메뉴 건너뛰기




Volumn 11, Issue 7, 2012, Pages

The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PAPG PROTEIN; UNCLASSIFIED DRUG; ADHESIN; ATPG PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; FIMBRIA PROTEIN; PAPD PROTEIN, E COLI; PAPG PROTEIN, E COLI; PERIPLASMIC PROTEIN; PORIN; RECOMBINANT PROTEIN;

EID: 84863810994     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.015289     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 0026509588 scopus 로고
    • P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips
    • Kuehn, M. J., Heuser, J., Normark, S., and Hultgren, S. J. (1992) P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips. Nature 356, 252-255
    • (1992) Nature , vol.356 , pp. 252-255
    • Kuehn, M.J.1    Heuser, J.2    Normark, S.3    Hultgren, S.J.4
  • 2
    • 0032035356 scopus 로고    scopus 로고
    • The chaperone/usher pathway: A major terminal branch of the general secretory pathway
    • Thanassi, D. G., Saulino, E. T., and Hultgren, S. J. (1998) The chaperone/usher pathway: a major terminal branch of the general secretory pathway. Curr. Opin. Microbiol. 1, 223-231 (Pubitemid 128428064)
    • (1998) Current Opinion in Microbiology , vol.1 , Issue.2 , pp. 223-231
    • Thanassi, D.G.1    Saulino, E.T.2    Hultgren, S.J.3
  • 4
    • 34547909227 scopus 로고    scopus 로고
    • Development of intracellular bacterial communities of uropathogenic Escherichia coli depends on type 1 pili
    • DOI 10.1111/j.1462-5822.2007.00952.x
    • Wright, K. J., Seed, P. C., and Hultgren, S. J. (2007) Development of intracellular bacterial communities of uropathogenic Escherichia coli depends on type 1 pili. Cell Microbiol. 9, 2230-2241 (Pubitemid 47250294)
    • (2007) Cellular Microbiology , vol.9 , Issue.9 , pp. 2230-2241
    • Wright, K.J.1    Seed, P.C.2    Hultgren, S.J.3
  • 5
    • 0038270674 scopus 로고    scopus 로고
    • Epidemiology of urinary tract infections: Transmission and risk factors, incidence, and costs
    • DOI 10.1016/S0891-5520(03)00005-9
    • Foxman, B., and Brown, P. (2003) Epidemiology of urinary tract infections: transmission and risk factors, incidence, and costs. Infect. Dis. Clin. North Am. 17, 227-241 (Pubitemid 36760181)
    • (2003) Infectious Disease Clinics of North America , vol.17 , Issue.2 , pp. 227-241
    • Foxman, B.1    Brown, P.2
  • 6
    • 0023389683 scopus 로고
    • The PapG protein is the alpha-D-galactopyranosyl-(1-4)-beta-D- galactopyranose-binding adhesin of uropathogenic Escherichia coli
    • Lund, B., Lindberg, F., Marklund, B. I., and Normark, S. (1987) The PapG protein is the alpha-D-galactopyranosyl-(1-4)-beta-D-galactopyranose-binding adhesin of uropathogenic Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 84, 5898-5902
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5898-5902
    • Lund, B.1    Lindberg, F.2    Marklund, B.I.3    Normark, S.4
  • 7
    • 0023663381 scopus 로고
    • Biogenesis of E. coli Pap pili: PapH, a minor pilin subunit involved in cell anchoring and length modulation
    • Båga, M., Norgren, M., and Normark, S. (1987) Biogenesis of E. coli Pap pili: papH, a minor pilin subunit involved in cell anchoring and length modulation. Cell 49, 241-251
    • (1987) Cell , vol.49 , pp. 241-251
    • Båga, M.1    Norgren, M.2    Normark, S.3
  • 8
    • 74349129601 scopus 로고    scopus 로고
    • Two-step and one-step secretion mechanisms in Gram-negative bacteria: Contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis
    • Rêgo, A. T., Chandran, V., and Waksman, G. (2010) Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis. Biochem. J. 425, 475-488
    • (2010) Biochem. J. , vol.425 , pp. 475-488
    • Rêgo, A.T.1    Chandran, V.2    Waksman, G.3
  • 9
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • DOI 10.1016/S0092-8674(02)01050-4
    • Sauer, F. G., Pinkner, J. S., Waksman, G., and Hultgren, S. J. (2002) Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 111, 543-551 (Pubitemid 35356559)
    • (2002) Cell , vol.111 , Issue.4 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 10
    • 33751534447 scopus 로고    scopus 로고
    • Molecular mechanism of P pilus termination in uropathogenic Escherichia coli
    • DOI 10.1038/sj.embor.7400833, PII 7400833
    • Verger, D., Miller, E., Remaut, H., Waksman, G., and Hultgren, S. (2006) Molecular mechanism of P pilus termination in uropathogenic Escherichia coli. EMBO Rep. 7, 1228-1232 (Pubitemid 44835090)
    • (2006) EMBO Reports , vol.7 , Issue.12 , pp. 1228-1232
    • Verger, D.1    Miller, E.2    Remaut, H.3    Waksman, G.4    Hultgren, S.5
  • 11
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen, A. J., and Nouwen, N. (2008) Protein translocation across the bacterial cytoplasmic membrane. Annu. Rev. Biochem. 77, 643-667
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 12
    • 0026076419 scopus 로고
    • Chaperone-assisted assembly and molecular architecture of adhesive pili
    • Hultgren, S. J., Normark, S., and Abraham, S. N. (1991) Chaperone-assisted assembly and molecular architecture of adhesive pili. Annu. Rev. Microbiol. 45, 383-415 (Pubitemid 21903797)
    • (1991) Annual Review of Microbiology , vol.45 , Issue.1 , pp. 383-415
    • Hultgren, S.J.1    Normark, S.2    Abraham, S.N.3
  • 14
    • 43049171700 scopus 로고    scopus 로고
    • Fiber Formation across the Bacterial Outer Membrane by the Chaperone/Usher Pathway
    • DOI 10.1016/j.cell.2008.03.033, PII S0092867408004625
    • Remaut, H., Tang, C., Henderson, N. S., Pinkner, J. S., Wang, T., Hultgren, S. J., Thanassi, D. G., Waksman, G., and Li, H. (2008) Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. Cell 133, 640-652 (Pubitemid 351636304)
    • (2008) Cell , vol.133 , Issue.4 , pp. 640-652
    • Remaut, H.1    Tang, C.2    Henderson, N.S.3    Pinkner, J.S.4    Wang, T.5    Hultgren, S.J.6    Thanassi, D.G.7    Waksman, G.8    Li, H.9
  • 16
    • 3843050179 scopus 로고    scopus 로고
    • The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events
    • DOI 10.1128/JB.186.16.5321-5331.2004
    • Ng, T. W., Akman, L., Osisami, M., and Thanassi, D. G. (2004) The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events. J. Bacteriol. 186, 5321-5331 (Pubitemid 39038134)
    • (2004) Journal of Bacteriology , vol.186 , Issue.16 , pp. 5321-5331
    • Ng, T.W.1    Akman, L.2    Osisami, M.3    Thanassi, D.G.4
  • 17
    • 42349106617 scopus 로고    scopus 로고
    • Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst
    • DOI 10.1126/science.1154994
    • Nishiyama, M., Ishikawa, T., Rechsteiner, H., and Glockshuber, R. (2008) Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst. Science 320, 376-379 (Pubitemid 351555660)
    • (2008) Science , vol.320 , Issue.5874 , pp. 376-379
    • Nishiyama, M.1    Ishikawa, T.2    Rechsteiner, H.3    Glockshuber, R.4
  • 19
    • 37349025742 scopus 로고    scopus 로고
    • Donor-Strand Exchange in Chaperone-Assisted Pilus Assembly Revealed in Atomic Detail by Molecular Dynamics
    • DOI 10.1016/j.jmb.2007.10.077, PII S0022283607014362
    • Rose, R. J., Welsh, T. S., Waksman, G., Ashcroft, A. E., Radford, S. E., and Paci, E. (2008) Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics. J. Mol. Biol. 375, 908-919 (Pubitemid 350309390)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.4 , pp. 908-919
    • Rose, R.J.1    Welsh, T.S.2    Waksman, G.3    Ashcroft, A.E.4    Radford, S.E.5    Paci, E.6
  • 20
    • 0028302264 scopus 로고
    • Chaperone-assisted self-assembly of pili independent of cellular energy
    • Jacob-Dubuisson, F., Striker, R., and Hultgren, S. J. (1994) Chaperone-Assisted Self-Assembly of Pili Independent of Cellular-Energy. J. Biol. Chem. 269, 12447-12455 (Pubitemid 24202024)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12447-12455
    • Jacob-Dubuisson, F.1    Striker, R.2    Hultgren, S.J.3
  • 21
    • 79960030567 scopus 로고    scopus 로고
    • Second Order Rate Constants of Donor-Strand Exchange Reveal Individual Amino Acid Residues Important in Determining the Subunit Specificity of Pilus Biogenesis
    • Leney, A.C., Phan, G., Allen, W., Verger, D., Waksman, G., Radford, S.E., and Ashcroft, A.E. (2011) Second Order Rate Constants of Donor-Strand Exchange Reveal Individual Amino Acid Residues Important in Determining the Subunit Specificity of Pilus Biogenesis. J. Am. Soc. Mass Spectrom. 22, 1214-1223
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1214-1223
    • Leney, A.C.1    Phan, G.2    Allen, W.3    Verger, D.4    Waksman, G.5    Radford, S.E.6    Ashcroft, A.E.7
  • 23
    • 39649123737 scopus 로고    scopus 로고
    • Crystal structure of the ternary FimC-FimF(t) -FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD
    • Eidam, O., Dworkowski, F. S., Glockshuber, R., Grütter, M. G., and Capitani, G. (2008) Crystal structure of the ternary FimC-FimF(t) -FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD. FEBS Lett. 582, 651-655
    • (2008) FEBS Lett. , vol.582 , pp. 651-655
    • Eidam, O.1    Dworkowski, F.S.2    Glockshuber, R.3    Grütter, M.G.4    Capitani, G.5
  • 25
    • 66149150292 scopus 로고    scopus 로고
    • Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC
    • Huang, Y., Smith, B. S., Chen, L. X., Baxter, R. H., and Deisenhofer, J. (2009) Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Proc. Natl. Acad. Sci. U.S.A. 106, 7403-7407
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7403-7407
    • Huang, Y.1    Smith, B.S.2    Chen, L.X.3    Baxter, R.H.4    Deisenhofer, J.5
  • 26
    • 3042610168 scopus 로고    scopus 로고
    • P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli
    • DOI 10.1128/JB.186.13.4326-4337.2004
    • Lee, Y. M., DiGiuseppe, P. A., Silhavy, T. J., and Hultgren, S. J. (2004) P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli. J. Bacteriol. 186, 4326-4337 (Pubitemid 38802581)
    • (2004) Journal of Bacteriology , vol.186 , Issue.13 , pp. 4326-4337
    • Lee, Y.M.1    DiGiuseppe, P.A.2    Silhavy, T.J.3    Hultgren, S.J.4
  • 27
    • 0023940514 scopus 로고
    • Structure and antigenic properties of the tip-located P pilus proteins of uropathogenic Escherichia coli
    • Lund, B., Lindberg, F., and Normark, S. (1988) Structure and antigenic properties of the tip-located P pilus proteins of uropathogenic Escherichia coli. J. Bacteriol. 170, 1887-1894
    • (1988) J. Bacteriol. , vol.170 , pp. 1887-1894
    • Lund, B.1    Lindberg, F.2    Normark, S.3
  • 28
    • 0035875099 scopus 로고    scopus 로고
    • Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor
    • DOI 10.1016/S0092-8674(01)00388-9
    • Dodson, K. W., Pinkner, J. S., Rose, T., Magnusson, G., Hultgren, S. J., and Waksman, G. (2001) Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor. Cell 105, 733-743 (Pubitemid 32635103)
    • (2001) Cell , vol.105 , Issue.6 , pp. 733-743
    • Dodson, K.W.1    Pinkner, J.S.2    Rose, T.3    Magnusson, G.4    Hultgren, S.J.5    Waksman, G.6
  • 29
    • 33645300368 scopus 로고    scopus 로고
    • Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher C-terminus
    • So, S. S., and Thanassi, D. G. (2006) Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher C-terminus. Mol Microbiol 60, 364-375
    • (2006) Mol Microbiol , vol.60 , pp. 364-375
    • So, S.S.1    Thanassi, D.G.2
  • 30
    • 0038047135 scopus 로고    scopus 로고
    • Identification and characterization of the chaperone-subunit complex-binding domain from the type 1 pilus assembly platform FimD
    • DOI 10.1016/S0022-2836(03)00591-6
    • Nishiyama, M., Vetsch, M., Puorger, C., Jelesarov, I., and Glockshuber, R. (2003) Identification and characterization of the chaperone-subunit complex- binding domain from the type 1 pilus assembly platform FimD. J. Mol. Biol. 330, 513-525 (Pubitemid 36808685)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.3 , pp. 513-525
    • Nishiyama, M.1    Vetsch, M.2    Puorger, C.3    Jelesarov, I.4    Glockshuber, R.5
  • 31
    • 0037090377 scopus 로고    scopus 로고
    • Quatitative determination of noncovalent binding interaction using soft ionization mass spectrometry
    • Daniel, J. M., Friess, S. D., Rajagopalan, S., Wendt, S., and Zenobi, R. (2002) Quatitative determination of noncovalent binding interaction using soft ionization mass spectrometry. Int. J. Mass Spectrom. 216, 1-27
    • (2002) Int. J. Mass Spectrom. , vol.216 , pp. 1-27
    • Daniel, J.M.1    Friess, S.D.2    Rajagopalan, S.3    Wendt, S.4    Zenobi, R.5
  • 32
    • 0037954045 scopus 로고    scopus 로고
    • Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry
    • DOI 10.1021/ac034132x
    • Benesch, J. L., Sobott, F., and Robinson, C. V. (2003) Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry. Anal. Chem. 75, 2208-2214 (Pubitemid 36582800)
    • (2003) Analytical Chemistry , vol.75 , Issue.10 , pp. 2208-2214
    • Benesch, J.L.P.1    Sobott, F.2    Robinson, C.V.3
  • 33
    • 71449126172 scopus 로고    scopus 로고
    • Characterization, stoichiometry, and stability of salivary protein-tannin complexes by ESI-MS and ESI-MS/MS
    • Canon, F., Paté, F., Meudec, E., Marlin, T., Cheynier, V., Giuliani, A., and Sarni-Manchado, P. (2009) Characterization, stoichiometry, and stability of salivary protein-tannin complexes by ESI-MS and ESI-MS/MS. Anal. Bioanal. Chem. 395, 2535-2545
    • (2009) Anal. Bioanal. Chem. , vol.395 , pp. 2535-2545
    • Canon, F.1    Paté, F.2    Meudec, E.3    Marlin, T.4    Cheynier, V.5    Giuliani, A.6    Sarni-Manchado, P.7
  • 34
    • 79960579141 scopus 로고    scopus 로고
    • Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent
    • Han, L., Hyung, S. J., Mayers, J. J., and Ruotolo, B. T. (2011) Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent. J. Am. Chem. Soc. 133, 11358-11367
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 11358-11367
    • Han, L.1    Hyung, S.J.2    Mayers, J.J.3    Ruotolo, B.T.4
  • 35
    • 79956138063 scopus 로고    scopus 로고
    • Determinants of gas-phase disassembly behavior in homodimeric protein complexes with related yet divergent structures
    • Dodds, E. D., Blackwell, A. E., Jones, C. M., Holso, K. L., O'Brien, D. J., Cordes, M. H., and Wysocki, V. H. (2011) Determinants of gas-phase disassembly behavior in homodimeric protein complexes with related yet divergent structures. Anal. Chem. 83, 3881-3889
    • (2011) Anal. Chem. , vol.83 , pp. 3881-3889
    • Dodds, E.D.1    Blackwell, A.E.2    Jones, C.M.3    Holso, K.L.4    O'Brien, D.J.5    Cordes, M.H.6    Wysocki, V.H.7
  • 36
    • 64749105610 scopus 로고    scopus 로고
    • Gas-phase unfolding and disassembly reveals stability differences in ligand-bound multiprotein complexes
    • Hyung, S. J., Robinson, C. V., and Ruotolo, B. T. (2009) Gas-phase unfolding and disassembly reveals stability differences in ligand-bound multiprotein complexes. Chem. Biol. 16, 382-390
    • (2009) Chem. Biol. , vol.16 , pp. 382-390
    • Hyung, S.J.1    Robinson, C.V.2    Ruotolo, B.T.3
  • 37
    • 70349108740 scopus 로고    scopus 로고
    • Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: The effect of ligand binding on conformational stability
    • Hopper, J. T., and Oldham, N. J. (2009) Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: the effect of ligand binding on conformational stability. J. Am. So.c Mass. Spectrom. 20, 1851-1858
    • (2009) J. Am. So.c Mass. Spectrom. , vol.20 , pp. 1851-1858
    • Hopper, J.T.1    Oldham, N.J.2
  • 39
    • 0032522714 scopus 로고    scopus 로고
    • Ramifications of kinetic partitioning on usher-mediated pilus biogenesis
    • DOI 10.1093/emboj/17.8.2177
    • Saulino, E. T., Thanassi, D. G., Pinkner, J. S., and Hultgren, S. J. (1998) Ramifications of kinetic partitioning on usher-mediated pilus biogenesis. EMBO J. 17, 2177-2185 (Pubitemid 28171903)
    • (1998) EMBO Journal , vol.17 , Issue.8 , pp. 2177-2185
    • Saulino, E.T.1    Thanassi, D.G.2    Pinkner, J.S.3    Hultgren, S.J.4
  • 41
    • 33745192792 scopus 로고    scopus 로고
    • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
    • Benesch, J. L., Aquilina, J. A., Ruotolo, B. T., Sobott, F., and Robinson, C. V. (2006) Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies. Chem. Biol. 13, 597-605
    • (2006) Chem. Biol. , vol.13 , pp. 597-605
    • Benesch, J.L.1    Aquilina, J.A.2    Ruotolo, B.T.3    Sobott, F.4    Robinson, C.V.5
  • 42
    • 35648957210 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes
    • DOI 10.1002/anie.200702161
    • Ruotolo, B. T., Hyung, S. J., Robinson, P. M., Giles, K., Bateman, R. H., and Robinson, C. V. (2007) Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes. Angew. Chem. Int. Ed. Engl. 46, 8001-8004 (Pubitemid 350033476)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.42 , pp. 8001-8004
    • Ruotolo, B.T.1    Hyung, S.-J.2    Robinson, P.M.3    Giles, K.4    Bateman, R.H.5    Robinson, C.V.6
  • 43
    • 77953548631 scopus 로고    scopus 로고
    • Alternate dissociation pathways identified in charge-reduced protein complex ions
    • Pagel, K., Hyung, S. J., Ruotolo, B. T., and Robinson, C. V. (2010) Alternate dissociation pathways identified in charge-reduced protein complex ions. Anal. Chem. 82, 5363-5372
    • (2010) Anal. Chem. , vol.82 , pp. 5363-5372
    • Pagel, K.1    Hyung, S.J.2    Ruotolo, B.T.3    Robinson, C.V.4
  • 48
    • 0023412066 scopus 로고
    • Nucleotide sequence, regulation and functional analysis of the papC gene required for cell surface localization of Pap pili of uropathogenic Escherichia coli
    • Norgren, M., Båga, M., Tennent, J. M., and Normark, S. (1987) Nucleotide sequence, regulation and functional analysis of the papC gene required for cell surface localization of Pap pili of uropathogenic Escherichia coli. Mol. Microbiol. 1, 169-178
    • (1987) Mol. Microbiol. , vol.1 , pp. 169-178
    • Norgren, M.1    Båga, M.2    Tennent, J.M.3    Normark, S.4
  • 49
    • 0025069863 scopus 로고
    • The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae
    • Klemm, P., and Christiansen, G. (1990) The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae. Mol. Gen. Genet. 220, 334-338 (Pubitemid 20036272)
    • (1990) Molecular and General Genetics , vol.220 , Issue.2 , pp. 334-338
    • Klemm, P.1    Christiansen, G.2
  • 50
    • 0036842083 scopus 로고    scopus 로고
    • Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis
    • DOI 10.1128/JB.184.22.6260-6269.2002
    • Thanassi, D. G., Stathopoulos, C., Dodson, K., Geiger, D., and Hultgren, S. J. (2002) Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis. J. Bacteriol. 184, 6260-6269 (Pubitemid 35265907)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6260-6269
    • Thanassi, D.G.1    Stathopoulos, C.2    Dodson, K.3    Geiger, D.4    Hultgren, S.J.5
  • 51
    • 73649132280 scopus 로고    scopus 로고
    • Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher
    • Mapingire, O. S., Henderson, N. S., Duret, G., Thanassi, D. G., and Delcour, A. H. (2009) Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher. J. Biol. Chem. 284, 36324-36333
    • (2009) J. Biol. Chem. , vol.284 , pp. 36324-36333
    • Mapingire, O.S.1    Henderson, N.S.2    Duret, G.3    Thanassi, D.G.4    Delcour, A.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.