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Items: 1 to 20 of 173

1.

GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.

Tyagi NK, Fenton WA, Horwich AL.

Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20264-9. doi: 10.1073/pnas.0911556106. Epub 2009 Nov 13.

2.

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.

Rye HS, Roseman AM, Chen S, Furtak K, Fenton WA, Saibil HR, Horwich AL.

Cell. 1999 Apr 30;97(3):325-38.

3.

Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.

Motojima F, Chaudhry C, Fenton WA, Farr GW, Horwich AL.

Proc Natl Acad Sci U S A. 2004 Oct 19;101(42):15005-12. Epub 2004 Oct 12.

4.

Expansion and compression of a protein folding intermediate by GroEL.

Lin Z, Rye HS.

Mol Cell. 2004 Oct 8;16(1):23-34. Erratum in: Mol Cell. 2004 Oct 22;16(2):317.

6.

Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.

Lin Z, Puchalla J, Shoup D, Rye HS.

J Biol Chem. 2013 Oct 25;288(43):30944-55. doi: 10.1074/jbc.M113.480178. Epub 2013 Sep 10.

7.

Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins.

Machida K, Fujiwara R, Tanaka T, Sakane I, Hongo K, Mizobata T, Kawata Y.

Biochim Biophys Acta. 2009 Sep;1794(9):1344-54. doi: 10.1016/j.bbapap.2008.12.003. Epub 2008 Dec 24.

PMID:
19130907
8.

Triggering protein folding within the GroEL-GroES complex.

Madan D, Lin Z, Rye HS.

J Biol Chem. 2008 Nov 14;283(46):32003-13. doi: 10.1074/jbc.M802898200. Epub 2008 Sep 9.

9.

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

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

Nature. 1997 Aug 21;388(6644):792-8.

PMID:
9285593
10.

Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.

Haldar S, Gupta AJ, Yan X, Miličić G, Hartl FU, Hayer-Hartl M.

J Mol Biol. 2015 Jun 19;427(12):2244-55. doi: 10.1016/j.jmb.2015.04.009. Epub 2015 Apr 23.

PMID:
25912285
11.

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
12.

Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.

Chaudhry C, Farr GW, Todd MJ, Rye HS, Brunger AT, Adams PD, Horwich AL, Sigler PB.

EMBO J. 2003 Oct 1;22(19):4877-87.

13.

GroEL stimulates protein folding through forced unfolding.

Lin Z, Madan D, Rye HS.

Nat Struct Mol Biol. 2008 Mar;15(3):303-11. doi: 10.1038/nsmb.1394. Epub 2008 Mar 2.

14.
16.

Chaperonin-mediated protein folding: fate of substrate polypeptide.

Fenton WA, Horwich AL.

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

PMID:
14686103
17.

A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.

Cliff MJ, Kad NM, Hay N, Lund PA, Webb MR, Burston SG, Clarke AR.

J Mol Biol. 1999 Oct 29;293(3):667-84.

PMID:
10543958
18.

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

Hayer-Hartl MK, Martin J, Hartl FU.

Science. 1995 Aug 11;269(5225):836-41.

PMID:
7638601
19.

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

Weissman JS, Hohl CM, Kovalenko O, Kashi Y, Chen S, Braig K, Saibil HR, Fenton WA, Horwich AL.

Cell. 1995 Nov 17;83(4):577-87.

20.

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.

Farr GW, Fenton WA, Chaudhuri TK, Clare DK, Saibil HR, Horwich AL.

EMBO J. 2003 Jul 1;22(13):3220-30.

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