Display Settings:

Format
Items per page
Sort by

Send to:

Choose Destination

Results: 1 to 20 of 135

1.

Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation.

Puorger C, Eidam O, Capitani G, Erilov D, Grütter MG, Glockshuber R.

Structure. 2008 Apr;16(4):631-42. doi: 10.1016/j.str.2008.01.013.

PMID:
18400183
[PubMed - indexed for MEDLINE]
Free Article
2.

NMR structure of the Escherichia coli type 1 pilus subunit FimF and its interactions with other pilus subunits.

Gossert AD, Bettendorff P, Puorger C, Vetsch M, Herrmann T, Glockshuber R, Wüthrich K.

J Mol Biol. 2008 Jan 18;375(3):752-63. Epub 2007 Nov 1.

PMID:
18048056
[PubMed - indexed for MEDLINE]
3.

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 23;412(3):520-35. doi: 10.1016/j.jmb.2011.07.044. Epub 2011 Jul 27.

PMID:
21816158
[PubMed - indexed for MEDLINE]
4.

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 16;431(7006):329-33.

PMID:
15372038
[PubMed - indexed for MEDLINE]
5.

Preclusion of irreversible destruction of Dr adhesin structures by a high activation barrier for the unfolding stage of the fimbrial DraE subunit.

Piatek R, Bruździak P, Zalewska-Piatek B, Kur J, Stangret J.

Biochemistry. 2009 Dec 15;48(49):11807-16. doi: 10.1021/bi900920k.

PMID:
19891507
[PubMed - indexed for MEDLINE]
6.

Chaperone-independent folding of type 1 pilus domains.

Vetsch M, Sebbel P, Glockshuber R.

J Mol Biol. 2002 Sep 27;322(4):827-40.

PMID:
12270717
[PubMed - indexed for MEDLINE]
7.

Structural basis of chaperone function and pilus biogenesis.

Sauer FG, Fütterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G.

Science. 1999 Aug 13;285(5430):1058-61.

PMID:
10446050
[PubMed - indexed for MEDLINE]
Free Article
8.

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 5;582(5):651-5. doi: 10.1016/j.febslet.2008.01.030. Epub 2008 Jan 31.

PMID:
18242189
[PubMed - indexed for MEDLINE]
Free Article
9.

Intramolecular donor strand complementation in the E. coli type 1 pilus subunit FimA explains the existence of FimA monomers as off-pathway products of pilus assembly that inhibit host cell apoptosis.

Walczak MJ, Puorger C, Glockshuber R, Wider G.

J Mol Biol. 2014 Feb 6;426(3):542-9. doi: 10.1016/j.jmb.2013.10.029. Epub 2013 Oct 30.

PMID:
24184277
[PubMed - indexed for MEDLINE]
10.

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 11;330(3):513-25.

PMID:
12842468
[PubMed - indexed for MEDLINE]
11.

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 13;285(5430):1061-6.

PMID:
10446051
[PubMed - indexed for MEDLINE]
Free Article
12.

A molecular dynamics study of pilus subunits: insights into pilus biogenesis.

Vitagliano L, Ruggiero A, Pedone C, Berisio R.

J Mol Biol. 2007 Apr 6;367(4):935-41. Epub 2007 Jan 20.

PMID:
17306829
[PubMed - indexed for MEDLINE]
13.

The outer membrane usher guarantees the formation of functional pili by selectively catalyzing donor-strand exchange between subunits that are adjacent in the mature pilus.

Nishiyama M, Glockshuber R.

J Mol Biol. 2010 Feb 12;396(1):1-8. doi: 10.1016/j.jmb.2009.12.005. Epub 2010 Jan 13.

PMID:
20004668
[PubMed - indexed for MEDLINE]
14.

Second order rate constants of donor-strand exchange reveal individual amino acid residues important in determining the subunit specificity of pilus biogenesis.

Leney AC, Phan G, Allen W, Verger D, Waksman G, Radford SE, Ashcroft AE.

J Am Soc Mass Spectrom. 2011 Jul;22(7):1214-23. doi: 10.1007/s13361-011-0146-4. Epub 2011 May 10.

PMID:
21953104
[PubMed - indexed for MEDLINE]
Free PMC Article
15.

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 15;24(12):2075-86. Epub 2005 May 26.

PMID:
15920478
[PubMed - indexed for MEDLINE]
Free PMC Article
16.

Donor strand exchange and conformational changes during E. coli fimbrial formation.

Le Trong I, Aprikian P, Kidd BA, Thomas WE, Sokurenko EV, Stenkamp RE.

J Struct Biol. 2010 Dec;172(3):380-8. doi: 10.1016/j.jsb.2010.06.002. Epub 2010 Jun 4.

PMID:
20570733
[PubMed - indexed for MEDLINE]
Free PMC Article
17.

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. doi: 10.1038/nchembio.1019. Epub 2012 Jul 1.

PMID:
22772153
[PubMed - indexed for MEDLINE]
18.

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.

PMID:
12700251
[PubMed - indexed for MEDLINE]
Free PMC Article
19.

Mechanism of fibre assembly through the chaperone-usher pathway.

Vetsch M, Erilov D, Molière N, Nishiyama M, Ignatov O, Glockshuber R.

EMBO Rep. 2006 Jul;7(7):734-8. Epub 2006 Jun 9.

PMID:
16767077
[PubMed - indexed for MEDLINE]
Free PMC Article
20.

Adaptor function of PapF depends on donor strand exchange in P-pilus biogenesis of Escherichia coli.

Lee YM, Dodson KW, Hultgren SJ.

J Bacteriol. 2007 Jul;189(14):5276-83. Epub 2007 May 11.

PMID:
17496084
[PubMed - indexed for MEDLINE]
Free PMC Article

Display Settings:

Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Write to the Help Desk