메뉴 건너뛰기




Volumn 46, Issue 4, 2002, Pages 1183-1197

SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; HYBRID PROTEIN; SYC PROTEIN; UNCLASSIFIED DRUG;

EID: 0036436338     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.03241.x     Document Type: Article
Times cited : (75)

References (52)
  • 1
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D.M., and Schneewind, O. (1997) A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 278: 1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 2
    • 0034753703 scopus 로고    scopus 로고
    • Structure of the Yersinia type III secretory system chaperone SycE
    • Birtalan, S., and Ghosh, P. (2001) Structure of the Yersinia type III secretory system chaperone SycE. Nature Struct Biol 8: 974-978.
    • (2001) Nature Struct Biol , vol.8 , pp. 974-978
    • Birtalan, S.1    Ghosh, P.2
  • 3
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S.C., Phillips, R.M., and Ghosh, P. (2002) Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell 9: 971-980.
    • (2002) Mol Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 4
    • 0035133489 scopus 로고    scopus 로고
    • Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton
    • Blocker, A., Jouihri, N., Larquet, E., Gounon, P., Ebel, F., Parsot, C., et al. (2001) Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton. Mol Microbiol 39: 652-663.
    • (2001) Mol Microbiol , vol.39 , pp. 652-663
    • Blocker, A.1    Jouihri, N.2    Larquet, E.3    Gounon, P.4    Ebel, F.5    Parsot, C.6
  • 5
    • 0033872740 scopus 로고    scopus 로고
    • Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE
    • Boyd, A.P., Lambermont, I., and Cornelis, G.R. (2000a) Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE. J Bacteriol 182: 4811-4821.
    • (2000) J Bacteriol , vol.182 , pp. 4811-4821
    • Boyd, A.P.1    Lambermont, I.2    Cornelis, G.R.3
  • 6
    • 0033754201 scopus 로고    scopus 로고
    • Yersinia enterocolitica can deliver Yop proteins into a wide range of cell types: Development of a delivery system for heterologous proteins
    • Boyd, A.P., Grosdent, N., Totemeyer, S., Geuijen, C., Bleves, S., Iriarte, M., et al. (2000b) Yersinia enterocolitica can deliver Yop proteins into a wide range of cell types: Development of a delivery system for heterologous proteins. Eur J Cell Biol 79: 659-671.
    • (2000) Eur J Cell Biol , vol.79 , pp. 659-671
    • Boyd, A.P.1    Grosdent, N.2    Totemeyer, S.3    Geuijen, C.4    Bleves, S.5    Iriarte, M.6
  • 7
    • 0033618257 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells
    • Cheng, L.W., and Schneewind, O. (1999) Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells. J Biol Chem 274: 22102-22108.
    • (1999) J Biol Chem , vol.274 , pp. 22102-22108
    • Cheng, L.W.1    Schneewind, O.2
  • 8
    • 0033613814 scopus 로고    scopus 로고
    • Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures
    • Clark, A.C., and Frieden, C. (1999) Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures. J Mol Biol 285: 1765-1776.
    • (1999) J Mol Biol , vol.285 , pp. 1765-1776
    • Clark, A.C.1    Frieden, C.2
  • 9
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis, G.R., and Van Gijsegem, F. (2000) Assembly and function of type III secretory systems. Annu Rev Microbiol 54: 735-774.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 10
    • 0023255341 scopus 로고
    • Transcription of the yop regulon from Y. enterocolitica requires trans acting pYV and chromosomal genes
    • Cornelis, G., Vanootegem, J.C., and Sluiters, C. (1987) Transcription of the yop regulon from Y. enterocolitica requires trans acting pYV and chromosomal genes. Microb Pathog 2: 367-379.
    • (1987) Microb Pathog , vol.2 , pp. 367-379
    • Cornelis, G.1    Vanootegem, J.C.2    Sluiters, C.3
  • 11
    • 0035901560 scopus 로고    scopus 로고
    • Type III secretion chaperone-dependent regulation: Activation of virulence genes by SicA and InvF in Salmonella typhimurium
    • Darwin, K.H., and Miller, V.L. (2001) Type III secretion chaperone-dependent regulation: Activation of virulence genes by SicA and InvF in Salmonella typhimurium. EMBO J 20: 1850-1862.
    • (2001) EMBO J , vol.20 , pp. 1850-1862
    • Darwin, K.H.1    Miller, V.L.2
  • 12
    • 0035339953 scopus 로고    scopus 로고
    • SecB, a molecular chaperone with two faces
    • Driessen, A.J. (2001) SecB, a molecular chaperone with two faces. Trends Microbiol 9: 193-196.
    • (2001) Trends Microbiol , vol.9 , pp. 193-196
    • Driessen, A.J.1
  • 13
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers, M., and Schatz, G. (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochon-dria. Nature 322: 228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 14
    • 0036149447 scopus 로고    scopus 로고
    • Crystal structure of the Yersinia pestis GTPase activator YopE
    • Evdokimov, A.G., Tropea, J.E., Routzahn, K.M., and Waugh, D.S. (2002) Crystal structure of the Yersinia pestis GTPase activator YopE. Protein Sci 11: 401-408.
    • (2002) Protein Sci , vol.11 , pp. 401-408
    • Evdokimov, A.G.1    Tropea, J.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 15
    • 0029070827 scopus 로고
    • The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensable for targeting to the secretion loci
    • Frithz-Lindsten, E., Rosqvist, R., Johansson, L., and Forsberg, A. (1995) The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensable for targeting to the secretion loci. Mol Microbiol 16: 635-647.
    • (1995) Mol Microbiol , vol.16 , pp. 635-647
    • Frithz-Lindsten, E.1    Rosqvist, R.2    Johansson, L.3    Forsberg, A.4
  • 16
    • 0029908022 scopus 로고    scopus 로고
    • The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-dependent membrane disrupting activity
    • Hakansson, S., Schesser, K., Persson, C., Galyov, E.E., Rosqvist, R., Homble, F., and Wolf-Watz, H. (1996) The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-dependent membrane disrupting activity. EMBO J 15: 5812-5823.
    • (1996) EMBO J , vol.15 , pp. 5812-5823
    • Hakansson, S.1    Schesser, K.2    Persson, C.3    Galyov, E.E.4    Rosqvist, R.5    Homble, F.6    Wolf-Watz, H.7
  • 17
    • 0022991437 scopus 로고
    • Restriction enzyme map of cryptic plasmid accompanying pR711b and pR409; identity of pR409 and pR388
    • Heidorn, J.V., and Valentine, C.R. (1986) Restriction enzyme map of cryptic plasmid accompanying pR711b and pR409; identity of pR409 and pR388. J Basic Microbiol 26: 621-625.
    • (1986) J Basic Microbiol , vol.26 , pp. 621-625
    • Heidorn, J.V.1    Valentine, C.R.2
  • 18
    • 0035836714 scopus 로고    scopus 로고
    • Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
    • Hoiczyk, E., and Blobel, G. (2001) Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells. Proc Natl Acad Sci USA 98: 4669-4674.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4669-4674
    • Hoiczyk, E.1    Blobel, G.2
  • 19
    • 0032567332 scopus 로고    scopus 로고
    • The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
    • Hynds, P.J., Robinson, D., and Robinson, C. (1998) The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J Biol Chem 273: 34868-34874.
    • (1998) J Biol Chem , vol.273 , pp. 34868-34874
    • Hynds, P.J.1    Robinson, D.2    Robinson, C.3
  • 20
    • 0031880899 scopus 로고    scopus 로고
    • YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells
    • Iriarte, M., and Cornelis, G.R. (1998) YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells. Mol Microbiol 29: 915-929.
    • (1998) Mol Microbiol , vol.29 , pp. 915-929
    • Iriarte, M.1    Cornelis, G.R.2
  • 21
    • 0033743958 scopus 로고    scopus 로고
    • Resistance to methotrexate due to AcrAB-dependent export from Escherichia coli
    • Kopytek, S.J., Dyer, J.C., Knapp, G.S., and Hu, J.C. (2000) Resistance to methotrexate due to AcrAB-dependent export from Escherichia coli. Antimicrob Agents Chemother 44: 3210-3212.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 3210-3212
    • Kopytek, S.J.1    Dyer, J.C.2    Knapp, G.S.3    Hu, J.C.4
  • 22
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M.E., Elzer, P.H., Hill, D.S., Robertson, G.T., Farris, M.A., Roop, R.M., II, and Peterson, K.M. (1995) Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166: 175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop R.M. II6    Peterson, K.M.7
  • 23
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • Kubori, T., Matsushima, Y., Nakamura, D., Uralil, J., Lara-Tejero, M., Sukhan, A., et al. (1998) Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280: 602-605.
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3    Uralil, J.4    Lara-Tejero, M.5    Sukhan, A.6
  • 24
    • 0036283447 scopus 로고    scopus 로고
    • Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion
    • Lee, V.T., and Schneewind, O. (2002) Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion. J Bacteriol 184: 3740-3745.
    • (2002) J Bacteriol , vol.184 , pp. 3740-3745
    • Lee, V.T.1    Schneewind, O.2
  • 25
    • 0001087151 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the type III secretion chaperones CesT and SigE
    • Luo, Y., Bertero, M.G., Frey, E.A., Pfuetzner, R.A., Wenk, M.R., Creagh, L., et al. (2001) Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nature Struct Biol 29: 29.
    • (2001) Nature Struct Biol , vol.29 , pp. 29
    • Luo, Y.1    Bertero, M.G.2    Frey, E.A.3    Pfuetzner, R.A.4    Wenk, M.R.5    Creagh, L.6
  • 26
    • 0028113512 scopus 로고
    • Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri
    • Menard, R., Sansonetti, P., Parsot, C., and Vasselon, T. (1994) Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri. Cell 79: 515-525.
    • (1994) Cell , vol.79 , pp. 515-525
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3    Vasselon, T.4
  • 27
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels, T., and Cornelis, G.R. (1991) Secretion of hybrid proteins by the Yersinia Yop export system. J Bacteriol 173: 1677-1685.
    • (1991) J Bacteriol , vol.173 , pp. 1677-1685
    • Michiels, T.1    Cornelis, G.R.2
  • 28
    • 0028800949 scopus 로고
    • A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site
    • Narayana, N., Matthews, D.A., Howell, E.E., and Nguyen-huu, X. (1995) A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site. Nature Struct Biol 2: 1018-1025.
    • (1995) Nature Struct Biol , vol.2 , pp. 1018-1025
    • Narayana, N.1    Matthews, D.A.2    Howell, E.E.3    Nguyen-huu, X.4
  • 29
    • 0032835828 scopus 로고    scopus 로고
    • Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: Requirement for translocators YopB and YopD, but not LcrG
    • Neyt, C., and Cornelis, G.R. (1999) Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: Requirement for translocators YopB and YopD, but not LcrG. Mol Microbiol 33: 971-981.
    • (1999) Mol Microbiol , vol.33 , pp. 971-981
    • Neyt, C.1    Cornelis, G.R.2
  • 30
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner, C., D'Arcy, A., and Winkler, F.K. (1988) Crystal structure of human dihydrofolate reductase complexed with folate. Eur J Biochem 174: 377-385.
    • (1988) Eur J Biochem , vol.174 , pp. 377-385
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3
  • 31
    • 0036267949 scopus 로고    scopus 로고
    • Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway
    • Page, A.L., Sansonetti, P., and Parsot, C. (2002) Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway. Mol Microbiol 43: 1533-1542.
    • (2002) Mol Microbiol , vol.43 , pp. 1533-1542
    • Page, A.L.1    Sansonetti, P.2    Parsot, C.3
  • 32
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N., and Geissler, A. (2001) Versatility of the mitochondrial protein import machinery. Nature Rev Mol Cell Biol 2: 339-349.
    • (2001) Nature Rev Mol Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 33
    • 0027085709 scopus 로고
    • Translocation of a folded protein across the outer membrane in Escherichia coli
    • Pugsley, A.P. (1992) Translocation of a folded protein across the outer membrane in Escherichia coli. Proc Natl Acad Sci USA 89: 12058-12062.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12058-12062
    • Pugsley, A.P.1
  • 34
    • 0034282931 scopus 로고    scopus 로고
    • Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • Salvador, N., Aguado, C., Horst, M., and Knecht, E. (2000) Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 275: 27447-27456.
    • (2000) J Biol Chem , vol.275 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 36
    • 0030474296 scopus 로고    scopus 로고
    • Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes
    • Schesser, K., Frithz-Lindsten, E., and Wolf-Watz, H. (1996) Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes. J Bacteriol 178: 7227-7233.
    • (1996) J Bacteriol , vol.178 , pp. 7227-7233
    • Schesser, K.1    Frithz-Lindsten, E.2    Wolf-Watz, H.3
  • 37
    • 0025006519 scopus 로고
    • A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes
    • Schlenstedt, G., Gudmundsson, G.H., Boman, H.G., and Zimmermann, R. (1990) A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes. J Biol Chem 265: 13960-13968.
    • (1990) J Biol Chem , vol.265 , pp. 13960-13968
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 38
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M.P., and Cornelis, G.R. (1994) Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol Microbiol 14: 583-594.
    • (1994) Mol Microbiol , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 39
    • 0029608720 scopus 로고
    • Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach
    • Sory, M.P., Boland, A., Lambermont, I., and Cornelis, G.R. (1995) Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc Natl Acad Sci USA 92: 11998-12002.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11998-12002
    • Sory, M.P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 40
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C.E., and Galan, J.E. (2001) Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414: 77-81.
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 41
    • 0021767942 scopus 로고
    • A novel in vitro transcription-translation system: Accurate and efficient synthesis of single proteins from cloned DNA sequences
    • Stueber, D., Ibrahimi, I., Cutler, D., Dobberstein, B., and Bujard, H. (1984) A novel in vitro transcription-translation system: Accurate and efficient synthesis of single proteins from cloned DNA sequences. EMBO J 3: 3143-3148.
    • (1984) EMBO J , vol.3 , pp. 3143-3148
    • Stueber, D.1    Ibrahimi, I.2    Cutler, D.3    Dobberstein, B.4    Bujard, H.5
  • 43
    • 0034079727 scopus 로고    scopus 로고
    • Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone
    • Tucker, S.C., and Galan, J.E. (2000) Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone. J Bacteriol 182: 2262-2268.
    • (2000) J Bacteriol , vol.182 , pp. 2262-2268
    • Tucker, S.C.1    Galan, J.E.2
  • 44
    • 0023987428 scopus 로고
    • Point mutations destabilizing a precursor protein enhance its post- translational import into mitochondria
    • Vestweber, D., and Schatz, G. (1988) Point mutations destabilizing a precursor protein enhance its post- translational import into mitochondria. EMBO J 7: 1147-1151.
    • (1988) EMBO J , vol.7 , pp. 1147-1151
    • Vestweber, D.1    Schatz, G.2
  • 45
    • 0029010680 scopus 로고
    • Import of stably folded proteins into peroxisomes
    • Walton, P.A., Hill, P.E., and Subramani, S. (1995) Import of stably folded proteins into peroxisomes. Mol Biol Cell 6: 675-683.
    • (1995) Mol Biol Cell , vol.6 , pp. 675-683
    • Walton, P.A.1    Hill, P.E.2    Subramani, S.3
  • 46
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in Ohe secretion of YopE
    • Wattiau, P., and Cornelis, G.R. (1993) SycE, a chaperone-like protein of Yersinia enterocolitica involved in Ohe secretion of YopE. Mol Microbiol 8: 123-131.
    • (1993) Mol Microbiol , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 48
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic bacteria
    • Wattiau, P., Woestyn, S., and Cornelis, G.R. (1996) Customized secretion chaperones in pathogenic bacteria. Mol Microbiol 20: 255-262.
    • (1996) Mol Microbiol , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 49
    • 0026338164 scopus 로고
    • Protein folding causes an arrest of preprotein translocation into mitochondria in vivo
    • Wienhues, U., Becker, K., Schleyer, M., Guiard, B., Tropschug, M., Horwich, A.L., et al. (1991) Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. J Cell Biol 115: 1601-1609.
    • (1991) J Cell Biol , vol.115 , pp. 1601-1609
    • Wienhues, U.1    Becker, K.2    Schleyer, M.3    Guiard, B.4    Tropschug, M.5    Horwich, A.L.6
  • 50
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., Allaoui, A., Wattiau, P., and Cornelis, G.R. (1994) YscN, the putative energizer of the Yersinia Yop secretion machinery. J Bacteriol 176: 1561-1569.
    • (1994) J Bacteriol , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 51
    • 0029944323 scopus 로고    scopus 로고
    • The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes
    • Woestyn, S., Sory, M.P., Boland, A., Lequenne, O., and Cornelis, G.R. (1996) The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes. Mol Microbiol 20: 1261-1271.
    • (1996) Mol Microbiol , vol.20 , pp. 1261-1271
    • Woestyn, S.1    Sory, M.P.2    Boland, A.3    Lequenne, O.4    Cornelis, G.R.5
  • 52
    • 0036170459 scopus 로고    scopus 로고
    • LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion
    • Wulff-Strobel, C.R., Williams, A.W., and Straley, S.C. (2002) LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion. Mol Microbiol 43: 411-423.
    • (2002) Mol Microbiol , vol.43 , pp. 411-423
    • Wulff-Strobel, C.R.1    Williams, A.W.2    Straley, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.