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Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a "fluidity gene".
Horváth I, Glatz A, Varvasovszki V, Török Z, Páli T, Balogh G, Kovács E, Nádasdi L, Benkö S, Joó F, Vígh L. Horváth I, et al. Among authors: balogh g. Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3513-8. doi: 10.1073/pnas.95.7.3513. Proc Natl Acad Sci U S A. 1998. PMID: 9520397 Free PMC article.
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. Among authors: balogh g. 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.
"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. Among authors: balogh g. Arch Biochem Biophys. 2005 Apr 15;436(2):346-54. doi: 10.1016/j.abb.2005.02.018. Arch Biochem Biophys. 2005. PMID: 15797247
293 results