Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 99

1.

Conditional disorder in chaperone action.

Bardwell JC, Jakob U.

Trends Biochem Sci. 2012 Dec;37(12):517-25. doi: 10.1016/j.tibs.2012.08.006. Epub 2012 Sep 24. Review.

2.

Conditional Chaperone-Client Interactions Revealed by Genetically Encoded Photo-cross-linkers.

Zhang S, He D, Lin Z, Yang Y, Song H, Chen PR.

Acc Chem Res. 2017 May 16;50(5):1184-1192. doi: 10.1021/acs.accounts.6b00647. Epub 2017 May 3.

PMID:
28467057
3.

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo.

Dahl JU, Koldewey P, Bardwell JC, Jakob U.

J Vis Exp. 2016 Oct 23;(116). doi: 10.3791/54527.

PMID:
27805614
4.

The role of structural disorder in the function of RNA and protein chaperones.

Tompa P, Csermely P.

FASEB J. 2004 Aug;18(11):1169-75. Review.

PMID:
15284216
5.

HdeB functions as an acid-protective chaperone in bacteria.

Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U.

J Biol Chem. 2015 Jan 2;290(1):65-75. doi: 10.1074/jbc.M114.612986. Epub 2014 Nov 12. Erratum in: J Biol Chem. 2015 Apr 17;290(16):9950.

6.

Diverse functional manifestations of intrinsic structural disorder in molecular chaperones.

Kovacs D, Tompa P.

Biochem Soc Trans. 2012 Oct;40(5):963-8. Review.

PMID:
22988848
7.

Folding on the chaperone: yield enhancement through loose binding.

Jewett AI, Shea JE.

J Mol Biol. 2006 Nov 10;363(5):945-57. Epub 2006 Aug 22.

PMID:
16987526
8.

Intrinsically disordered proteins display no preference for chaperone binding in vivo.

Hegyi H, Tompa P.

PLoS Comput Biol. 2008 Mar 7;4(3):e1000017. doi: 10.1371/journal.pcbi.1000017.

9.

Intrinsically disordered proteins as molecular shields.

Chakrabortee S, Tripathi R, Watson M, Schierle GS, Kurniawan DP, Kaminski CF, Wise MJ, Tunnacliffe A.

Mol Biosyst. 2012 Jan;8(1):210-9. doi: 10.1039/c1mb05263b. Epub 2011 Sep 9.

10.

The intramolecular chaperone-mediated protein folding.

Chen YJ, Inouye M.

Curr Opin Struct Biol. 2008 Dec;18(6):765-70. doi: 10.1016/j.sbi.2008.10.005. Epub 2008 Nov 13. Review.

PMID:
18973809
11.

Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.

Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S.

Proc Natl Acad Sci U S A. 2015 Aug 4;112(31):E4206-15. doi: 10.1073/pnas.1505173112. Epub 2015 Jul 20.

12.

Super Spy variants implicate flexibility in chaperone action.

Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC.

Elife. 2014;3:e01584. doi: 10.7554/eLife.01584. Epub 2014 Feb 4.

13.

CHIP: a co-chaperone for degradation by the proteasome.

Edkins AL.

Subcell Biochem. 2015;78:219-42. doi: 10.1007/978-3-319-11731-7_11. Review.

PMID:
25487024
14.

Protein unfolding as a switch from self-recognition to high-affinity client binding.

Groitl B, Horowitz S, Makepeace KA, Petrotchenko EV, Borchers CH, Reichmann D, Bardwell JC, Jakob U.

Nat Commun. 2016 Jan 20;7:10357. doi: 10.1038/ncomms10357.

15.

Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012).

Foffi G, Pastore A, Piazza F, Temussi PA.

Phys Biol. 2013 Aug 2;10(4):040301. [Epub ahead of print]

PMID:
23912807
16.

The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis.

Brandvold KR, Morimoto RI.

J Mol Biol. 2015 Sep 11;427(18):2931-47. doi: 10.1016/j.jmb.2015.05.010. Epub 2015 May 21. Review.

17.

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.

Mattoo RU, Goloubinoff P.

Cell Mol Life Sci. 2014 Sep;71(17):3311-25. doi: 10.1007/s00018-014-1627-y. Epub 2014 Apr 24. Review.

18.

Multiscale modeling of a conditionally disordered pH-sensing chaperone.

Ahlstrom LS, Law SM, Dickson A, Brooks CL 3rd.

J Mol Biol. 2015 Apr 24;427(8):1670-80. doi: 10.1016/j.jmb.2015.01.002. Epub 2015 Jan 10.

19.

Supervising the fold: functional principles of molecular chaperones.

Buchner J.

FASEB J. 1996 Jan;10(1):10-9. Review.

PMID:
8566529
20.

Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone.

Acosta-Sampson L, King J.

J Mol Biol. 2010 Aug 6;401(1):134-52. doi: 10.1016/j.jmb.2010.05.067. Epub 2010 Jun 1.

Supplemental Content

Support Center