메뉴 건너뛰기




Volumn 188, Issue 10, 2006, Pages 3525-3534

Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CHAPERONE; GLUTATHIONE TRANSFERASE; YERSINIA OUTER PROTEIN E;

EID: 33646543996     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.10.3525-3534.2006     Document Type: Article
Times cited : (74)

References (55)
  • 1
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda, Y., and J. E. Galan. 2005. Chaperone release and unfolding of substrates in type III secretion. Nature 437:911-915.
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 2
    • 1842506700 scopus 로고    scopus 로고
    • Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains
    • Akeda, Y., and J. E. Galan. 2004. Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains. J. Bacteriol. 186:2402-2412.
    • (2004) J. Bacteriol. , vol.186 , pp. 2402-2412
    • Akeda, Y.1    Galan, J.E.2
  • 3
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D. M., and O. Schneewind. 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
  • 4
    • 0033003131 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: An mRNA signal that couples translation and secretion of YopQ
    • Anderson, D. M., and O. Schneewind. 1999. Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ. Mol. Microbiol. 31:1139-1148.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1139-1148
    • Anderson, D.M.1    Schneewind, O.2
  • 5
    • 0037053426 scopus 로고    scopus 로고
    • Intrinsic membrane targeting of the flagellar export ATPase FliI: Interaction with acidic phospholipids and FliH
    • Auvray, F., A. J. Ozin, L. Claret, and C. Hughes. 2002. Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH. J. Mol. Biol. 318:941-950.
    • (2002) J. Mol. Biol. , vol.318 , pp. 941-950
    • Auvray, F.1    Ozin, A.J.2    Claret, L.3    Hughes, C.4
  • 6
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S. C., R. M. Phillips, and P. Ghosh. 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
  • 7
    • 0033861270 scopus 로고    scopus 로고
    • The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence
    • Black, D. S., and J. B. Bliska. 2000. The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence. Mol. Microbiol. 37:515-527.
    • (2000) Mol. Microbiol. , vol.37 , pp. 515-527
    • Black, D.S.1    Bliska, J.B.2
  • 8
    • 0030967331 scopus 로고    scopus 로고
    • Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica
    • Cheng, L. W., D. M. Anderson, and O. Schneewind. 1997. Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica. Mol. Microbiol. 24:757-765.
    • (1997) Mol. Microbiol. , vol.24 , pp. 757-765
    • Cheng, L.W.1    Anderson, D.M.2    Schneewind, O.3
  • 9
    • 0034864508 scopus 로고    scopus 로고
    • Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica
    • Cheng, L. W., O. Kay, and O. Schneewind. 2001. Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica. J. Bacteriol. 183:5293-5301.
    • (2001) J. Bacteriol. , vol.183 , pp. 5293-5301
    • Cheng, L.W.1    Kay, O.2    Schneewind, O.3
  • 10
    • 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 O. Schneewind. 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
  • 11
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret, L., S. R. Calder, M. Higgins, and C. Hughes. 2003. Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol. Microbiol. 48:1349-1355.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 12
    • 0016637595 scopus 로고
    • Restriction of DNA in Yersinia enterocolitica detected by recipient ability for a derepressed R factor from Escherichia coli
    • Cornelis, G., and C. Colson. 1975. Restriction of DNA in Yersinia enterocolitica detected by recipient ability for a derepressed R factor from Escherichia coli. J. Gen. Microbiol. 87:285-291.
    • (1975) J. Gen. Microbiol. , vol.87 , pp. 285-291
    • Cornelis, G.1    Colson, C.2
  • 13
    • 0345257863 scopus 로고    scopus 로고
    • How Yop proteins find their way out of Yersinia
    • Cornelis, G. R. 2003. How Yop proteins find their way out of Yersinia. Mol. Microbiol. 50:1091-1094.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1091-1094
    • Cornelis, G.R.1
  • 15
    • 0029730706 scopus 로고    scopus 로고
    • Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium
    • Fan, F., and R. M. Macnab. 1996. Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. J. Biol. Chem. 271:31981-331988.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31981-331988
    • Fan, F.1    Macnab, R.M.2
  • 16
    • 23744437504 scopus 로고    scopus 로고
    • Selection and characterization of Yersinia pestis YopN mutants that constitutively block Yop secretion
    • Ferracci, F., F. D. Schubot, D. S. Waugh, and G. V. Plano. 2005. Selection and characterization of Yersinia pestis YopN mutants that constitutively block Yop secretion. Mol. Microbiol. 57:970-987.
    • (2005) Mol. Microbiol. , vol.57 , pp. 970-987
    • Ferracci, F.1    Schubot, F.D.2    Waugh, D.S.3    Plano, G.V.4
  • 17
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galan, J. E., and A. Collmer. 1999. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284:1322-1333.
    • (1999) Science , vol.284 , pp. 1322-1333
    • Galan, J.E.1    Collmer, A.2
  • 18
    • 0344825097 scopus 로고    scopus 로고
    • Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli
    • Gauthier, A., and B. B. Finlay. 2003. Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli. J. Bacteriol. 185:6747-6755.
    • (2003) J. Bacteriol. , vol.185 , pp. 6747-6755
    • Gauthier, A.1    Finlay, B.B.2
  • 19
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • Gonzalez-Pedrajo, B., G. M. Fraser, T. Minamino, and R. M. Macnab. 2002. Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol. Microbiol. 45:967-982.
    • (2002) Mol. Microbiol. , vol.45 , pp. 967-982
    • Gonzalez-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    Macnab, R.M.4
  • 20
    • 0035836714 scopus 로고    scopus 로고
    • Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
    • Hoiczyk, E., and G. Blobel. 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
  • 21
    • 0034193707 scopus 로고    scopus 로고
    • Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system
    • Jackson, M. W., and G. V. Plano. 2000. Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system. FEMS Microbiol. Lett. 186:85-90.
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 85-90
    • Jackson, M.W.1    Plano, G.V.2
  • 22
    • 0041663990 scopus 로고    scopus 로고
    • MxiK and MxiN interact with the Spa47 ATPase and are required for transit of the needle components MxiH and MxiI, but not of Ipa proteins, through the type III secretion apparatus of Shigella flexneri
    • Jouihri, N., M. P. Sory, A. L. Page, P. Gounon, C. Parsot, and A. Allaoui. 2003. MxiK and MxiN interact with the Spa47 ATPase and are required for transit of the needle components MxiH and MxiI, but not of Ipa proteins, through the type III secretion apparatus of Shigella flexneri. Mol. Microbiol. 49:755-767.
    • (2003) Mol. Microbiol. , vol.49 , pp. 755-767
    • Jouihri, N.1    Sory, M.P.2    Page, A.L.3    Gounon, P.4    Parsot, C.5    Allaoui, A.6
  • 23
  • 24
    • 0031970595 scopus 로고    scopus 로고
    • Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: One-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone
    • Lee, V. T., D. M. Anderson, and O. Schneewind. 1998. Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone. Mol. Microbiol. 28:593-601.
    • (1998) Mol. Microbiol. , vol.28 , pp. 593-601
    • Lee, V.T.1    Anderson, D.M.2    Schneewind, O.3
  • 25
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • Lloyd, S. A., M. Norman, R. Rosqvist, and H. Wolf-Watz. 2001. Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol. Microbiol. 39:520-531.
    • (2001) Mol. Microbiol. , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 26
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • Marlovits, T. C., T. Kubori, A. Sukhan, D. R. Thomas, J. E. Galan, and V. M. Unger. 2004. Structural insights into the assembly of the type III secretion needle complex. Science 306:1040-1042.
    • (2004) Science , vol.306 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    Sukhan, A.3    Thomas, D.R.4    Galan, J.E.5    Unger, V.M.6
  • 27
    • 0037133213 scopus 로고    scopus 로고
    • An iron-regulated sortase enzyme anchors a class of surface protein during Staphylococcus aureus pathogenesis
    • Mazmanian, S. K., H. Ton-That, K. Su, and O. Schneewind. 2002. An iron-regulated sortase enzyme anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc. Natl. Acad. Sci. USA 99:2293-2298.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2293-2298
    • Mazmanian, S.K.1    Ton-That, H.2    Su, K.3    Schneewind, O.4
  • 28
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels, T., and G. R. Cornelis. 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
  • 30
    • 0037701404 scopus 로고    scopus 로고
    • The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH
    • Minamino, T., B. Gonzalez-Pedrajo, M. Kihara, K. Namba, and R. M. Macnab. 2003. The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. J. Bacteriol. 185:3983-3988.
    • (2003) J. Bacteriol. , vol.185 , pp. 3983-3988
    • Minamino, T.1    Gonzalez-Pedrajo, B.2    Kihara, M.3    Namba, K.4    Macnab, R.M.5
  • 31
    • 0036384413 scopus 로고    scopus 로고
    • Structural properties of FliH. an ATPase regulatory component of the Salmonella type III flagellar export apparatus
    • Minamino, T., B. Gonzalez-Pedrajo, K. Oosawa, K. Namba, and R. M. Macnab. 2002. Structural properties of FliH. an ATPase regulatory component of the Salmonella type III flagellar export apparatus. J. Mol. Biol. 322:281-290.
    • (2002) J. Mol. Biol. , vol.322 , pp. 281-290
    • Minamino, T.1    Gonzalez-Pedrajo, B.2    Oosawa, K.3    Namba, K.4    Macnab, R.M.5
  • 32
    • 0033779545 scopus 로고    scopus 로고
    • FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity
    • Minamino, T., and R. M. Macnab. 2000. FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity. Mol. Microbiol. 37:1494-1503.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1494-1503
    • Minamino, T.1    Macnab, R.M.2
  • 33
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T., and R. M. Macnab. 2000. Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol. Microbiol. 35:1052-1064.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1052-1064
    • Minamino, T.1    Macnab, R.M.2
  • 35
    • 11844279779 scopus 로고    scopus 로고
    • A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal
    • Ramamurthi, K. S., and O. Schneewind. 2005. A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal. J. Bacteriol. 187:707-715.
    • (2005) J. Bacteriol. , vol.187 , pp. 707-715
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 37
    • 0029123567 scopus 로고
    • Functional conservation of the secretion and translocation machinery for virulence proteins of yersinia, salmonellae and shigellae
    • Rosqvist, R., S. Hakansson, A. Forsberg, and H. Wolf-Watz. 1995. Functional conservation of the secretion and translocation machinery for virulence proteins of yersinia, salmonellae and shigellae. EMBO J. 14:4187-4195.
    • (1995) EMBO J. , vol.14 , pp. 4187-4195
    • Rosqvist, R.1    Hakansson, S.2    Forsberg, A.3    Wolf-Watz, H.4
  • 38
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., K.-E. Magnusson, and H. Wolf-Watz. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:964-972.
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.-E.2    Wolf-Watz, H.3
  • 41
    • 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., E. Fritzh-Lindsten, and H. Wolf-Watz. 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    Fritzh-Lindsten, E.2    Wolf-Watz, H.3
  • 42
    • 0030707876 scopus 로고    scopus 로고
    • Death by lethal injection
    • Silhavy, T. J. 1997. Death by lethal injection. Science 278:1085-1086.
    • (1997) Science , vol.278 , pp. 1085-1086
    • Silhavy, T.J.1
  • 43
    • 26444526690 scopus 로고    scopus 로고
    • Rejection of impassable substrates by Yersinia type III secretion machines
    • Sorg, J. A., N. C. Miller, M. M. Marketon, and O. Schneewind. 2005. Rejection of impassable substrates by Yersinia type III secretion machines. J. Bacteriol. 187:7090-7102.
    • (2005) J. Bacteriol. , vol.187 , pp. 7090-7102
    • Sorg, J.A.1    Miller, N.C.2    Marketon, M.M.3    Schneewind, O.4
  • 44
    • 23844485234 scopus 로고    scopus 로고
    • Substrate recognition of type III secretion machines-testing the RNA signal hypothesis
    • Sorg, J. A., N. C. Miller, and O. Schneewind. 2005. Substrate recognition of type III secretion machines-testing the RNA signal hypothesis. Cell. Microbiol. 7:1217-1225.
    • (2005) Cell. Microbiol. , vol.7 , pp. 1217-1225
    • Sorg, J.A.1    Miller, N.C.2    Schneewind, O.3
  • 45
    • 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., A. Boland, I. Lambermont, and G. R. Cornelis. 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
  • 46
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol- or kanamycin-resistance selection
    • Takeshita, S., M. Sato, M. Toba, W. Masahashi, and T. Hashimoto-Gotoh. 1987. High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol- or kanamycin-resistance selection. Gene 61:63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 47
    • 0033621062 scopus 로고    scopus 로고
    • Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor
    • Thomas, D. R., D. G. Morgan, and D. J. DeRosier. 1999. Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor. Proc. Natl. Acad. Sci. USA 96:10134-10139.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10134-10139
    • Thomas, D.R.1    Morgan, D.G.2    Derosier, D.J.3
  • 48
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • Thomas, J., G. P. Stafford, and C. Hughes. 2004. Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc. Natl. Acad. Sci. USA 101:3945-3950.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 49
    • 25144508100 scopus 로고    scopus 로고
    • CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli
    • Thomas, N. A., W. Deng, J. L. Puente, E. A. Frey, C. K. Yip, N. C. Strynadka, and B. B. Finlay. 2005. CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli. Mol. Microbiol. 57:1762-1779.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1762-1779
    • Thomas, N.A.1    Deng, W.2    Puente, J.L.3    Frey, E.A.4    Yip, C.K.5    Strynadka, N.C.6    Finlay, B.B.7
  • 51
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE
    • Wattiau, P., and G. R. Cornelis. 1993. SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE. Mol. Microbiol. 8:123-131.
    • (1993) Mol. Microbiol. , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 52
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S, A. Allaoui, P. Wattiau, and G. R. Cornelis. 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
  • 53
    • 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., M.-P. Sory, A. Boland, O. Lequenne, and G. R. Cornelis. 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
  • 54
  • 55
    • 0037199491 scopus 로고    scopus 로고
    • Interactions among membrane and soluble components of the flagellar export apparatus of Salmonella
    • Zhu, K., B. Gonzalez-Pedrajo, and R. M. Macnab. 2002. Interactions among membrane and soluble components of the flagellar export apparatus of Salmonella. Biochemistry 41:9516-9524.
    • (2002) Biochemistry , vol.41 , pp. 9516-9524
    • Zhu, K.1    Gonzalez-Pedrajo, B.2    Macnab, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.