242 related articles for article (PubMed ID: 12270717)
1. Chaperone-independent folding of type 1 pilus domains.
Vetsch M; Sebbel P; Glockshuber R
J Mol Biol; 2002 Sep; 322(4):827-40. PubMed ID: 12270717
[TBL] [Abstract][Full Text] [Related]
2. Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli.
Hermanns U; Sebbel P; Eggli V; Glockshuber R
Biochemistry; 2000 Sep; 39(38):11564-70. PubMed ID: 10995223
[TBL] [Abstract][Full Text] [Related]
3. X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.
Choudhury D; Thompson A; Stojanoff V; Langermann S; Pinkner J; Hultgren SJ; Knight SD
Science; 1999 Aug; 285(5430):1061-6. PubMed ID: 10446051
[TBL] [Abstract][Full Text] [Related]
4. Identification and characterization of the chaperone-subunit complex-binding domain from the type 1 pilus assembly platform FimD.
Nishiyama M; Vetsch M; Puorger C; Jelesarov I; Glockshuber R
J Mol Biol; 2003 Jul; 330(3):513-25. PubMed ID: 12842468
[TBL] [Abstract][Full Text] [Related]
5. The Escherichia coli P and Type 1 Pilus Assembly Chaperones PapD and FimC Are Monomeric in Solution.
Sarowar S; Hu OJ; Werneburg GT; Thanassi DG; Li H
J Bacteriol; 2016 Sep; 198(17):2360-9. PubMed ID: 27353649
[TBL] [Abstract][Full Text] [Related]
6. Pilus chaperones represent a new type of protein-folding catalyst.
Vetsch M; Puorger C; Spirig T; Grauschopf U; Weber-Ban EU; Glockshuber R
Nature; 2004 Sep; 431(7006):329-33. PubMed ID: 15372038
[TBL] [Abstract][Full Text] [Related]
7. Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD.
Du M; Yuan Z; Yu H; Henderson N; Sarowar S; Zhao G; Werneburg GT; Thanassi DG; Li H
Nature; 2018 Oct; 562(7727):444-447. PubMed ID: 30283140
[TBL] [Abstract][Full Text] [Related]
8. Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.
Crespo MD; Puorger C; Schärer MA; Eidam O; Grütter MG; Capitani G; Glockshuber R
Nat Chem Biol; 2012 Aug; 8(8):707-13. PubMed ID: 22772153
[TBL] [Abstract][Full Text] [Related]
9. Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD.
Eidam O; Dworkowski FS; Glockshuber R; Grütter MG; Capitani G
FEBS Lett; 2008 Mar; 582(5):651-5. PubMed ID: 18242189
[TBL] [Abstract][Full Text] [Related]
10. Recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis.
Munera D; Hultgren S; Fernández LA
Mol Microbiol; 2007 Apr; 64(2):333-46. PubMed ID: 17378923
[TBL] [Abstract][Full Text] [Related]
11. Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD.
Nishiyama M; Horst R; Eidam O; Herrmann T; Ignatov O; Vetsch M; Bettendorff P; Jelesarov I; Grütter MG; Wüthrich K; Glockshuber R; Capitani G
EMBO J; 2005 Jun; 24(12):2075-86. PubMed ID: 15920478
[TBL] [Abstract][Full Text] [Related]
12. Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR.
Pellecchia M; Sebbel P; Hermanns U; Wüthrich K; Glockshuber R
Nat Struct Biol; 1999 Apr; 6(4):336-9. PubMed ID: 10201401
[TBL] [Abstract][Full Text] [Related]
13. Mechanical architecture and folding of E. coli type 1 pilus domains.
Alonso-Caballero A; Schönfelder J; Poly S; Corsetti F; De Sancho D; Artacho E; Perez-Jimenez R
Nat Commun; 2018 Jul; 9(1):2758. PubMed ID: 30013059
[TBL] [Abstract][Full Text] [Related]
14. Structure, folding and stability of FimA, the main structural subunit of type 1 pili from uropathogenic Escherichia coli strains.
Puorger C; Vetsch M; Wider G; Glockshuber R
J Mol Biol; 2011 Sep; 412(3):520-35. PubMed ID: 21816158
[TBL] [Abstract][Full Text] [Related]
15. NMR studies of interactions between periplasmic chaperones from uropathogenic E. coli and pilicides that interfere with chaperone function and pilus assembly.
Hedenström M; Emtenäs H; Pemberton N; Aberg V; Hultgren SJ; Pinkner JS; Tegman V; Almqvist F; Sethson I; Kihlberg J
Org Biomol Chem; 2005 Dec; 3(23):4193-200. PubMed ID: 16294247
[TBL] [Abstract][Full Text] [Related]
16. The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS.
Morrissey B; Leney AC; Toste Rêgo A; Phan G; Allen WJ; Verger D; Waksman G; Ashcroft AE; Radford SE
Mol Cell Proteomics; 2012 Jul; 11(7):M111.015289. PubMed ID: 22371487
[TBL] [Abstract][Full Text] [Related]
17. A molecular dynamics study of pilus subunits: insights into pilus biogenesis.
Vitagliano L; Ruggiero A; Pedone C; Berisio R
J Mol Biol; 2007 Apr; 367(4):935-41. PubMed ID: 17306829
[TBL] [Abstract][Full Text] [Related]
18. The structure of the PapD-PapGII pilin complex reveals an open and flexible P5 pocket.
Ford B; Verger D; Dodson K; Volkan E; Kostakioti M; Elam J; Pinkner J; Waksman G; Hultgren S
J Bacteriol; 2012 Dec; 194(23):6390-7. PubMed ID: 23002225
[TBL] [Abstract][Full Text] [Related]
19. Donor strand sequence, rather than donor strand orientation, determines the stability and non-equilibrium folding of the type 1 pilus subunit FimA.
Zyla D; Echeverria B; Glockshuber R
J Biol Chem; 2020 Aug; 295(35):12437-12448. PubMed ID: 32651228
[TBL] [Abstract][Full Text] [Related]
20. Chaperone-subunit-usher interactions required for donor strand exchange during bacterial pilus assembly.
Barnhart MM; Sauer FG; Pinkner JS; Hultgren SJ
J Bacteriol; 2003 May; 185(9):2723-30. PubMed ID: 12700251
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
