메뉴 건너뛰기




Volumn 91, Issue 10, 2006, Pages 3848-3856

The mechanical properties of E. coli type 1 pili measured by atomic force microscopy techniques

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN SUBUNIT;

EID: 33751245905     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.088989     Document Type: Article
Times cited : (136)

References (40)
  • 2
    • 0031962234 scopus 로고    scopus 로고
    • Bacterial adhesion pili are heterologous assemblies of similar subunits
    • Bullitt, E., and L. Makowski. 1998. Bacterial adhesion pili are heterologous assemblies of similar subunits. Biophys. J. 74:623-632.
    • (1998) Biophys. J. , vol.74 , pp. 623-632
    • Bullitt, E.1    Makowski, L.2
  • 3
    • 0027049870 scopus 로고
    • Helical structure of P pili from Escherichia coli. Evidence from x-ray fiber diffraction and scanning transmission electron microscopy
    • Gong, M., and L. Makowski. 1992. Helical structure of P pili from Escherichia coli. Evidence from x-ray fiber diffraction and scanning transmission electron microscopy. J. Mol. Biol. 228:735-742.
    • (1992) J. Mol. Biol. , vol.228 , pp. 735-742
    • Gong, M.1    Makowski, L.2
  • 4
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: Common themes and variations in architecture and assembly
    • Soto, G. E., and S. J. Hultgren. 1999. Bacterial adhesins: common themes and variations in architecture and assembly. J. Bacteriol. 181: 1059-1071.
    • (1999) J. Bacteriol. , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hultgren, S.J.2
  • 9
    • 0026076419 scopus 로고
    • Chaperone-assisted assembly and molecular architecture of adhesive pili
    • Hultgren, S. J., S. Normark, and S. N. Abraham. 1991. Chaperone-assisted assembly and molecular architecture of adhesive pili. Annu. Rev. Microbiol. 45:383-415.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 383-415
    • Hultgren, S.J.1    Normark, S.2    Abraham, S.N.3
  • 10
    • 0024215464 scopus 로고
    • Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobacteriaceae
    • Abraham, S. N., D. Sun, J. B. Dale, and E. H. Beachey. 1988. Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobacteriaceae. Nature. 336:682-684.
    • (1988) Nature , vol.336 , pp. 682-684
    • Abraham, S.N.1    Sun, D.2    Dale, J.B.3    Beachey, E.H.4
  • 11
    • 0034978222 scopus 로고    scopus 로고
    • Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection
    • Mulvey, M. A., J. D. Schilling, and S. J. Hultgren. 2001. Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection. Infect. Immun. 69:4572-4579.
    • (2001) Infect. Immun. , vol.69 , pp. 4572-4579
    • Mulvey, M.A.1    Schilling, J.D.2    Hultgren, S.J.3
  • 12
    • 0343668561 scopus 로고
    • The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in gram negative bacteria
    • Brinton, C. C., Jr. 1965. The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in gram negative bacteria. Trans. N. Y. Acad. Sci. 27: 1003-1054.
    • (1965) Trans. N. Y. Acad. Sci. , vol.27 , pp. 1003-1054
    • Brinton Jr., C.C.1
  • 13
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer, F. G., J. S. Pinkner, G. Waksman, and S. J. Hultgren. 2002. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell. 111:543-551.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 15
    • 21444442002 scopus 로고    scopus 로고
    • The unfolding of the P pili quaternary structure by stretching is reversible, not plastic
    • Fallman, E., S. Schedin, J. Jass, B. E. Uhlin, and O. Axner. 2005. The unfolding of the P pili quaternary structure by stretching is reversible, not plastic. EMBO Rep. 6:52-56.
    • (2005) EMBO Rep. , vol.6 , pp. 52-56
    • Fallman, E.1    Schedin, S.2    Jass, J.3    Uhlin, B.E.4    Axner, O.5
  • 16
    • 33646164897 scopus 로고    scopus 로고
    • A sticky chain model of the elongation and unfolding of Escherichia coli P pili under stress
    • Andersson, M., E. Fallman, B. E. Uhlin, and O. Axner. 2006. A sticky chain model of the elongation and unfolding of Escherichia coli P pili under stress. Biophys. J. 90:1521-1534.
    • (2006) Biophys. J. , vol.90 , pp. 1521-1534
    • Andersson, M.1    Fallman, E.2    Uhlin, B.E.3    Axner, O.4
  • 17
    • 0037188917 scopus 로고    scopus 로고
    • Bacterial adhesion to target cells enhanced by shear force
    • Thomas, W. E., E. Trintchina, M. Forero, V. Vogel, and E. V. Sokurenko. 2002. Bacterial adhesion to target cells enhanced by shear force. Cell. 109:913-923.
    • (2002) Cell , vol.109 , pp. 913-923
    • Thomas, W.E.1    Trintchina, E.2    Forero, M.3    Vogel, V.4    Sokurenko, E.V.5
  • 19
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 22
    • 0021435558 scopus 로고
    • Genes of pyelonephritogenic E. coli required for digalactoside-specific agglutination of human cells
    • Lindberg, F. P., B. Lund, and S. Normark. 1984. Genes of pyelonephritogenic E. coli required for digalactoside-specific agglutination of human cells. EMBO J. 3:1167-1173.
    • (1984) EMBO J. , vol.3 , pp. 1167-1173
    • Lindberg, F.P.1    Lund, B.2    Normark, S.3
  • 23
    • 0021232839 scopus 로고
    • Organization and expression of genes responsible for type 1 piliation in Escherichia coli
    • Orndorff, P. E., and S. Falkow. 1984. Organization and expression of genes responsible for type 1 piliation in Escherichia coli. J. Bacteriol. 159:736-744.
    • (1984) J. Bacteriol. , vol.159 , pp. 736-744
    • Orndorff, P.E.1    Falkow, S.2
  • 24
    • 0026509588 scopus 로고
    • P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips
    • Kuehn, M. J., J. Heuser, S. Normark, and S. J. Hultgren. 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
  • 26
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante, C., J. F. Marko, E. D. Siggia, and S. Smith. 1994. Entropic elasticity of lambda-phage DNA. Science. 265:1599-1600.
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 28
    • 4444247401 scopus 로고    scopus 로고
    • Shear-dependent 'stick-and-roll' adhesion of type 1 fimbriated Escherichia coli
    • Thomas, W. E., L. M. Nilsson, M. Forero, E. V. Sokurenko, and V. Vogel. 2004. Shear-dependent 'stick-and-roll' adhesion of type 1 fimbriated Escherichia coli. Mol. Microbiol. 53:1545-1557.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1545-1557
    • Thomas, W.E.1    Nilsson, L.M.2    Forero, M.3    Sokurenko, E.V.4    Vogel, V.5
  • 31
    • 0028794484 scopus 로고
    • Structural polymorphism of bacterial adhesion pili
    • Bullitt, E., and L. Makowski. 1995. Structural polymorphism of bacterial adhesion pili. Nature. 373:164-167.
    • (1995) Nature , vol.373 , pp. 164-167
    • Bullitt, E.1    Makowski, L.2
  • 33
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 35
    • 0035919831 scopus 로고    scopus 로고
    • Flexibility and extensibility in the titin molecule: Analysis of electron microscope data
    • Tskhovrebova, L., and J. Trinick. 2001. Flexibility and extensibility in the titin molecule: analysis of electron microscope data. J. Mol. Biol. 310:755-771.
    • (2001) J. Mol. Biol. , vol.310 , pp. 755-771
    • Tskhovrebova, L.1    Trinick, J.2
  • 36
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for the specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 37
    • 11844258265 scopus 로고    scopus 로고
    • A speed limit for conformational change of an allosteric membrane protein
    • Chakrapani, S., and A. Auerbach. 2005. A speed limit for conformational change of an allosteric membrane protein. Proc. Natl. Acad. Sci. USA. 102:87-92.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 87-92
    • Chakrapani, S.1    Auerbach, A.2
  • 38
    • 85030593578 scopus 로고    scopus 로고
    • Accessed October, 2006. [Online]
    • Protein ligand database. http://www-mitchell.ch.cam.ac.uk/pld. Accessed October, 2006. [Online].
    • Protein Ligand Database
  • 39
    • 0030884913 scopus 로고    scopus 로고
    • The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling
    • Alon, R., S. Chen, K. D. Puri, E. B. Finger, and T. A. Springer. 1997. The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling. J. Cell Biol. 138:1169-1180.
    • (1997) J. Cell Biol. , vol.138 , pp. 1169-1180
    • Alon, R.1    Chen, S.2    Puri, K.D.3    Finger, E.B.4    Springer, T.A.5
  • 40
    • 3342922288 scopus 로고    scopus 로고
    • A force-dependent switch reverses type IV pilus retraction
    • Maier, B., M. Koomey, and M. P. Sheetz. 2004. A force-dependent switch reverses type IV pilus retraction. Proc. Natl. Acad. Sci. USA. 101:10961-10966.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10961-10966
    • Maier, B.1    Koomey, M.2    Sheetz, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.