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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: glatz a. 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: glatz a. 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.
Membrane-lipid therapy in operation: the HSP co-inducer BGP-15 activates stress signal transduction pathways by remodeling plasma membrane rafts.
Gombos I, Crul T, Piotto S, Güngör B, Török Z, Balogh G, Péter M, Slotte JP, Campana F, Pilbat AM, Hunya A, Tóth N, Literati-Nagy Z, Vígh L Jr, Glatz A, Brameshuber M, Schütz GJ, Hevener A, Febbraio MA, Horváth I, Vígh L. Gombos I, et al. Among authors: glatz a. PLoS One. 2011;6(12):e28818. doi: 10.1371/journal.pone.0028818. Epub 2011 Dec 12. PLoS One. 2011. PMID: 22174906 Free PMC article.
277 results