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Items: 1 to 20 of 103

2.

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
3.

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.

4.

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.

5.

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
6.

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
7.

The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation.

Entzminger KC, Chang C, Myhre RO, McCallum KC, Maynard JA.

Biochemistry. 2012 Jun 19;51(24):4822-34. doi: 10.1021/bi300412y. Epub 2012 Jun 8.

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.

Skp Trimer Formation Is Insensitive to Salts in the Physiological Range.

Sandlin CW, Zaccai NR, Fleming KG.

Biochemistry. 2015 Dec 8;54(48):7059-62. doi: 10.1021/acs.biochem.5b00806. Epub 2015 Nov 24.

11.

Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture.

Korndörfer IP, Dommel MK, Skerra A.

Nat Struct Mol Biol. 2004 Oct;11(10):1015-20. Epub 2004 Sep 12.

PMID:
15361861
12.

Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.

Thoma J, Burmann BM, Hiller S, Müller DJ.

Nat Struct Mol Biol. 2015 Oct;22(10):795-802. doi: 10.1038/nsmb.3087. Epub 2015 Sep 7.

PMID:
26344570
13.

The lipid bilayer-inserted membrane protein BamA of Escherichia coli facilitates insertion and folding of outer membrane protein A from its complex with Skp.

Patel GJ, Kleinschmidt JH.

Biochemistry. 2013 Jun 11;52(23):3974-86. doi: 10.1021/bi400103t. Epub 2013 May 24.

PMID:
23641708
14.

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.

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.

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
17.

Revisiting the interaction between the chaperone Skp and lipopolysaccharide.

Burmann BM, Holdbrook DA, Callon M, Bond PJ, Hiller S.

Biophys J. 2015 Mar 24;108(6):1516-26. doi: 10.1016/j.bpj.2015.01.029.

19.

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
20.

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.

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