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Items: 1 to 20 of 101

1.

Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.

Lyu ZX, Shao Q, Gao YQ, Zhao XS.

PLoS One. 2012;7(9):e46068. doi: 10.1371/journal.pone.0046068. Epub 2012 Sep 26.

2.

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
3.

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
4.

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
5.

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
7.

The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains.

Walton TA, Sandoval CM, Fowler CA, Pardi A, Sousa MC.

Proc Natl Acad Sci U S A. 2009 Feb 10;106(6):1772-7. doi: 10.1073/pnas.0809275106. Epub 2009 Jan 30.

8.

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
9.

Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.

Burmann BM, Wang C, Hiller S.

Nat Struct Mol Biol. 2013 Nov;20(11):1265-72. doi: 10.1038/nsmb.2677. Epub 2013 Sep 29.

PMID:
24077225
10.

Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP.

McMorran LM, Bartlett AI, Huysmans GH, Radford SE, Brockwell DJ.

J Mol Biol. 2013 Sep 9;425(17):3178-91. doi: 10.1016/j.jmb.2013.06.017. Epub 2013 Jun 22.

11.

Role for Skp in LptD assembly in Escherichia coli.

Schwalm J, Mahoney TF, Soltes GR, Silhavy TJ.

J Bacteriol. 2013 Aug;195(16):3734-42. doi: 10.1128/JB.00431-13. Epub 2013 Jun 14.

12.
13.

Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.

Denoncin K, Schwalm J, Vertommen D, Silhavy TJ, Collet JF.

Proteomics. 2012 May;12(9):1391-401. doi: 10.1002/pmic.201100633.

15.

Skp is a multivalent chaperone of outer-membrane proteins.

Schiffrin B, Calabrese AN, Devine PWA, Harris SA, Ashcroft AE, Brockwell DJ, Radford SE.

Nat Struct Mol Biol. 2016 Sep;23(9):786-793. doi: 10.1038/nsmb.3266. Epub 2016 Jul 25.

16.

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.

17.

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.

18.

The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane.

Grabowicz M, Koren D, Silhavy TJ.

MBio. 2016 Apr 5;7(2):e00312-16. doi: 10.1128/mBio.00312-16.

19.

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.

20.

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

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