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Items: 1 to 20 of 204

2.

The single-ring Thermoanaerobacter brockii chaperonin 60 (Tbr-EL7) dimerizes to Tbr-EL14.Tbr-ES7 under protein folding conditions.

Todd MJ, Walke S, Lorimer G, Truscott K, Scopes RK.

Biochemistry. 1995 Nov 14;34(45):14932-41.

PMID:
7578105
3.

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.

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.

5.

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH.

Nature. 1989 Dec 21-28;342(6252):884-9.

PMID:
10532860
6.

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.

7.

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
8.
9.
10.

Folding of malate dehydrogenase inside the GroEL-GroES cavity.

Chen J, Walter S, Horwich AL, Smith DL.

Nat Struct Biol. 2001 Aug;8(8):721-8.

PMID:
11473265
11.

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

Engel A, Hayer-Hartl MK, Goldie KN, Pfeifer G, Hegerl R, Müller S, da Silva AC, Baumeister W, Hartl FU.

Science. 1995 Aug 11;269(5225):832-6.

PMID:
7638600
12.

GroEL-mediated protein folding.

Fenton WA, Horwich AL.

Protein Sci. 1997 Apr;6(4):743-60. Review.

13.

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.

14.

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.

15.
16.

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

Martin J, Mayhew M, Langer T, Hartl FU.

Nature. 1993 Nov 18;366(6452):228-33.

PMID:
7901770
17.

Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring.

van Duijn E, Simmons DA, van den Heuvel RH, Bakkes PJ, van Heerikhuizen H, Heeren RM, Robinson CV, van der Vies SM, Heck AJ.

J Am Chem Soc. 2006 Apr 12;128(14):4694-702.

PMID:
16594706
18.

Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.

Nieba-Axmann SE, Ottiger M, Wüthrich K, Plückthun A.

J Mol Biol. 1997 Sep 5;271(5):803-18.

PMID:
9299328
19.
20.

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.

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