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4. 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 NA; Deng W; Puente JL; Frey EA; Yip CK; Strynadka NC; Finlay BB Mol Microbiol; 2005 Sep; 57(6):1762-79. PubMed ID: 16135239 [TBL] [Abstract][Full Text] [Related]
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6. Structure of the Yersinia type III secretory system chaperone SycE. Birtalan S; Ghosh P Nat Struct Biol; 2001 Nov; 8(11):974-8. PubMed ID: 11685245 [TBL] [Abstract][Full Text] [Related]
7. Chaperone release and unfolding of substrates in type III secretion. Akeda Y; Galán JE Nature; 2005 Oct; 437(7060):911-5. PubMed ID: 16208377 [TBL] [Abstract][Full Text] [Related]
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10. Crystallographic analysis of Bacillus subtilis CsaA. Shapova YA; Paetzel M Acta Crystallogr D Biol Crystallogr; 2007 Apr; 63(Pt 4):478-85. PubMed ID: 17372352 [TBL] [Abstract][Full Text] [Related]
11. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Stebbins CE; Galán JE Nature; 2001 Nov; 414(6859):77-81. PubMed ID: 11689946 [TBL] [Abstract][Full Text] [Related]
12. The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces. Van Molle I; Moonens K; Buts L; Garcia-Pino A; Panjikar S; Wyns L; De Greve H; Bouckaert J Acta Crystallogr D Biol Crystallogr; 2009 May; 65(Pt 5):411-20. PubMed ID: 19390146 [TBL] [Abstract][Full Text] [Related]
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15. Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis. Singer AU; Desveaux D; Betts L; Chang JH; Nimchuk Z; Grant SR; Dangl JL; Sondek J Structure; 2004 Sep; 12(9):1669-81. PubMed ID: 15341731 [TBL] [Abstract][Full Text] [Related]
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18. SigE is a chaperone for the Salmonella enterica serovar Typhimurium invasion protein SigD. Darwin KH; Robinson LS; Miller VL J Bacteriol; 2001 Feb; 183(4):1452-4. PubMed ID: 11157959 [TBL] [Abstract][Full Text] [Related]
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