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Volumn 6, Issue 13, 2004, Pages 1205-1211

Re-structuring the host cell: Up close with Salmonella's molecular machinery

Author keywords

Actin; Rho GTP binding proteins; Salmonella; Type III secretion; X ray crystallography

Indexed keywords

ACTIN;

EID: 5644282652     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micinf.2004.08.001     Document Type: Short Survey
Times cited : (10)

References (59)
  • 1
    • 0034255340 scopus 로고    scopus 로고
    • Striking a balance: Modulation of the actin cytoskeleton by Salmonella
    • J.E. Galan, and D. Zhou Striking a balance: modulation of the actin cytoskeleton by Salmonella Proc. Natl. Acad. Sci. USA 97 16 2000 8754 8761
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.16 , pp. 8754-8761
    • Galan, J.E.1    Zhou, D.2
  • 2
    • 0034237801 scopus 로고    scopus 로고
    • Bacterial protein toxins targeting Rho GTPases
    • M. Lerm, G. Schmidt, and K. Aktories Bacterial protein toxins targeting Rho GTPases FEMS Microbiol. Lett. 188 1 2000 1 6
    • (2000) FEMS Microbiol. Lett. , vol.188 , Issue.1 , pp. 1-6
    • Lerm, M.1    Schmidt, G.2    Aktories, K.3
  • 3
    • 0033924259 scopus 로고    scopus 로고
    • Rho GTPases as targets of bacterial protein toxins
    • K. Aktories, G. Schmidt, and I. Just Rho GTPases as targets of bacterial protein toxins Biol. Chem. 381 5-6 2000 421 426
    • (2000) Biol. Chem. , vol.381 , Issue.5-6 , pp. 421-426
    • Aktories, K.1    Schmidt, G.2    Just, I.3
  • 4
    • 0035188434 scopus 로고    scopus 로고
    • Salmonella interactions with host cell: Type III secretion at work
    • J.E. Galan Salmonella interactions with host cell: type III secretion at work Annu. Rev. Cell Dev. Biol. 17 2001 53 86
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 53-86
    • Galan, J.E.1
  • 6
    • 0036161224 scopus 로고    scopus 로고
    • The invasion-associated type III secretion system of Salmonella enterica serovar typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells
    • O. Steele-Mortimer, J.H. Brumell, L.A. Knodler, S. Meresse, A. Lopez, and B.B. Finlay The invasion-associated type III secretion system of Salmonella enterica serovar typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells Cell Microbiol. 4 1 2002 43 54
    • (2002) Cell Microbiol. , vol.4 , Issue.1 , pp. 43-54
    • Steele-Mortimer, O.1    Brumell, J.H.2    Knodler, L.A.3    Meresse, S.4    Lopez, A.5    Finlay, B.B.6
  • 7
    • 0029051147 scopus 로고
    • Typhoid fever and other salmonellosis: A continuing challenge
    • T. Pang, Z.A. Bhutta, B.B. Finlay, and M. Altwegg Typhoid fever and other salmonellosis: a continuing challenge Trends Microbiol. 3 7 1995 253 255
    • (1995) Trends Microbiol. , vol.3 , Issue.7 , pp. 253-255
    • Pang, T.1    Bhutta, Z.A.2    Finlay, B.B.3    Altwegg, M.4
  • 8
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • J.E. Galan, and A. Collmer Type III secretion machines: bacterial devices for protein delivery into host cells Science 284 5418 1999 1322 1328
    • (1999) Science , vol.284 , Issue.5418 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 9
    • 0036165971 scopus 로고    scopus 로고
    • Assembly of the type III secretion needle complex of Salmonella typhimurium
    • T.G. Kimbrough, and S.I. Miller Assembly of the type III secretion needle complex of Salmonella typhimurium Microbes Infect. 4 1 2002 75 82
    • (2002) Microbes Infect. , vol.4 , Issue.1 , pp. 75-82
    • Kimbrough, T.G.1    Miller, S.I.2
  • 10
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • T. Kubori, Y. Matsushima, D. Nakamura, J. Uralil, M. Lara-Tejero, and A. Sukhan Supramolecular structure of the Salmonella typhimurium type III protein secretion system Science 280 5363 1998 602 605
    • (1998) Science , vol.280 , Issue.5363 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3    Uralil, J.4    Lara-Tejero, M.5    Sukhan, A.6
  • 11
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar typhimurium type III secretion-associated needle complex
    • A. Sukhan, T. Kubori, J. Wilson, and J.E. Galan Genetic analysis of assembly of the Salmonella enterica serovar typhimurium type III secretion-associated needle complex J. Bacteriol. 183 4 2001 1159 1167
    • (2001) J. Bacteriol. , vol.183 , Issue.4 , pp. 1159-1167
    • Sukhan, A.1    Kubori, T.2    Wilson, J.3    Galan, J.E.4
  • 12
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • C.J. Hueck Type III protein secretion systems in bacterial pathogens of animals and plants Microbiol. Mol. Biol. Rev. 62 2 1998 379 433
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , Issue.2 , pp. 379-433
    • Hueck, C.J.1
  • 14
    • 0025852616 scopus 로고
    • Cytoskeletal rearrangements accompanying Salmonella entry into epithelial cells
    • B.B. Finlay, S. Ruschkowski, and S. Dedhar Cytoskeletal rearrangements accompanying Salmonella entry into epithelial cells J. Cell Sci. 99 Pt 2 1991 283 296
    • (1991) J. Cell Sci. , vol.99 , Issue.2 , pp. 283-296
    • Finlay, B.B.1    Ruschkowski, S.2    Dedhar, S.3
  • 15
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • N. Tapon, and A. Hall Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton Curr. Opin. Cell Biol. 9 1 1997 86 92
    • (1997) Curr. Opin. Cell Biol. , vol.9 , Issue.1 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 16
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • D. Yarar, W. To, A. Abo, and M.D. Welch The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex Curr. Biol. 9 10 1999 555 558
    • (1999) Curr. Biol. , vol.9 , Issue.10 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, M.D.4
  • 17
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • A. Hall Rho GTPases and the actin cytoskeleton Science 279 5350 1998 509 514
    • (1998) Science , vol.279 , Issue.5350 , pp. 509-514
    • Hall, A.1
  • 18
    • 0033923731 scopus 로고    scopus 로고
    • Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell
    • S. Stender, A. Friebel, S. Linder, M. Rohde, S. Mirold, and W.D. Hardt Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell Mol. Microbiol. 36 6 2000 1206 1221
    • (2000) Mol. Microbiol. , vol.36 , Issue.6 , pp. 1206-1221
    • Stender, S.1    Friebel, A.2    Linder, S.3    Rohde, M.4    Mirold, S.5    Hardt, W.D.6
  • 19
    • 0034074961 scopus 로고    scopus 로고
    • Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells
    • C.S. Bakshi, V.P. Singh, M.W. Wood, P.W. Jones, T.S. Wallis, and E.E. Galyov Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells J. Bacteriol. 182 8 2000 2341 2344
    • (2000) J. Bacteriol. , vol.182 , Issue.8 , pp. 2341-2344
    • Bakshi, C.S.1    Singh, V.P.2    Wood, M.W.3    Jones, P.W.4    Wallis, T.S.5    Galyov, E.E.6
  • 20
    • 0032577563 scopus 로고    scopus 로고
    • Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • W.D. Hardt, L.M. Chen, K.E. Schuebel, X.R. Bustelo, and J.E. Galan Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells Cell 93 5 1998 815 826
    • (1998) Cell , vol.93 , Issue.5 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galan, J.E.5
  • 21
    • 0032748576 scopus 로고    scopus 로고
    • Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for Rho GTPases
    • M.G. Rudolph, C. Weise, S. Mirold, B. Hillenbrand, B. Bader, and A. Wittinghofer Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for Rho GTPases J. Biol. Chem. 274 43 1999 30501 30509
    • (1999) J. Biol. Chem. , vol.274 , Issue.43 , pp. 30501-30509
    • Rudolph, M.G.1    Weise, C.2    Mirold, S.3    Hillenbrand, B.4    Bader, B.5    Wittinghofer, A.6
  • 22
    • 0033575956 scopus 로고    scopus 로고
    • A Salmonella protein antagonizes Rac1 and Cdc42 to mediate host cell recovery after bacterial invasion
    • Y. Fu, and J.E. Galan A Salmonella protein antagonizes Rac1 and Cdc42 to mediate host cell recovery after bacterial invasion Nature 401 6750 1999 293 297
    • (1999) Nature , vol.401 , Issue.6750 , pp. 293-297
    • Fu, Y.1    Galan, J.E.2
  • 23
    • 0036646473 scopus 로고    scopus 로고
    • Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
    • G. Buchwald, A. Friebel, J.E. Galan, W.D. Hardt, A. Wittinghofer, and K. Scheffzek Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE EMBO J. 21 13 2002 3286 3295
    • (2002) EMBO J. , vol.21 , Issue.13 , pp. 3286-3295
    • Buchwald, G.1    Friebel, A.2    Galan, J.E.3    Hardt, W.D.4    Wittinghofer, A.5    Scheffzek, K.6
  • 24
    • 0035147455 scopus 로고    scopus 로고
    • A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
    • D. Zhou, L.M. Chen, L. Hernandez, S.B. Shears, and J.E. Galan A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization Mol. Microbiol. 39 2 2001 248 259
    • (2001) Mol. Microbiol. , vol.39 , Issue.2 , pp. 248-259
    • Zhou, D.1    Chen, L.M.2    Hernandez, L.3    Shears, S.B.4    Galan, J.E.5
  • 25
    • 0035823591 scopus 로고    scopus 로고
    • SopE and SopE2 from Salmonella typhimurium activate different sets of Rho GTPases of the host cell
    • A. Friebel, H. Ilchmann, M. Aepfelbacher, K. Ehrbar, W. Machleidt, and W.D. Hardt SopE and SopE2 from Salmonella typhimurium activate different sets of Rho GTPases of the host cell J. Biol. Chem. 276 36 2001 34035 34040
    • (2001) J. Biol. Chem. , vol.276 , Issue.36 , pp. 34035-34040
    • Friebel, A.1    Ilchmann, H.2    Aepfelbacher, M.3    Ehrbar, K.4    MacHleidt, W.5    Hardt, W.D.6
  • 26
    • 0032564446 scopus 로고    scopus 로고
    • SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase
    • F.A. Norris, M.P. Wilson, T.S. Wallis, E.E. Galyov, and P.W. Majerus SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase Proc. Natl. Acad. Sci. USA 95 24 1998 14057 14059
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.24 , pp. 14057-14059
    • Norris, F.A.1    Wilson, M.P.2    Wallis, T.S.3    Galyov, E.E.4    Majerus, P.W.5
  • 27
    • 0035970013 scopus 로고    scopus 로고
    • Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export
    • Y. Feng, S.R. Wente, and P.W. Majerus Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export Proc. Natl. Acad. Sci. USA 98 3 2001 875 879
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.3 , pp. 875-879
    • Feng, Y.1    Wente, S.R.2    Majerus, P.W.3
  • 28
    • 0036081338 scopus 로고    scopus 로고
    • The Salmonella enterica serotype typhimurium effector proteins SipA, SopA, SopB, SopD, and SopE2 act in concert to induce diarrhea in calves
    • S. Zhang, R.L. Santos, R.M. Tsolis, S. Stender, W.D. Hardt, and A.J. Baumler The Salmonella enterica serotype typhimurium effector proteins SipA, SopA, SopB, SopD, and SopE2 act in concert to induce diarrhea in calves Infect. Immun. 70 7 2002 3843 3855
    • (2002) Infect. Immun. , vol.70 , Issue.7 , pp. 3843-3855
    • Zhang, S.1    Santos, R.L.2    Tsolis, R.M.3    Stender, S.4    Hardt, W.D.5    Baumler, A.J.6
  • 29
    • 0036319223 scopus 로고    scopus 로고
    • Salmonella enterica serovar typhimurium effector SigD/SopB is membrane-associated and ubiquitinated inside host cells
    • S.L. Marcus, L.A. Knodler, and B.B. Finlay Salmonella enterica serovar typhimurium effector SigD/SopB is membrane-associated and ubiquitinated inside host cells Cell. Microbiol. 4 7 2002 435 446
    • (2002) Cell. Microbiol. , vol.4 , Issue.7 , pp. 435-446
    • Marcus, S.L.1    Knodler, L.A.2    Finlay, B.B.3
  • 30
    • 0035853477 scopus 로고    scopus 로고
    • A synaptojanin-homologous region of Salmonella typhimurium SigD is essential for inositol phosphatase activity and Akt activation
    • S.L. Marcus, M.R. Wenk, O. Steele-Mortimer, and B.B. Finlay A synaptojanin-homologous region of Salmonella typhimurium SigD is essential for inositol phosphatase activity and Akt activation FEBS Lett. 494 3 2001 201 207
    • (2001) FEBS Lett. , vol.494 , Issue.3 , pp. 201-207
    • Marcus, S.L.1    Wenk, M.R.2    Steele-Mortimer, O.3    Finlay, B.B.4
  • 31
    • 0031983624 scopus 로고    scopus 로고
    • The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton
    • Y. Fu, and J.E. Galan The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton Mol. Microbiol. 27 2 1998 359 368
    • (1998) Mol. Microbiol. , vol.27 , Issue.2 , pp. 359-368
    • Fu, Y.1    Galan, J.E.2
  • 32
    • 0344413859 scopus 로고    scopus 로고
    • Temporal regulation of Salmonella virulence effector function by proteasome-dependent protein degradation
    • T. Kubori, and J.E. Galan Temporal regulation of Salmonella virulence effector function by proteasome-dependent protein degradation Cell 115 3 2003 333 342
    • (2003) Cell , vol.115 , Issue.3 , pp. 333-342
    • Kubori, T.1    Galan, J.E.2
  • 33
    • 0031801744 scopus 로고    scopus 로고
    • Identification of a specific chaperone for SptP, a substrate of the centisome 63 type III secretion system of Salmonella typhimurium
    • Y. Fu, and J.E. Galan Identification of a specific chaperone for SptP, a substrate of the centisome 63 type III secretion system of Salmonella typhimurium J. Bacteriol. 180 13 1998 3393 3399
    • (1998) J. Bacteriol. , vol.180 , Issue.13 , pp. 3393-3399
    • Fu, Y.1    Galan, J.E.2
  • 34
    • 0034502457 scopus 로고    scopus 로고
    • Modulation of host signaling by a bacterial mimic: Structure of the Salmonella effector SptP bound to Rac1
    • C.E. Stebbins, and J.E. Galan Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1 Mol. Cell 6 6 2000 1449 1460
    • (2000) Mol. Cell , vol.6 , Issue.6 , pp. 1449-1460
    • Stebbins, C.E.1    Galan, J.E.2
  • 35
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • C.E. Stebbins, and J.E. Galan Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion Nature 414 6859 2001 77 81
    • (2001) Nature , vol.414 , Issue.6859 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 36
    • 0042338640 scopus 로고    scopus 로고
    • Priming virulence factors for delivery into the host
    • C.E. Stebbins, and J.E. Galan Priming virulence factors for delivery into the host Nat. Rev. Mol. Cell Biol. 4 9 2003 738 743
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.9 , pp. 738-743
    • Stebbins, C.E.1    Galan, J.E.2
  • 37
    • 0035899360 scopus 로고    scopus 로고
    • Structural mimicry in bacterial virulence
    • C.E. Stebbins, and J.E. Galan Structural mimicry in bacterial virulence Nature 412 6848 2001 701 705
    • (2001) Nature , vol.412 , Issue.6848 , pp. 701-705
    • Stebbins, C.E.1    Galan, J.E.2
  • 38
    • 0033605618 scopus 로고    scopus 로고
    • Role of the Salmonella typhimurium actin-binding protein SipA in bacterial internalization
    • D. Zhou, M.S. Mooseker, and J.E. Galan Role of the Salmonella typhimurium actin-binding protein SipA in bacterial internalization Science 283 5410 1999 2092 2095
    • (1999) Science , vol.283 , Issue.5410 , pp. 2092-2095
    • Zhou, D.1    Mooseker, M.S.2    Galan, J.E.3
  • 39
    • 0035341210 scopus 로고    scopus 로고
    • Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin
    • E.J. McGhie, R.D. Hayward, and V. Koronakis Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin EMBO J. 20 9 2001 2131 2139
    • (2001) EMBO J. , vol.20 , Issue.9 , pp. 2131-2139
    • McGhie, E.J.1    Hayward, R.D.2    Koronakis, V.3
  • 40
    • 1542315318 scopus 로고    scopus 로고
    • Control of actin turnover by a Salmonella invasion protein
    • E.J. McGhie, R.D. Hayward, and V. Koronakis Control of actin turnover by a Salmonella invasion protein Mol. Cell 13 4 2004 497 510
    • (2004) Mol. Cell , vol.13 , Issue.4 , pp. 497-510
    • McGhie, E.J.1    Hayward, R.D.2    Koronakis, V.3
  • 41
    • 0035064654 scopus 로고    scopus 로고
    • The Salmonella SpvB virulence gene encodes an enzyme that ADP-ribosylates actin and destabilizes the cytoskeleton of eukaryotic cells
    • M.L. Lesnick, N.E. Reiner, J. Fierer, and D.G. Guiney The Salmonella SpvB virulence gene encodes an enzyme that ADP-ribosylates actin and destabilizes the cytoskeleton of eukaryotic cells Mol. Microbiol. 39 6 2001 1464 1470
    • (2001) Mol. Microbiol. , vol.39 , Issue.6 , pp. 1464-1470
    • Lesnick, M.L.1    Reiner, N.E.2    Fierer, J.3    Guiney, D.G.4
  • 42
    • 0035131629 scopus 로고    scopus 로고
    • Actin is ADP-ribosylated by the Salmonella enterica virulence-associated protein SpvB
    • D. Tezcan-Merdol, T. Nyman, U. Lindberg, F. Haag, F. Koch-Nolte, and M. Rhen Actin is ADP-ribosylated by the Salmonella enterica virulence-associated protein SpvB Mol. Microbiol. 39 3 2001 606 619
    • (2001) Mol. Microbiol. , vol.39 , Issue.3 , pp. 606-619
    • Tezcan-Merdol, D.1    Nyman, T.2    Lindberg, U.3    Haag, F.4    Koch-Nolte, F.5    Rhen, M.6
  • 43
    • 0033817265 scopus 로고    scopus 로고
    • The Salmonella type III secretion translocon protein SspC is inserted into the epithelial cell plasma membrane upon infection
    • C.A. Scherer, E. Cooper, and S.I. Miller The Salmonella type III secretion translocon protein SspC is inserted into the epithelial cell plasma membrane upon infection Mol. Microbiol. 37 5 2000 1133 1145
    • (2000) Mol. Microbiol. , vol.37 , Issue.5 , pp. 1133-1145
    • Scherer, C.A.1    Cooper, E.2    Miller, S.I.3
  • 44
    • 0030921542 scopus 로고    scopus 로고
    • A secreted effector protein of Salmonella dublin is translocated into eukaryotic cells and mediates inflammation and fluid secretion in infected ileal mucosa
    • E.E. Galyov, M.W. Wood, R. Rosqvist, P.B. Mullan, P.R. Watson, and S. Hedges A secreted effector protein of Salmonella dublin is translocated into eukaryotic cells and mediates inflammation and fluid secretion in infected ileal mucosa Mol. Microbiol. 25 5 1997 903 912
    • (1997) Mol. Microbiol. , vol.25 , Issue.5 , pp. 903-912
    • Galyov, E.E.1    Wood, M.W.2    Rosqvist, R.3    Mullan, P.B.4    Watson, P.R.5    Hedges, S.6
  • 45
    • 0029806327 scopus 로고    scopus 로고
    • SopE, a secreted protein of Salmonella dublin, is translocated into the target eukaryotic cell via a sip-dependent mechanism and promotes bacterial entry
    • M.W. Wood, R. Rosqvist, P.B. Mullan, M.H. Edwards, and E.E. Galyov SopE, a secreted protein of Salmonella dublin, is translocated into the target eukaryotic cell via a sip-dependent mechanism and promotes bacterial entry Mol. Microbiol. 22 2 1996 327 338
    • (1996) Mol. Microbiol. , vol.22 , Issue.2 , pp. 327-338
    • Wood, M.W.1    Rosqvist, R.2    Mullan, P.B.3    Edwards, M.H.4    Galyov, E.E.5
  • 46
    • 0033567985 scopus 로고    scopus 로고
    • Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella
    • R.D. Hayward, and V. Koronakis Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella EMBO J. 18 18 1999 4926 4934
    • (1999) EMBO J. , vol.18 , Issue.18 , pp. 4926-4934
    • Hayward, R.D.1    Koronakis, V.2
  • 47
    • 0034949261 scopus 로고    scopus 로고
    • Role of SipA in the early stages of Salmonella typhimurium entry into epithelial cells
    • M.A. Jepson, B. Kenny, and A.D. Leard Role of SipA in the early stages of Salmonella typhimurium entry into epithelial cells Cell. Microbiol. 3 6 2001 417 426
    • (2001) Cell. Microbiol. , vol.3 , Issue.6 , pp. 417-426
    • Jepson, M.A.1    Kenny, B.2    Leard, A.D.3
  • 48
    • 0036307043 scopus 로고    scopus 로고
    • Involvement of SipA in modulating actin dynamics during Salmonella invasion into cultured epithelial cells
    • W. Higashide, S. Dai, V.P. Hombs, and D. Zhou Involvement of SipA in modulating actin dynamics during Salmonella invasion into cultured epithelial cells Cell. Microbiol. 4 6 2002 357 365
    • (2002) Cell. Microbiol. , vol.4 , Issue.6 , pp. 357-365
    • Higashide, W.1    Dai, S.2    Hombs, V.P.3    Zhou, D.4
  • 50
    • 0033621058 scopus 로고    scopus 로고
    • An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
    • D. Zhou, M.S. Mooseker, and J.E. Galan An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin Proc. Natl. Acad. Sci. USA 96 18 1999 10176 10181
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.18 , pp. 10176-10181
    • Zhou, D.1    Mooseker, M.S.2    Galan, J.E.3
  • 51
    • 1842829164 scopus 로고    scopus 로고
    • Efficient Salmonella entry requires activity cycles of host ADF and cofilin
    • S. Dai, P.D. Sarmiere, O. Wiggan, J.R. Bamburg, and D. Zhou Efficient Salmonella entry requires activity cycles of host ADF and cofilin Cell. Microbiol. 6 5 2004 459 471
    • (2004) Cell. Microbiol. , vol.6 , Issue.5 , pp. 459-471
    • Dai, S.1    Sarmiere, P.D.2    Wiggan, O.3    Bamburg, J.R.4    Zhou, D.5
  • 52
    • 0141868915 scopus 로고    scopus 로고
    • Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms
    • M. Lilic, V.E. Galkin, A. Orlova, M.S. VanLoock, E.H. Egelman, and C.E. Stebbins Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms Science 301 5641 2003 1918 1921
    • (2003) Science , vol.301 , Issue.5641 , pp. 1918-1921
    • Lilic, M.1    Galkin, V.E.2    Orlova, A.3    Vanloock, M.S.4    Egelman, E.H.5    Stebbins, C.E.6
  • 53
    • 0034730896 scopus 로고    scopus 로고
    • Biophysical characterization of SipA, an actin-binding protein from Salmonella enterica
    • K. Mitra, D. Zhou, and J.E. Galan Biophysical characterization of SipA, an actin-binding protein from Salmonella enterica FEBS Lett. 482 1-2 2000 81 84
    • (2000) FEBS Lett. , vol.482 , Issue.120-132 , pp. 81-84
    • Mitra, K.1    Zhou, D.2    Galan, J.E.3
  • 54
    • 0343517154 scopus 로고    scopus 로고
    • Salmonella maintains the integrity of its intracellular vacuole through the action of SifA
    • C.R. Beuzon, S. Meresse, K.E. Unsworth, J. Ruiz-Albert, S. Garvis, and S.R. Waterman Salmonella maintains the integrity of its intracellular vacuole through the action of SifA EMBO J. 19 13 2000 3235 3249
    • (2000) EMBO J. , vol.19 , Issue.13 , pp. 3235-3249
    • Beuzon, C.R.1    Meresse, S.2    Unsworth, K.E.3    Ruiz-Albert, J.4    Garvis, S.5    Waterman, S.R.6
  • 55
    • 0027375512 scopus 로고
    • Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells
    • F. Garcia-del Portillo, M.B. Zwick, K.Y. Leung, and B.B. Finlay Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells Proc. Natl. Acad. Sci. USA 90 22 1993 10544 10548
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.22 , pp. 10544-10548
    • Garcia-Del Portillo, F.1    Zwick, M.B.2    Leung, K.Y.3    Finlay, B.B.4
  • 56
    • 0036300862 scopus 로고    scopus 로고
    • SifA, a type III secreted effector of Salmonella typhimurium, directs Salmonella-induced filament (Sif) formation along microtubules
    • J.H. Brumell, D.L. Goosney, and B.B. Finlay SifA, a type III secreted effector of Salmonella typhimurium, directs Salmonella-induced filament (Sif) formation along microtubules Traffic 3 6 2002 407 415
    • (2002) Traffic , vol.3 , Issue.6 , pp. 407-415
    • Brumell, J.H.1    Goosney, D.L.2    Finlay, B.B.3
  • 57
    • 0037218484 scopus 로고    scopus 로고
    • The Salmonella enterica serovar typhimurium translocated effectors SseJ and SifB are targeted to the Salmonella-containing vacuole
    • J.A. Freeman, M.E. Ohl, and S.I. Miller The Salmonella enterica serovar typhimurium translocated effectors SseJ and SifB are targeted to the Salmonella-containing vacuole Infect. Immun. 71 1 2003 418 427
    • (2003) Infect. Immun. , vol.71 , Issue.1 , pp. 418-427
    • Freeman, J.A.1    Ohl, M.E.2    Miller, S.I.3
  • 58
    • 0037772375 scopus 로고    scopus 로고
    • Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton
    • E.A. Miao, M. Brittnacher, A. Haraga, R.L. Jeng, M.D. Welch, and S.I. Miller Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton Mol. Microbiol. 48 2 2003 401 415
    • (2003) Mol. Microbiol. , vol.48 , Issue.2 , pp. 401-415
    • Miao, E.A.1    Brittnacher, M.2    Haraga, A.3    Jeng, R.L.4    Welch, M.D.5    Miller, S.I.6
  • 59
    • 1842584706 scopus 로고    scopus 로고
    • Microtubule motors control membrane dynamics of Salmonella-containing vacuoles
    • J. Guignot, E. Caron, C. Beuzon, C. Bucci, J. Kagan, and C. Roy Microtubule motors control membrane dynamics of Salmonella-containing vacuoles J. Cell Sci. 117 Pt 7 2004 1033 1045
    • (2004) J. Cell Sci. , vol.117 , Issue.7 , pp. 1033-1045
    • Guignot, J.1    Caron, E.2    Beuzon, C.3    Bucci, C.4    Kagan, J.5    Roy, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.