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Items: 17

1.

A two-step mechanism for the folding of actin by the yeast cytosolic chaperonin.

Stuart SF, Leatherbarrow RJ, Willison KR.

J Biol Chem. 2011 Jan 7;286(1):178-84. doi: 10.1074/jbc.M110.166256. Epub 2010 Nov 5.

2.

Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.

Altschuler GM, Willison KR.

J R Soc Interface. 2008 Dec 6;5(29):1391-408. doi: 10.1098/rsif.2008.0185. Review.

3.

Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.

Valpuesta JM, Martín-Benito J, Gómez-Puertas P, Carrascosa JL, Willison KR.

FEBS Lett. 2002 Oct 2;529(1):11-6. Review.

4.

[CCT chaperonins and their cochaperons].

Bregier C, Kupikowska B, Fabczak H, Fabczak S.

Postepy Biochem. 2008;54(1):64-70. Review. Polish.

PMID:
18610583
5.

Function and regulation of cytosolic molecular chaperone CCT.

Kubota H.

Vitam Horm. 2002;65:313-31. Review.

PMID:
12481552
6.

The substrate recognition mechanisms in chaperonins.

Gómez-Puertas P, Martín-Benito J, Carrascosa JL, Willison KR, Valpuesta JM.

J Mol Recognit. 2004 Mar-Apr;17(2):85-94. Review.

PMID:
15027029
7.

Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.

Leroux MR, Hartl FU.

Curr Biol. 2000 Apr 6;10(7):R260-4. Review.

8.

Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding.

Willardson BM, Howlett AC.

Cell Signal. 2007 Dec;19(12):2417-27. Epub 2007 Jun 28. Review.

10.

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.

11.

[GLOBULAR ACTIN IS THE PARTIALLY INTRINSICALLY DISORDERED PROTEIN WITH QUASI-STATIONARY STRUCTURE].

Povarova OI, Gagarskaia YA, Uversky VN, Kuznetsova IM, Turoverov KK.

Tsitologiia. 2015;57(7):467-79. Review. Russian.

PMID:
26591059
12.

Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation.

Brackley KI, Grantham J.

Cell Stress Chaperones. 2009 Jan;14(1):23-31. doi: 10.1007/s12192-008-0057-x. Epub 2008 Jul 2. Review.

13.

Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis.

Roh SH, Kasembeli M, Bakthavatsalam D, Chiu W, Tweardy DJ.

Int J Mol Sci. 2015 Nov 6;16(11):26706-20. doi: 10.3390/ijms161125975. Review.

14.

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

Spiess C, Meyer AS, Reissmann S, Frydman J.

Trends Cell Biol. 2004 Nov;14(11):598-604. Review.

15.

Actinous enigma or enigmatic actin: Folding, structure, and functions of the most abundant eukaryotic protein.

Povarova OI, Uversky VN, Kuznetsova IM, Turoverov KK.

Intrinsically Disord Proteins. 2014 Aug 15;2(1):e34500. doi: 10.4161/idp.34500. eCollection 2014. Review.

16.

Nuclear functions of prefoldin.

Millán-Zambrano G, Chávez S.

Open Biol. 2014 Jul;4(7). pii: 140085. doi: 10.1098/rsob.140085. Review.

17.

Spatial protein quality control and the evolution of lineage-specific ageing.

Nyström T.

Philos Trans R Soc Lond B Biol Sci. 2011 Jan 12;366(1561):71-5. doi: 10.1098/rstb.2010.0282. Review.

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