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Items: 1 to 20 of 357

2.

Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.

Sklar JG, Wu T, Kahne D, Silhavy TJ.

Genes Dev. 2007 Oct 1;21(19):2473-84.

3.

The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential.

Patel GJ, Behrens-Kneip S, Holst O, Kleinschmidt JH.

Biochemistry. 2009 Nov 3;48(43):10235-45. doi: 10.1021/bi901403c.

PMID:
19780589
4.

Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study.

Qu J, Behrens-Kneip S, Holst O, Kleinschmidt JH.

Biochemistry. 2009 Jun 9;48(22):4926-36. doi: 10.1021/bi9004039.

PMID:
19382746
6.

The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.

Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H.

J Biol Chem. 2001 Jun 1;276(22):18804-11. Epub 2001 Mar 5.

7.

The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions.

Qu J, Mayer C, Behrens S, Holst O, Kleinschmidt JH.

J Mol Biol. 2007 Nov 16;374(1):91-105. Epub 2007 Sep 14.

PMID:
17928002
8.
9.

Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains.

Bodelón G, Marín E, Fernández LA.

J Bacteriol. 2009 Aug;191(16):5169-79. doi: 10.1128/JB.00458-09. Epub 2009 Jun 12.

10.

Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp.

Jarchow S, Lück C, Görg A, Skerra A.

Proteomics. 2008 Dec;8(23-24):4987-94. doi: 10.1002/pmic.200800288.

PMID:
19003857
11.

Membrane protein folding on the example of outer membrane protein A of Escherichia coli.

Kleinschmidt JH.

Cell Mol Life Sci. 2003 Aug;60(8):1547-58. Review.

PMID:
14513830
12.

Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.

Bulieris PV, Behrens S, Holst O, Kleinschmidt JH.

J Biol Chem. 2003 Mar 14;278(11):9092-9. Epub 2002 Dec 30.

13.
14.

Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism.

Wu S, Ge X, Lv Z, Zhi Z, Chang Z, Zhao XS.

Biochem J. 2011 Sep 15;438(3):505-11. doi: 10.1042/BJ20110264.

PMID:
21671888
15.

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

Matern Y, Barion B, Behrens-Kneip S.

BMC Microbiol. 2010 Sep 29;10:251. doi: 10.1186/1471-2180-10-251.

16.

The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization.

Schlapschy M, Dommel MK, Hadian K, Fogarasi M, Korndörfer IP, Skerra A.

Biol Chem. 2004 Feb;385(2):137-43.

PMID:
15101556
17.

Periplasmic quality control in biogenesis of outer membrane proteins.

Lyu ZX, Zhao XS.

Biochem Soc Trans. 2015 Apr;43(2):133-8. doi: 10.1042/BST20140217. Review.

PMID:
25849907
18.

[Transport of outer membrane proteins].

Matsuyama S, Tokuda H.

Tanpakushitsu Kakusan Koso. 2004 May;49(7 Suppl):965-6. Review. Japanese. No abstract available.

PMID:
15168504
19.

The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli.

Palomino C, Marín E, Fernández LÁ.

J Bacteriol. 2011 Oct;193(19):5222-30. doi: 10.1128/JB.05585-11. Epub 2011 Jul 22.

20.

Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane.

Müller M, Koch HG, Beck K, Schäfer U.

Prog Nucleic Acid Res Mol Biol. 2001;66:107-57. Review.

PMID:
11051763
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