Synechocystis HSP17 is an Amphitropic Protein That Stabilizes Heat-Stressed Membranes and Binds Denatured Proteins for Subsequent Chaperone-Mediated Refolding von Török, Zsolt, Goloubinoff, Pierre, Horváth, Ibolya, Tsvetkova, Nelly M., Glatz, Attila, Balogh, Gábor, Varvasovszki, Viktória, Los, Dmitry A., Vierling, Elizabeth, Crowe, John H., Vigh, László

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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 von Horvath, Ibolya, Glatz, Attila, Varvasovszki, Viktoria, Torok, Zsolt, Pali, Tibor, Balogh, Gabor, Kovacs, Eszter, Nadasdi, Levente, Benko, Sandor, Joo, Ferenc, Vigh, Laszlo

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The Chaperonins of Synechocystis PCC 6803 Differ in Heat Inducibility and Chaperone Activity von Kovács, Eszter, van der Vies, Saskia M., Glatz, Attila, Török, Zsolt, Varvasovszki, Viktória, Horváth, Ibolya, Vígh, László

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Only one dnaK homolog, dnaK2, is active transcriptionally and is essential in Synechocystis von Varvasovszki, Viktória, Glatz, Attila, Shigapova, Natalia, Jósvay, Katalin, Vı́gh, László, Horváth, Ibolya

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Chaperonin Genes of theSynechocystisPCC 6803 Are Differentially Regulated under Light–Dark Transition during Heat Stress von Glatz, Attila, Horváth, Ibolya, Varvasovszki, Viktória, Kovács, Eszter, Török, Zsolt, Vigh, László

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Chaperonin genes of the Synechocystis PCC 6803 are differentially regulated under light-dark transition during heat stress von Glatz, A, Horváth, I, Varvasovszki, V, Kovács, E, Török, Z, Vigh, L

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