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Items: 1 to 20 of 83

1.

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.

Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D, Hayer-Hartl M, Mann M, Hartl FU.

Cell. 2005 Jul 29;122(2):209-20.

2.
3.

Chaperone-assisted protein folding in the cell cytoplasm.

Houry WA.

Curr Protein Pept Sci. 2001 Sep;2(3):227-44. Review.

PMID:
12369934
4.

Mechanism of substrate recognition by the chaperonin GroEL.

Houry WA.

Biochem Cell Biol. 2001;79(5):569-77. Review.

PMID:
11716298
5.

What distinguishes GroEL substrates from other Escherichia coli proteins?

Azia A, Unger R, Horovitz A.

FEBS J. 2012 Feb;279(4):543-50. doi: 10.1111/j.1742-4658.2011.08458.x. Epub 2012 Jan 4. Review.

6.

Structure and function of the molecular chaperone Trigger Factor.

Hoffmann A, Bukau B, Kramer G.

Biochim Biophys Acta. 2010 Jun;1803(6):650-61. doi: 10.1016/j.bbamcr.2010.01.017. Epub 2010 Feb 2. Review.

7.

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms.

Netzer WJ, Hartl FU.

Trends Biochem Sci. 1998 Feb;23(2):68-73. Review.

PMID:
9538692
8.

Molecular chaperone GroEL/ES: unfolding and refolding processes.

Ryabova NA, Marchenkov VV, Marchenkova SY, Kotova NV, Semisotnov GV.

Biochemistry (Mosc). 2013 Dec;78(13):1405-14. doi: 10.1134/S0006297913130038. Review.

9.

Protein folding assisted by the GroEL/GroES chaperonin system.

Martin J.

Biochemistry (Mosc). 1998 Apr;63(4):374-81. Review.

PMID:
9556520
10.

GroE chaperonin-assisted folding and assembly of dodecameric glutamine synthetase.

Fisher MT.

Biochemistry (Mosc). 1998 Apr;63(4):382-98. Review.

PMID:
9556521
11.

GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future.

Chaudhuri TK, Verma VK, Maheshwari A.

Prog Biophys Mol Biol. 2009 Jan;99(1):42-50. doi: 10.1016/j.pbiomolbio.2008.10.007. Epub 2008 Nov 7. Review.

PMID:
19027782
12.

Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL.

Bhandari V, Houry WA.

Adv Exp Med Biol. 2015;883:271-94. doi: 10.1007/978-3-319-23603-2_15. Review.

PMID:
26621473
13.

GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?

Marchenkov VV, Semisotnov GV.

Int J Mol Sci. 2009 May 12;10(5):2066-83. doi: 10.3390/ijms10052066. Review.

14.

Chaperomics: in vivo GroEL function defined.

Ellis RJ.

Curr Biol. 2005 Sep 6;15(17):R661-3. Review.

15.
16.

La cage aux fold: asymmetry in the crystal structure of GroEL-GroES-(ADP)7.

Harrison CJ.

Structure. 1997 Oct 15;5(10):1261-4. Review.

PMID:
9351802
17.

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
18.

The Escherichia coli groE chaperonins.

Georgopoulos C, Ang D.

Semin Cell Biol. 1990 Feb;1(1):19-25. Review.

PMID:
1983267
19.

Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding?

Craig EA, Eisenman HC, Hundley HA.

Curr Opin Microbiol. 2003 Apr;6(2):157-62. Review.

PMID:
12732306
20.

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.

Todd MJ, Viitanen PV, Lorimer GH.

Science. 1994 Jul 29;265(5172):659-66. Review.

PMID:
7913555
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