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Numrering	Referens	Omslagsbild	Hitta
1.	Pedersen, TR, et al. (författare) Cholesterol lowering and the use of healthcare resources. Results of the Scandinavian Simvastatin Survival Study 1996 Ingår i: Circulation. - 0009-7322. ; 93:10, s. 1796-1802 Tidskriftsartikel (refereegranskat)
2.	Cedervall, T, et al. (författare) Allosteric and temperature effects on the plasma protein binding by streptococcal M protein family members 1995 Ingår i: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 42:4, s. 41-433 Tidskriftsartikel (refereegranskat)abstract Most group A streptococcal strains bind immunoglobulins (Ig) and fibrinogen to their cell walls. It is shown in this paper that the Ig-binding of three different strains was much weaker at 37 degrees C than at room temperature (20 degrees C), whereas the fibrinogen binding was unaffected by temperature. The binding properties and molecular sizes of two purified group A streptococcal cell surface proteins from the M protein family were studied at various temperatures, M1 protein with affinity for IgG, fibrinogen and albumin, and protein Sir22 with affinity for IgA and IgG. Both proteins appeared as monomers which bound all their ligands, including fibrinogen, very weakly at 37 degrees C, and as strongly binding dimers at 10 and 20 degrees C. Furthermore, the results demonstrated that the plasma protein binding of the bacterial proteins was allosterically regulated, i.e. the binding of a ligand to one site modulated the binding of a ligand to a second site. For example, the binding of albumin or IgG to purified M1 protein at 10 and 20 degrees C strongly enhanced the binding of fibrinogen at 37 degrees C. This indicates that the high affinity dimer form of the bacterial proteins can be stabilized at 37 degrees C, a possible explanation for the strong fibrinogen binding of whole bacteria. Finally, the sizes and binding properties of three M1 protein fragments were studied and the results indicated that the centrally located C-repeats, which are conserved among the members of the M protein family, are important for the formation of the high-affinity dimers of the bacterial proteins.

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Typ av publikation: tidskriftsartikel (2)

Typ av innehåll: refereegranskat (2)

Författare/redaktör: Cook, J. (1); Nilsson, J. (1); Andersson, K (1); Holm, T (1); Larsson, O (1); Aukrust, P. (1); visa fler...; Wagner, V. (1); Jorgensen, C. (1); Nielsen, H (1); Malmberg, K (1); Svensson, L (1); Karlsson, L (1); Kjekshus, J (1); Nilsson, O (1); Miettinen, H. (1); Andersson, G (1); Wagner, F. (1); Jonsson, B (1); Persson, S (1); Torp, R (1); Hansson, E (1); Nielsen, L (1); Johansen, T (1); Olsson, A (1); Linden, T. (1); Sundstrom, M (1); Thompson, S (1); Frisell, J (1); Jensen, S (1); Soderstrom, M (1); Stenberg, L (1); Johansson, S (1); Andreasson, M (1); Bergman, E (1); Boman, K. (1); Jonsson, E (1); Olsson, C (1); Svensson, O (1); Hansson, A (1); Ahlberg, G (1); Cook, T (1); Jansson, T (1); Akerström, B (1); Gustafsson, E. (1); Thoresen, L (1); Hoglund, C (1); Hedman, A (1); Sjogren, A (1); Andersen, G. (1); Thomsen, H (1); visa färre...

Lärosäte: Lunds universitet (1); Karolinska Institutet (1)

Språk: Engelska (2)

Forskningsämne (UKÄ/SCB): Medicin och hälsovetenskap (1)

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