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Items: 1 to 20 of 629

1.

Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.

Figueiredo L, Klunker D, Ang D, Naylor DJ, Kerner MJ, Georgopoulos C, Hartl FU, Hayer-Hartl M.

J Biol Chem. 2004 Jan 9;279(2):1090-9. Epub 2003 Oct 23.

2.

Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei.

Klunker D, Haas B, Hirtreiter A, Figueiredo L, Naylor DJ, Pfeifer G, Müller V, Deppenmeier U, Gottschalk G, Hartl FU, Hayer-Hartl M.

J Biol Chem. 2003 Aug 29;278(35):33256-67. Epub 2003 Jun 9.

3.

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.

Weber F, Keppel F, Georgopoulos C, Hayer-Hartl MK, Hartl FU.

Nat Struct Biol. 1998 Nov;5(11):977-85. Erratum in: Nat Struct Biol 1999 Feb;6(2):200.

PMID:
9808043
4.

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.

6.

Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.

Nojima T, Murayama S, Yoshida M, Motojima F.

J Biol Chem. 2008 Jun 27;283(26):18385-92. doi: 10.1074/jbc.M709825200. Epub 2008 Apr 22.

8.

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.

Chatellier J, Hill F, Foster NW, Goloubinoff P, Fersht AR.

J Mol Biol. 2000 Dec 15;304(5):897-910.

PMID:
11124035
9.

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
10.

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
11.

The effect of macromolecular crowding on chaperonin-mediated protein folding.

Martin J, Hartl FU.

Proc Natl Acad Sci U S A. 1997 Feb 18;94(4):1107-12.

12.

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.

Weissman JS, Rye HS, Fenton WA, Beechem JM, Horwich AL.

Cell. 1996 Feb 9;84(3):481-90.

13.

Dual function of protein confinement in chaperonin-assisted protein folding.

Brinker A, Pfeifer G, Kerner MJ, Naylor DJ, Hartl FU, Hayer-Hartl M.

Cell. 2001 Oct 19;107(2):223-33.

14.

GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.

Miyazaki T, Yoshimi T, Furutsu Y, Hongo K, Mizobata T, Kanemori M, Kawata Y.

J Biol Chem. 2002 Dec 27;277(52):50621-8. Epub 2002 Oct 10.

15.

Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.

Gupta P, Aggarwal N, Batra P, Mishra S, Chaudhuri TK.

Int J Biochem Cell Biol. 2006;38(11):1975-85. Epub 2006 Jun 2. Erratum in: Int J Biochem Cell Biol. 2007;39(3):660.

PMID:
16822698
16.

Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding.

Llorca O, Carrascosa JL, Valpuesta JM.

J Biol Chem. 1996 Jan 5;271(1):68-76.

17.

Minimal and optimal mechanisms for GroE-mediated protein folding.

Ben-Zvi AP, Chatellier J, Fersht AR, Goloubinoff P.

Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15275-80. Erratum in: Proc Natl Acad Sci U S A 1999 May 11;96(10):5890.

18.

Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.

Illingworth M, Salisbury J, Li W, Lin D, Chen L.

Biochem Biophys Res Commun. 2015 Oct 9;466(1):15-20. doi: 10.1016/j.bbrc.2015.08.034. Epub 2015 Aug 11.

PMID:
26271593
19.

Reversible oligomerization and denaturation of the chaperonin GroES.

Seale JW, Gorovits BM, Ybarra J, Horowitz PM.

Biochemistry. 1996 Apr 2;35(13):4079-83.

PMID:
8672442
20.

Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.

Betancourt MR, Thirumalai D.

J Mol Biol. 1999 Apr 2;287(3):627-44.

PMID:
10092464
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