Similar articles for PMID: 12368478

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1

Small heat-shock proteins regulate membrane lipid polymorphism.

Tsvetkova NM, Horváth I, Török Z, Wolkers WF, Balogi Z, Shigapova N, Crowe LM, Tablin F, Vierling E, Crowe JH, Vigh L. Tsvetkova NM, et al. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13504-9. doi: 10.1073/pnas.192468399. Epub 2002 Oct 4. Proc Natl Acad Sci U S A. 2002. PMID: 12368478 Free PMC article.

2

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding.

Török Z, Goloubinoff P, Horváth I, Tsvetkova NM, Glatz A, Balogh G, Varvasovszki V, Los DA, Vierling E, Crowe JH, Vigh L. Török Z, et al. Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3098-103. doi: 10.1073/pnas.051619498. Epub 2001 Feb 27. Proc Natl Acad Sci U S A. 2001. PMID: 11248038 Free PMC article.

3

Wrapping the alpha-crystallin domain fold in a chaperone assembly.

Stamler R, Kappé G, Boelens W, Slingsby C. Stamler R, et al. J Mol Biol. 2005 Oct 14;353(1):68-79. doi: 10.1016/j.jmb.2005.08.025. J Mol Biol. 2005. PMID: 16165157

4

"Heat shock lipid" in cyanobacteria during heat/light-acclimation.

Balogi Z, Török Z, Balogh G, Jósvay K, Shigapova N, Vierling E, Vígh L, Horváth I. Balogi Z, et al. Arch Biochem Biophys. 2005 Apr 15;436(2):346-54. doi: 10.1016/j.abb.2005.02.018. Arch Biochem Biophys. 2005. PMID: 15797247

5

Lipids, proteins, and their interplay in the dynamics of temperature-stressed membranes of a cyanobacterium, Synechocystis PCC 6803.

Laczkó-Dobos H, Szalontai B. Laczkó-Dobos H, et al. Biochemistry. 2009 Oct 27;48(42):10120-8. doi: 10.1021/bi9011034. Biochemistry. 2009. PMID: 19788309

6

Site-directed mutations within the core "alpha-crystallin" domain of the small heat-shock protein, human alphaB-crystallin, decrease molecular chaperone functions.

Muchowski PJ, Wu GJ, Liang JJ, Adman ET, Clark JI. Muchowski PJ, et al. J Mol Biol. 1999 Jun 4;289(2):397-411. doi: 10.1006/jmbi.1999.2759. J Mol Biol. 1999. PMID: 10366513

7

The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions.

Xi D, Wei P, Zhang C, Lai L. Xi D, et al. Proteins. 2014 Jul;82(7):1156-67. doi: 10.1002/prot.24480. Epub 2013 Dec 6. Proteins. 2014. PMID: 24243469

8

Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization.

Chen J, Feige MJ, Franzmann TM, Bepperling A, Buchner J. Chen J, et al. J Mol Biol. 2010 Apr 23;398(1):122-31. doi: 10.1016/j.jmb.2010.02.022. Epub 2010 Feb 18. J Mol Biol. 2010. PMID: 20171228

9

Differential scanning calorimetric study of the interaction of cholesterol with the major lipids of the Acholeplasma laidlawii B membrane.

McMullen TP, Wong BC, Tham EL, Lewis RN, McElhaney RN. McMullen TP, et al. Biochemistry. 1996 Dec 24;35(51):16789-98. doi: 10.1021/bi962098t. Biochemistry. 1996. PMID: 8988017

10

Effect of independent variations in fatty acid structure and chain length on lipid polar headgroup composition in Acholeplasma laidlawii B membranes: regulation of lamellar/nonlamellar phase propensity.

Yue AW, Wong BC, Rieder J, Lewis RN, Mannock DA, McElhaney RN. Yue AW, et al. Biochemistry. 2003 Feb 11;42(5):1309-17. doi: 10.1021/bi026923j. Biochemistry. 2003. PMID: 12564934

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