| 1. |
- Arvastson, Gösta, et al.
(author)
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Det urbana rummet
- 1999
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Book (pop. science, debate, etc.)
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| 2. |
- Arvastson, Gösta, Lennartsson, Rebecka, Andersson, Maria, Zackariasson, Maria, Ljung, Anna , Ek-Nilsson, Katarina, Mebius, Anders, Vallström, Mikael
(author)
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Järnbur eller frigörelse.Studier i moderniseringen av Sverige.
- 1999
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Book (other academic/artistic)
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| 3. |
- Hamid, Nivia, et al.
(author)
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YopH dephosphorylates Cas and Fyn-binding protein in macrophages
- 1999
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In: Microbial Pathogenesis. - : Academic Press. - 0882-4010 .- 1096-1208. ; 27:4, s. 231-242
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Journal article (peer-reviewed)abstract
- The tyrosine phosphatase YopH is an essential virulence effector of pathogenic Yersinia spp. YopH, which is translocated from extracellularly located bacteria into interacting target cells, blocks phagocytosis by professional phagocytes. We show here that immunoprecipitation of YopH from lysates of J774 cells infected with Y. pseudotuberculosis expressing an inactive form of YopH resulted in co-precipitation of certain phosphotyrosine proteins. The association between the inactive YopH and phosphotyrosine proteins in the 120 kDa range was rapid and could be detected after 2 min of infection. The proteins were identified as the docking proteins Cas and Fyn-binding protein (FYB). Upon infection of J774 cells with Y. pseudotuberculosis lacking YopH expression both of these proteins became tyrosine phosphorylated. Moreover, this infection caused recruitment of Cas to peripheral focal complexes, and FYB was relocalized to areas surrounding these structures. Both Cas and FYB became dephosphorylated upon infection with Y. pseudotuberculosis expressing active YopH, and this was associated with disruption of focal complexes. With regard to the previous identification of Cas and focal complexes as targets of YopH in HeLa cells, the present study supports an important role for these targets in a general mechanism of bacterial uptake.
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| 4. |
- Lobell, Anna, et al.
(author)
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Vaccination with DNA encoding an immunodominant myelin basic protein peptide targeted to Fc of immunoglobulin G suppresses experimental autoimmune encephalomyelitis
- 1998
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In: Journal of Experimental Medicine. - : Rockefeller University Press. - 0022-1007 .- 1540-9538. ; 187:9, s. 1543-1548
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Journal article (peer-reviewed)abstract
- We explore here if vaccination with DNA encoding an autoantigenic peptide can suppress autoimmune disease. For this purpose we used experimental autoimmune encephalomyelitis (EAE), which is an autoaggressive disease in the central nervous system and an animal model for multiple sclerosis. Lewis rats were vaccinated with DNA encoding an encephalitogenic T cell epitope, guinea pig myelin basic protein peptide 68-85 (MBP68-85), before induction of EAE with MBP68-85 in complete Freund's adjuvant. Compared to vaccination with a control DNA construct, the vaccination suppressed clinical and histopathological signs of EAE, and reduced the interferon gamma production after challenge with MBP68-85. Targeting of the gene product to Fc of IgG was essential for this effect. There were no signs of a Th2 cytokine bias. Our data suggest that DNA vaccines encoding autoantigenic peptides may be useful tools in controlling autoimmune disease.
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