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Results: 1 to 20 of 141

Related Citations for PubMed (Select 23167595)

1.

Cumulative impact of chaperone-mediated folding on genome evolution.

Bogumil D, Dagan T.

Biochemistry. 2012 Dec 18;51(50):9941-53. doi: 10.1021/bi3013643. Epub 2012 Dec 10. Review.

PMID:
23167595
2.

Microbial molecular chaperones.

Lund PA.

Adv Microb Physiol. 2001;44:93-140. Review.

PMID:
11407116
3.

ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.

Thomas JG, Baneyx F.

Mol Microbiol. 2000 Jun;36(6):1360-70.

PMID:
10931286
4.
5.

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function.

Cheetham ME, Caplan AJ.

Cell Stress Chaperones. 1998 Mar;3(1):28-36. Review. No abstract available.

6.

A chaperone network controls the heat shock response in E. coli.

Guisbert E, Herman C, Lu CZ, Gross CA.

Genes Dev. 2004 Nov 15;18(22):2812-21.

7.

Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses.

Diamant S, Eliahu N, Rosenthal D, Goloubinoff P.

J Biol Chem. 2001 Oct 26;276(43):39586-91. Epub 2001 Aug 21.

8.

Molecular chaperones--cellular machines for protein folding.

Walter S, Buchner J.

Angew Chem Int Ed Engl. 2002 Apr 2;41(7):1098-113. Review.

PMID:
12491239
9.

Protein folding in vivo: the importance of molecular chaperones.

Feldman DE, Frydman J.

Curr Opin Struct Biol. 2000 Feb;10(1):26-33. Review.

PMID:
10679467
10.
11.

The roles of molecular chaperones in vivo.

Lund PA.

Essays Biochem. 1995;29:113-23. Review.

PMID:
9189716
12.

Limits of protein folding inside GroE complexes.

Grallert H, Rutkat K, Buchner J.

J Biol Chem. 2000 Jul 7;275(27):20424-30.

13.

Chaperone-assisted protein folding in the cell cytoplasm.

Houry WA.

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

PMID:
12369934
14.

Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.

Saibil H.

Curr Opin Struct Biol. 2000 Apr;10(2):251-8. Review.

PMID:
10753820
15.

Hop: more than an Hsp70/Hsp90 adaptor protein.

Odunuga OO, Longshaw VM, Blatch GL.

Bioessays. 2004 Oct;26(10):1058-68. Review.

PMID:
15382137
16.

Roles of molecular chaperones in protein misfolding diseases.

Barral JM, Broadley SA, Schaffar G, Hartl FU.

Semin Cell Dev Biol. 2004 Feb;15(1):17-29. Review.

PMID:
15036203
17.

Roles of heat-shock chaperones in the production of recombinant proteins in Escherichia coli.

Hoffmann F, Rinas U.

Adv Biochem Eng Biotechnol. 2004;89:143-61. Review.

PMID:
15217158
18.

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.

Mattoo RU, Goloubinoff P.

Cell Mol Life Sci. 2014 Sep;71(17):3311-25. doi: 10.1007/s00018-014-1627-y. Epub 2014 Apr 24. Review.

19.

Between genotype and phenotype: protein chaperones and evolvability.

Rutherford SL.

Nat Rev Genet. 2003 Apr;4(4):263-74. Review.

PMID:
12671657
20.

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.

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