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Thermal shock proteins

Aujame, L. Firko, H. (1988). The major inducible heat shock protein hsp68 is not required for acquisition of thermal resistance in mouse plasmacytoma cell lines. Mol. Cell. Biol. 8,5486-5494. [Pg.451]

Bansal, G.S., Norton, P.M., Latchman, D.S. (1991). The 90-kDa heat shock protein protects matiunalian cells from thermal stress but not from viral infection. Exp. Cell Res. 195,303-306. [Pg.451]

Li, G.C., Li, L.G., Liu, R.Y., Rehman, M., Lee, W.M. (1992). Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP binding domain. Proc. Natl. Acad. Sci. USA 89,2036-2040. [Pg.457]

McAlister, L. Finkelstein, D.B. (1980). Heat shock proteins and thermal resistance in yeast. Biochem. Biophys. Res. Commun. 93,819-824. [Pg.457]

Some proteins, generally with limited molecular weight, are expressed at high levels as a response to thermal shocks. [Pg.137]

An interesting illustration of the roles played by low-molecular-mass protein stabilizers in assisting cells to cope with heat stress is provided by work of Singer and Lindquist (1998a,b), who examined the complementary roles of the disaccharide trehalose and heat-shock proteins in recovery from thermal stress by the yeast Saccharomyces cerevisiae. Many types of yeast produce high concentrations of... [Pg.340]

Nisbet, E. G. Fowler, C. M. R. 19966. The hydro-thermal imprint on life did heat shock proteins, metalloproteins and photosynthesis begin around hydrothermal vents In MacLeod, C. J., Tyler, P. A. Walker, C. L. (eds) Tectonic, Magmatic, Hydrothermal and Biological Segmentation of Midocean Ridges. Geological Society, London, Special Publications, 118, 239-251. [Pg.306]

Diagram of the peripheral thermal damage after ablative laser treatment. The number of lethal lesions is proportional to the degree of shading. The skin is repaired from peripheral keratinocytes some have suffered sublethal damage. Heat-shock protein (HSP) inducers help improve keratinocyte resistance to heat shock. [Pg.14]

Mueller, U., Perl, D., Schmid, F.X., Heinemann, U. Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein, J. Mol. Biol. 2000,297,975-88. [Pg.30]

However, hundreds of studies and publications reported biological and clinical effects at low-intensity and low-frequency electromagnetic fields, as well as at static magnetic fields. At these interactions it is very unlikely, or even impossible, to expect thermal effects, and the threshold level approach is not reasonable. Several other mechanisms of interactions as ion-pair and free radical formation, heat shock proteins, and cal-cium-calmoduUn interactions have been proposed. One of the most reasonable hypotheses is window hypothesis to be discussed next. [Pg.381]


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