : 405 410.
    • (1990) J Magn Reson , vol.90 , pp. 405-410
    • Zhu, G.1    Bax, A.2
  • 81
    • 0000131371 scopus 로고
    • Two-dimensional linear prediction for signals truncated in both dimensions
    • Zhu, G. Bax, A. (1992) Two-dimensional linear prediction for signals truncated in both dimensions. J Magn Reson 98 : 192 199.
    • (1992) J Magn Reson , vol.98 , pp. 192-199
    • Zhu, G.1    Bax, A.2
  • 82
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • Zweckstetter, M. Bax, A. (2000) Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J Am Chem Soc 122 : 3791 3792.
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.