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Items: 19

1.

Mechanism of folding chamber closure in a group II chaperonin.

Zhang J, Baker ML, Schröder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W.

Nature. 2010 Jan 21;463(7279):379-83. doi: 10.1038/nature08701.

2.

The Mechanism and Function of Group II Chaperonins.

Lopez T, Dalton K, Frydman J.

J Mol Biol. 2015 Sep 11;427(18):2919-30. doi: 10.1016/j.jmb.2015.04.013. Epub 2015 Apr 30. Review.

3.

Dynamics, flexibility, and allostery in molecular chaperonins.

Skjærven L, Cuellar J, Martinez A, Valpuesta JM.

FEBS Lett. 2015 Sep 14;589(19 Pt A):2522-32. doi: 10.1016/j.febslet.2015.06.019. Epub 2015 Jun 30. Review.

4.

Chaperonins: The hunt for the Group II mechanism.

Bigotti MG, Clarke AR.

Arch Biochem Biophys. 2008 Jun 15;474(2):331-9. doi: 10.1016/j.abb.2008.03.015. Epub 2008 Mar 22. Review.

PMID:
18395510
5.

Group II chaperonins: new TRiC(k)s and turns of a protein folding machine.

Gutsche I, Essen LO, Baumeister W.

J Mol Biol. 1999 Oct 22;293(2):295-312. Review.

PMID:
10550210
6.

Allosteric Mechanisms in Chaperonin Machines.

Gruber R, Horovitz A.

Chem Rev. 2016 Jun 8;116(11):6588-606. doi: 10.1021/acs.chemrev.5b00556. Epub 2016 Jan 4. Review.

PMID:
26726755
7.

Chaperonins: two rings for folding.

Yébenes H, Mesa P, Muñoz IG, Montoya G, Valpuesta JM.

Trends Biochem Sci. 2011 Aug;36(8):424-32. doi: 10.1016/j.tibs.2011.05.003. Epub 2011 Jun 30. Review.

PMID:
21723731
8.

Chaperonin-mediated protein folding: fate of substrate polypeptide.

Fenton WA, Horwich AL.

Q Rev Biophys. 2003 May;36(2):229-56. Review.

PMID:
14686103
9.

Chaperonin-co-chaperonin interactions.

Boshoff A.

Subcell Biochem. 2015;78:153-78. doi: 10.1007/978-3-319-11731-7_8. Review.

PMID:
25487021
10.
11.

Structure and function of archaeal prefoldin, a co-chaperone of group II chaperonin.

Ohtaki A, Noguchi K, Yohda M.

Front Biosci (Landmark Ed). 2010 Jan 1;15:708-17. Review.

PMID:
20036841
12.

Chaperonins.

Ranson NA, White HE, Saibil HR.

Biochem J. 1998 Jul 15;333 ( Pt 2):233-42. Review.

13.

Structure and function in GroEL-mediated protein folding.

Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL.

Annu Rev Biochem. 1998;67:581-608. Review.

PMID:
9759498
14.

GroEL/GroES: structure and function of a two-stroke folding machine.

Xu Z, Sigler PB.

J Struct Biol. 1998 Dec 15;124(2-3):129-41. Review.

PMID:
10049801
15.

Chaperonin-mediated protein folding.

Thirumalai D, Lorimer GH.

Annu Rev Biophys Biomol Struct. 2001;30:245-69. Review.

PMID:
11340060
16.

Allosteric regulation of chaperonins.

Horovitz A, Willison KR.

Curr Opin Struct Biol. 2005 Dec;15(6):646-51. Epub 2005 Oct 24. Review.

PMID:
16249079
17.

Archaeal chaperonins.

Large AT, Lund PA.

Front Biosci (Landmark Ed). 2009 Jan 1;14:1304-24. Review.

PMID:
19273132
18.

Visualizing microtubule structural transitions and interactions with associated proteins.

Nogales E, Zhang R.

Curr Opin Struct Biol. 2016 Apr;37:90-6. doi: 10.1016/j.sbi.2015.12.009. Epub 2016 Jan 21. Review.

19.

Advances in high-resolution cryo-EM of oligomeric enzymes.

Vonck J, Mills DJ.

Curr Opin Struct Biol. 2017 Jun 15;46:48-54. doi: 10.1016/j.sbi.2017.05.016. [Epub ahead of print] Review.

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