Pinkner JS - Search Results

1

Structural basis of chaperone function and pilus biogenesis.

Sauer FG, Fütterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G. Sauer FG, et al. Among authors: pinkner js. Science. 1999 Aug 13;285(5430):1058-61. doi: 10.1126/science.285.5430.1058. Science. 1999. PMID: 10446050

2

PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.

Jacob-Dubuisson F, Pinkner J, Xu Z, Striker R, Padmanhaban A, Hultgren SJ. Jacob-Dubuisson F, et al. Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11552-6. doi: 10.1073/pnas.91.24.11552. Proc Natl Acad Sci U S A. 1994. PMID: 7972100 Free PMC article.

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. Choudhury D, et al. Science. 1999 Aug 13;285(5430):1061-6. doi: 10.1126/science.285.5430.1061. Science. 1999. PMID: 10446051

4

Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.

Slonim LN, Pinkner JS, Brändén CI, Hultgren SJ. Slonim LN, et al. Among authors: pinkner js. EMBO J. 1992 Dec;11(13):4747-56. doi: 10.1002/j.1460-2075.1992.tb05580.x. EMBO J. 1992. PMID: 1361168 Free PMC article.

5

Molecular dissection of PapD interaction with PapG reveals two chaperone-binding sites.

Xu Z, Jones CH, Haslam D, Pinkner JS, Dodson K, Kihlberg J, Hultgren SJ. Xu Z, et al. Among authors: pinkner js. Mol Microbiol. 1995 Jun;16(5):1011-20. doi: 10.1111/j.1365-2958.1995.tb02326.x. Mol Microbiol. 1995. PMID: 7476177

6

FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria.

Jones CH, Pinkner JS, Nicholes AV, Slonim LN, Abraham SN, Hultgren SJ. Jones CH, et al. Among authors: pinkner js. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8397-401. doi: 10.1073/pnas.90.18.8397. Proc Natl Acad Sci U S A. 1993. PMID: 8104335 Free PMC article.

7

Molecular basis of two subfamilies of immunoglobulin-like chaperones.

Hung DL, Knight SD, Woods RM, Pinkner JS, Hultgren SJ. Hung DL, et al. Among authors: pinkner js. EMBO J. 1996 Aug 1;15(15):3792-805. EMBO J. 1996. PMID: 8670884 Free PMC article.

8

The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems.

Jones CH, Danese PN, Pinkner JS, Silhavy TJ, Hultgren SJ. Jones CH, et al. Among authors: pinkner js. EMBO J. 1997 Nov 3;16(21):6394-406. doi: 10.1093/emboj/16.21.6394. EMBO J. 1997. PMID: 9351822 Free PMC article.

9

Ramifications of kinetic partitioning on usher-mediated pilus biogenesis.

Saulino ET, Thanassi DG, Pinkner JS, Hultgren SJ. Saulino ET, et al. Among authors: pinkner js. EMBO J. 1998 Apr 15;17(8):2177-85. doi: 10.1093/emboj/17.8.2177. EMBO J. 1998. PMID: 9545231 Free PMC article.

10

Structural basis of chaperone self-capping in P pilus biogenesis.

Hung DL, Pinkner JS, Knight SD, Hultgren SJ. Hung DL, et al. Among authors: pinkner js. Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):8178-83. doi: 10.1073/pnas.96.14.8178. Proc Natl Acad Sci U S A. 1999. PMID: 10393968 Free PMC article.

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