Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT

Buttner CR, Cornelis GR, Heinz DW, Niemann H (2005)
Protein Sci 14(8): 1993-2002.

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Protein Sci
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14
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8
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1993-2002
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Buttner CR, Cornelis GR, Heinz DW, Niemann H. Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT. Protein Sci. 2005;14(8):1993-2002.
Buttner, C. R., Cornelis, G. R., Heinz, D. W., & Niemann, H. (2005). Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT. Protein Sci, 14(8), 1993-2002. doi:10.1110/ps.051474605
Buttner, C. R., Cornelis, G. R., Heinz, D. W., and Niemann, H. (2005). Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT. Protein Sci 14, 1993-2002.
Buttner, C.R., et al., 2005. Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT. Protein Sci, 14(8), p 1993-2002.
C.R. Buttner, et al., “Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT”, Protein Sci, vol. 14, 2005, pp. 1993-2002.
Buttner, C.R., Cornelis, G.R., Heinz, D.W., Niemann, H.: Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT. Protein Sci. 14, 1993-2002 (2005).
Buttner, C. R., Cornelis, G. R., Heinz, D. W., and Niemann, Hartmut. “Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT”. Protein Sci 14.8 (2005): 1993-2002.

19 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT.
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The Deinococcus radiodurans DR1245 protein, a DdrB partner homologous to YbjN proteins and reminiscent of type III secretion system chaperones.
Norais C, Servant P, Bouthier-de-la-Tour C, Coureux PD, Ithurbide S, Vannier F, Guerin PP, Dulberger CL, Satyshur KA, Keck JL, Armengaud J, Cox MM, Sommer S., PLoS One 8(2), 2013
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Chlamydia trachomatis Slc1 is a type III secretion chaperone that enhances the translocation of its invasion effector substrate TARP.
Brinkworth AJ, Malcolm DS, Pedrosa AT, Roguska K, Shahbazian S, Graham JE, Hayward RD, Carabeo RA., Mol Microbiol 82(1), 2011
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Rodgers L, Mukerjea R, Birtalan S, Friedberg D, Ghosh P., J Bacteriol 192(12), 2010
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The Helicobacter pylori CagD (HP0545, Cag24) protein is essential for CagA translocation and maximal induction of interleukin-8 secretion.
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Yersinia enterocolitica type III secretion chaperone SycD: recombinant expression, purification and characterization of a homodimer.
Schmid A, Dittmann S, Grimminger V, Walter S, Heesemann J, Wilharm G., Protein Expr Purif 49(2), 2006
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Letzelter M, Sorg I, Mota LJ, Meyer S, Stalder J, Feldman M, Kuhn M, Callebaut I, Cornelis GR., EMBO J 25(13), 2006
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Structure-based mutagenesis of SigE verifies the importance of hydrophobic and electrostatic residues in type III chaperone function.
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The type III secretion injectisome.
Cornelis GR., Nat Rev Microbiol 4(11), 2006
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The type III needle and the damage done.
Johnson S, Deane JE, Lea SM., Curr Opin Struct Biol 15(6), 2005
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