메뉴 건너뛰기




Volumn 189, Issue 18, 2007, Pages 6626-6634

In vivo oligomerization of the F conjugative coupling protein TraD

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TRAD; UNCLASSIFIED DRUG;

EID: 34548583310     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00513-07     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 0015057741 scopus 로고
    • Beginning a genetic analysis of conjugational transfer determined by the F factor in Escherichia coli by isolation and characterization of transfer-deficient mutants
    • Achtman, M., N. Willetts, and A. J. Clark. 1971. Beginning a genetic analysis of conjugational transfer determined by the F factor in Escherichia coli by isolation and characterization of transfer-deficient mutants. J. Bacteriol. 106:529-538.
    • (1971) J. Bacteriol , vol.106 , pp. 529-538
    • Achtman, M.1    Willetts, N.2    Clark, A.J.3
  • 2
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 9644272811 scopus 로고    scopus 로고
    • Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion
    • Atmakuri, K., E. Cascales, and P. J. Christie. 2004. Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion. Mol. Microbiol. 54:1199-1211.
    • (2004) Mol. Microbiol , vol.54 , pp. 1199-1211
    • Atmakuri, K.1    Cascales, E.2    Christie, P.J.3
  • 4
    • 0141789692 scopus 로고    scopus 로고
    • VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens
    • Atmakuri, K., Z. Ding, and P. J. Christie. 2003. VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens. Mol. Microbiol. 49:1699-1713.
    • (2003) Mol. Microbiol , vol.49 , pp. 1699-1713
    • Atmakuri, K.1    Ding, Z.2    Christie, P.J.3
  • 5
    • 2442483942 scopus 로고    scopus 로고
    • Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation
    • Cabezón, E., J. I. Sastre, and F. de la Cruz. 1997. Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation. Mol. Gen. Genet. 254:400-406.
    • (1997) Mol. Gen. Genet , vol.254 , pp. 400-406
    • Cabezón, E.1    Sastre, J.I.2    de la Cruz, F.3
  • 6
    • 33750210515 scopus 로고    scopus 로고
    • Homology modeling using parametric alignment ensemble generation with consensus and energy-based model selection
    • Chivian, D., and D. Baker. 2006. Homology modeling using parametric alignment ensemble generation with consensus and energy-based model selection. Nucleic Acids Res. 34:e112.
    • (2006) Nucleic Acids Res , vol.34
    • Chivian, D.1    Baker, D.2
  • 7
    • 30344443955 scopus 로고    scopus 로고
    • Prediction of CASP6 structures using automated Robetta protocols
    • Chivian, D., D. E. Kim, L. Malmstrom, J. Schonbrun, C. A. Rohl, and D. Baker. 2005. Prediction of CASP6 structures using automated Robetta protocols. Proteins 61(Suppl. 7):157-166.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 157-166
    • Chivian, D.1    Kim, D.E.2    Malmstrom, L.3    Schonbrun, J.4    Rohl, C.A.5    Baker, D.6
  • 8
    • 0035035578 scopus 로고    scopus 로고
    • Type IV secretion: Intercellular transfer of macromolecules by systems ancestrally related to conjugation machines
    • Christie, P. J. 2001. Type IV secretion: intercellular transfer of macromolecules by systems ancestrally related to conjugation machines. Mol. Microbiol. 40:294-305.
    • (2001) Mol. Microbiol , vol.40 , pp. 294-305
    • Christie, P.J.1
  • 9
    • 8844259469 scopus 로고    scopus 로고
    • Type IV secretion: The Agrobacterium VirB/D4 and related conjugation systems
    • Christie, P. J. 2004. Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems. Biochim. Biophys. Acta 1694:219-234.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 219-234
    • Christie, P.J.1
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 12
    • 0039702020 scopus 로고    scopus 로고
    • The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro
    • Disque-Kochem, C., and B. Dreiseikelmann. 1997. The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro. J. Bacteriol. 179:6133-6137.
    • (1997) J. Bacteriol , vol.179 , pp. 6133-6137
    • Disque-Kochem, C.1    Dreiseikelmann, B.2
  • 13
    • 0000862044 scopus 로고    scopus 로고
    • Structure and function of the F factor and mechanisms of conjugation
    • F. C. Neidhardt, R. Curtiss III, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, 2nd ed. ASM Press, Washington, DC
    • Firth, N., K. Ippen-Ihler, and R. A. Skurray. 1996. Structure and function of the F factor and mechanisms of conjugation, p. 2377-2382. In F. C. Neidhardt, R. Curtiss III, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 2377-2382
    • Firth, N.1    Ippen-Ihler, K.2    Skurray, R.A.3
  • 14
    • 0038385173 scopus 로고    scopus 로고
    • Interaction between the IncHI1 plasmid R27 coupling protein and type IV secretion system: TraG associates with the coiled-coil mating pair formation protein TrhB
    • Gilmour, M. W., J. E. Gunton, T. D. Lawley, and D. E. Taylor. 2003. Interaction between the IncHI1 plasmid R27 coupling protein and type IV secretion system: TraG associates with the coiled-coil mating pair formation protein TrhB. Mol. Microbiol. 49:105-116.
    • (2003) Mol. Microbiol , vol.49 , pp. 105-116
    • Gilmour, M.W.1    Gunton, J.E.2    Lawley, T.D.3    Taylor, D.E.4
  • 15
    • 0036217298 scopus 로고    scopus 로고
    • Structure and role of coupling proteins in conjugal DNA transfer
    • Gomis-Ruth, F. X., F. de la Cruz, and M. Coll. 2002. Structure and role of coupling proteins in conjugal DNA transfer. Res. Microbiol. 153:199-204.
    • (2002) Res. Microbiol , vol.153 , pp. 199-204
    • Gomis-Ruth, F.X.1    de la Cruz, F.2    Coll, M.3
  • 16
    • 0036510408 scopus 로고    scopus 로고
    • Conjugative plasmid protein TrwB, an integral membrane type IV secretion system coupling protein. Detailed structural features and mapping of the active site cleft
    • Gomis-Ruth, F. X., G. Moncalian, F. de la Cruz, and M. Coll. 2002. Conjugative plasmid protein TrwB, an integral membrane type IV secretion system coupling protein. Detailed structural features and mapping of the active site cleft. J. Biol. Chem. 277:7556-7566.
    • (2002) J. Biol. Chem , vol.277 , pp. 7556-7566
    • Gomis-Ruth, F.X.1    Moncalian, G.2    de la Cruz, F.3    Coll, M.4
  • 18
    • 27744482189 scopus 로고    scopus 로고
    • Subcellular localization and functional domains of the coupling protein, TraG, from IncHI1 plasmid R27
    • Gunton, J. E., M. W. Gilmour, G. Alonso, and D. E. Taylor. 2005. Subcellular localization and functional domains of the coupling protein, TraG, from IncHI1 plasmid R27. Microbiology 151:3549-3561.
    • (2005) Microbiology , vol.151 , pp. 3549-3561
    • Gunton, J.E.1    Gilmour, M.W.2    Alonso, G.3    Taylor, D.E.4
  • 19
    • 33847225606 scopus 로고    scopus 로고
    • Interaction between the co-inherited TraG coupling protein and the TraJ membrane-associated protein of the H-plasmid conjugative DNA transfer system resembles chromosomal DNA translocases
    • Gunton, J. E., M. W. Gilmour, K. P. Baptista, T. D. Lawley, and D. E. Taylor. 2007. Interaction between the co-inherited TraG coupling protein and the TraJ membrane-associated protein of the H-plasmid conjugative DNA transfer system resembles chromosomal DNA translocases. Microbiology 153: 428-441.
    • (2007) Microbiology , vol.153 , pp. 428-441
    • Gunton, J.E.1    Gilmour, M.W.2    Baptista, K.P.3    Lawley, T.D.4    Taylor, D.E.5
  • 21
    • 0034053027 scopus 로고    scopus 로고
    • TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58
    • Hamilton, C. M., H. Lee, P. L. Li, D. M. Cook, K. R. Piper, S. B. von Bodman, E. Lanka, W. Ream, and S. K. Farrand. 2000. TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58. J. Bacteriol. 182:1541-1548.
    • (2000) J. Bacteriol , vol.182 , pp. 1541-1548
    • Hamilton, C.M.1    Lee, H.2    Li, P.L.3    Cook, D.M.4    Piper, K.R.5    von Bodman, S.B.6    Lanka, E.7    Ream, W.8    Farrand, S.K.9
  • 22
    • 0037195792 scopus 로고    scopus 로고
    • Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation
    • Hormaeche, I., I. Alkorta, F. Moro, J. M. Valpuesta, F. M. Goni, and F. De La Cruz. 2002. Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation. J. Biol. Chem. 277:46456-46462.
    • (2002) J. Biol. Chem , vol.277 , pp. 46456-46462
    • Hormaeche, I.1    Alkorta, I.2    Moro, F.3    Valpuesta, J.M.4    Goni, F.M.5    De La Cruz, F.6
  • 23
    • 1642483698 scopus 로고    scopus 로고
    • Role of the transmembrane domain in the stability of TrwB, an integral protein involved in bacterial conjugation
    • Hormaeche, I., I. Iloro, J. L. Arrondo, F. M. Goni, F. de la Cruz, and I. Alkorta. 2004. Role of the transmembrane domain in the stability of TrwB, an integral protein involved in bacterial conjugation. J. Biol. Chem. 279: 10955-10961.
    • (2004) J. Biol. Chem , vol.279 , pp. 10955-10961
    • Hormaeche, I.1    Iloro, I.2    Arrondo, J.L.3    Goni, F.M.4    de la Cruz, F.5    Alkorta, I.6
  • 24
    • 33646586059 scopus 로고    scopus 로고
    • The transmembrane domain provides nucleotide binding specificity to the bacterial conjugation protein TrwB
    • Hormaeche, I., R. L. Segura, A. J. Vecino, F. M. Goni, F. de la Cruz, and I. Alkorta. 2006. The transmembrane domain provides nucleotide binding specificity to the bacterial conjugation protein TrwB. FEBS Lett. 580:3075-3082.
    • (2006) FEBS Lett , vol.580 , pp. 3075-3082
    • Hormaeche, I.1    Segura, R.L.2    Vecino, A.J.3    Goni, F.M.4    de la Cruz, F.5    Alkorta, I.6
  • 26
    • 4043169178 scopus 로고    scopus 로고
    • Evidence for multiple pathways in the assembly of the Escherichia coli maltose transport complex
    • Kennedy, K. A., E. G. Gachelet, and B. Traxler. 2004. Evidence for multiple pathways in the assembly of the Escherichia coli maltose transport complex. J. Biol. Chem. 279:33290-33297.
    • (2004) J. Biol. Chem , vol.279 , pp. 33290-33297
    • Kennedy, K.A.1    Gachelet, E.G.2    Traxler, B.3
  • 27
    • 0033525529 scopus 로고    scopus 로고
    • 2 ATP-binding cassette transporter of Escherichia coli
    • 2 ATP-binding cassette transporter of Escherichia coli. J. Biol. Chem. 274:6259-6264.
    • (1999) J. Biol. Chem , vol.274 , pp. 6259-6264
    • Kennedy, K.A.1    Traxler, B.2
  • 28
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • Kuhlman, B., and D. Baker. 2000. Native protein sequences are close to optimal for their structures. Proc. Natl. Acad. Sci. USA 97:10383-10388.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 29
    • 0036268202 scopus 로고    scopus 로고
    • Polar location and functional domains of the Agrobacterium tumefaciens DNA transfer protein VirD4
    • Kumar, R. B., and A. Das. 2002. Polar location and functional domains of the Agrobacterium tumefaciens DNA transfer protein VirD4. Mol. Microbiol. 43:1523-1532.
    • (2002) Mol. Microbiol , vol.43 , pp. 1523-1532
    • Kumar, R.B.1    Das, A.2
  • 30
    • 34548571303 scopus 로고    scopus 로고
    • Lawley, T. D., B. M. Wilkins, and L. Frost. 2004. Bacterial conjugation in gram-negative bacteria, p. 203-226. In G. Phillips and B. E. Funnell (ed.), Plasmid biology. ASM Press, Washington, DC.
    • Lawley, T. D., B. M. Wilkins, and L. Frost. 2004. Bacterial conjugation in gram-negative bacteria, p. 203-226. In G. Phillips and B. E. Funnell (ed.), Plasmid biology. ASM Press, Washington, DC.
  • 31
    • 0032878816 scopus 로고    scopus 로고
    • Analysis of F factor TraD membrane topology by use of gene fusions and trypsin-sensitive insertions
    • Lee, M. H., N. Kosuk, J. Bailey, B. Traxler, and C. Manoil. 1999. Analysis of F factor TraD membrane topology by use of gene fusions and trypsin-sensitive insertions. J. Bacteriol. 181:6108-6113.
    • (1999) J. Bacteriol , vol.181 , pp. 6108-6113
    • Lee, M.H.1    Kosuk, N.2    Bailey, J.3    Traxler, B.4    Manoil, C.5
  • 32
    • 0026452284 scopus 로고
    • Relationship of DNA-transfer-systems: Essential transfer factors of plasmids RP4, Ti and F share common sequences
    • Lessl, M., W. Pansegrau, and E. Lanka. 1992. Relationship of DNA-transfer-systems: essential transfer factors of plasmids RP4, Ti and F share common sequences. Nucleic Acids Res. 20:6099-6100.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6099-6100
    • Lessl, M.1    Pansegrau, W.2    Lanka, E.3
  • 33
    • 0031039347 scopus 로고    scopus 로고
    • MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants
    • Lippincott, J., and B. Traxler. 1997. MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants. J. Bacteriol. 179:1337-1343.
    • (1997) J. Bacteriol , vol.179 , pp. 1337-1343
    • Lippincott, J.1    Traxler, B.2
  • 34
    • 0036047412 scopus 로고    scopus 로고
    • Bacterial conjugation: A two-step mechanism for DNA transport
    • Llosa, M., F. X. Gomis-Ruth, M. Coll, and F. de la Cruz. 2002. Bacterial conjugation: a two-step mechanism for DNA transport. Mol. Microbiol. 45:1-8.
    • (2002) Mol. Microbiol , vol.45 , pp. 1-8
    • Llosa, M.1    Gomis-Ruth, F.X.2    Coll, M.3    de la Cruz, F.4
  • 35
    • 0042838290 scopus 로고    scopus 로고
    • Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes
    • Llosa, M., S. Zunzunegui, and F. de la Cruz. 2003. Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes. Proc. Natl. Acad. Sci. USA 100:10465-10470.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10465-10470
    • Llosa, M.1    Zunzunegui, S.2    de la Cruz, F.3
  • 36
    • 21844449126 scopus 로고    scopus 로고
    • Mutations in the C-terminal region of TraM provide evidence for in vivo TraM-TraD interactions during F-plasmid conjugation
    • Lu, J., and L. S. Frost. 2005. Mutations in the C-terminal region of TraM provide evidence for in vivo TraM-TraD interactions during F-plasmid conjugation. J. Bacteriol. 187:4767-4773.
    • (2005) J. Bacteriol , vol.187 , pp. 4767-4773
    • Lu, J.1    Frost, L.S.2
  • 38
    • 0031588907 scopus 로고    scopus 로고
    • A simple screen for permissive sites in proteins: Analysis of Escherichia coli lac permease
    • Manoil, C., and J. Bailey. 1997. A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease. J. Mol. Biol. 267:250-263.
    • (1997) J. Mol. Biol , vol.267 , pp. 250-263
    • Manoil, C.1    Bailey, J.2
  • 39
    • 0034090215 scopus 로고    scopus 로고
    • Insertion of in-frame sequence tags into proteins using transposons
    • Manoil, C., and B. Traxler. 2000. Insertion of in-frame sequence tags into proteins using transposons. Methods 20:55-61.
    • (2000) Methods , vol.20 , pp. 55-61
    • Manoil, C.1    Traxler, B.2
  • 41
    • 0027375813 scopus 로고
    • Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter: The maltose transport system of Escherichia coli
    • Panagiotidis, C., M. Reyes, A. Sievertsen, W. Boos, and H. Shuman. 1993. Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter: the maltose transport system of Escherichia coli. J. Biol. Chem. 268:23685-23696.
    • (1993) J. Biol. Chem , vol.268 , pp. 23685-23696
    • Panagiotidis, C.1    Reyes, M.2    Sievertsen, A.3    Boos, W.4    Shuman, H.5
  • 42
    • 0021821333 scopus 로고    scopus 로고
    • Panicker, M. M., and E. G. Minkley, Jr. 1985. DNA transfer occurs during a cell surface contact stage of F sex factor-mediated bacterial conjugation. J. Bacteriol. 162:584-590.
    • Panicker, M. M., and E. G. Minkley, Jr. 1985. DNA transfer occurs during a cell surface contact stage of F sex factor-mediated bacterial conjugation. J. Bacteriol. 162:584-590.
  • 43
    • 0026628697 scopus 로고    scopus 로고
    • Panicker, M. M., and E. G. Minkley, Jr. 1992. Purification and properties of the F sex factor TraD protein, an inner membrane conjugal transfer protein. J. Biol. Chem. 267:12761-12766.
    • Panicker, M. M., and E. G. Minkley, Jr. 1992. Purification and properties of the F sex factor TraD protein, an inner membrane conjugal transfer protein. J. Biol. Chem. 267:12761-12766.
  • 44
    • 2442449534 scopus 로고    scopus 로고
    • Modeling structurally variable regions in homologous proteins with Rosetta
    • Rohl, C. A., C. E. Strauss, D. Chivian, and D. Baker. 2004. Modeling structurally variable regions in homologous proteins with Rosetta. Proteins 55:656-677.
    • (2004) Proteins , vol.55 , pp. 656-677
    • Rohl, C.A.1    Strauss, C.E.2    Chivian, D.3    Baker, D.4
  • 45
    • 0031765579 scopus 로고    scopus 로고
    • The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer
    • Sastre, J. I., E. Cabezón, and F. de la Cruz. 1998. The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer. J. Bacteriol. 180:6039-6042.
    • (1998) J. Bacteriol , vol.180 , pp. 6039-6042
    • Sastre, J.I.1    Cabezón, E.2    de la Cruz, F.3
  • 46
    • 0036239133 scopus 로고    scopus 로고
    • TraG-like proteins of DNA transfer systems and of the Helicobacter pylori type IV secretion system: Inner membrane gate for exported substrates?
    • Schröder, G., S. Krause, E. L. Zechner, B. Traxler, H. J. Yeo, R. Lurz, G. Waksman, and E. Lanka. 2002. TraG-like proteins of DNA transfer systems and of the Helicobacter pylori type IV secretion system: inner membrane gate for exported substrates? J. Bacteriol. 184:2767-2779.
    • (2002) J. Bacteriol , vol.184 , pp. 2767-2779
    • Schröder, G.1    Krause, S.2    Zechner, E.L.3    Traxler, B.4    Yeo, H.J.5    Lurz, R.6    Waksman, G.7    Lanka, E.8
  • 47
    • 0037767570 scopus 로고    scopus 로고
    • TraG-like proteins of type IV secretion systems: Functional dissection of the multiple activities of TraG (RP4) and TrwB (R388)
    • Schröder, G., and E. Lanka. 2003. TraG-like proteins of type IV secretion systems: functional dissection of the multiple activities of TraG (RP4) and TrwB (R388). J. Bacteriol. 185:4371-4381.
    • (2003) J. Bacteriol , vol.185 , pp. 4371-4381
    • Schröder, G.1    Lanka, E.2
  • 48
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons, K. T., C. Kooperberg, E. Huang, and D. Baker. 1997. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268:209-225.
    • (1997) J. Mol. Biol , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 49
    • 20444431234 scopus 로고    scopus 로고
    • TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase
    • Tato, I., S. Zunzunegui, F. de la Cruz, and E. Cabezón. 2005. TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase. Proc. Natl. Acad. Sci. USA 102:8156-8161.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8156-8161
    • Tato, I.1    Zunzunegui, S.2    de la Cruz, F.3    Cabezón, E.4
  • 50
    • 0026469992 scopus 로고
    • Assembly of a hetero-oligomeric membrane protein complex
    • Traxler, B., and J. Beckwith. 1992. Assembly of a hetero-oligomeric membrane protein complex. Proc. Natl. Acad. Sci. USA 89:10852-10856.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10852-10856
    • Traxler, B.1    Beckwith, J.2
  • 51
    • 0034806683 scopus 로고    scopus 로고
    • Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance
    • Waters, C. M., and G. M. Dunny. 2001. Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance. J. Bacteriol. 183:5659-5667.
    • (2001) J. Bacteriol , vol.183 , pp. 5659-5667
    • Waters, C.M.1    Dunny, G.M.2
  • 52
    • 3142683278 scopus 로고    scopus 로고
    • An amino-terminal domain of Enterococcus faecalis aggregation substance is required for aggregation, bacterial internalization by epithelial cells and binding to lipoteichoic acid
    • Waters, C. M., H. Hirt, J. K. McCormick, P. M. Schlievert, C. L. Wells, and G. M. Dunny. 2004. An amino-terminal domain of Enterococcus faecalis aggregation substance is required for aggregation, bacterial internalization by epithelial cells and binding to lipoteichoic acid. Mol. Microbiol. 52:1159-1171.
    • (2004) Mol. Microbiol , vol.52 , pp. 1159-1171
    • Waters, C.M.1    Hirt, H.2    McCormick, J.K.3    Schlievert, P.M.4    Wells, C.L.5    Dunny, G.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.