Prostaglandin E2 regulates Th17 cell differentiation and function through cyclic AMP and EP2/EP4 receptor signaling

Autor: Robert A. Kastelein, Kristian Sass Bak-Jensen, Daniel J. Cua, Brent S. McKenzie, Wendy M. Blumenschein, Katia Boniface, Rene de Waal Malefyt, Ying Li, Mandy J. McGeachy, Terrill K. McClanahan

Publikováno v: The Journal of Experimental Medicine

Prostaglandins, particularly prostaglandin E2 (PGE2), play an important role during inflammation. This is exemplified by the clinical use of cyclooxygenase 2 inhibitors, which interfere with PGE2 synthesis, as effective antiinflammatory drugs. Here,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4753a63e30ed560852402ca28730f206
http://europepmc.org/articles/PMC2699124

TGF-β and IL-6 drive the production of IL-17 and IL-10 by T cells and restrain TH-17 cell–mediated pathology

Autor: Wendy M. Blumenschein, Yi Chen, Mandy J. McGeachy, Terrill K. McClanahan, Daniel J. Cua, Kristian Sass Bak-Jensen, Cristina M. Tato

Publikováno v: Nature Immunology. 8:1390-1397

Studies have shown that transforming growth factor-beta (TGF-beta) and interleukin 6 (IL-6) are required for the lineage commitment of pathogenic IL-17-producing T helper cells (T(H)-17 cells). Unexpectedly, here we found that stimulation of myelin-r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b5cd4f82e822ca575ad1ca731a8d7c77
https://doi.org/10.1038/ni1539

Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome

Autor: Kristian Sass Bak-Jensen, Sabrina Laugesen, Peter Roepstorff, Christine Finnie, Birte Svensson

Publikováno v: Finnie, C, Bak-Jensen, K S, Laugesen, S, Roepstorff, P & Svensson, B 2006, ' Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome ', Plant Science, vol. 170, pp. 808-821 . https://doi.org/10.1016/j.plantsci.2005.11.012

Proteome analysis of mature barley (Hordeum vulgare subsp. vulgare) seeds has led to the identification of proteins in about 450 spots on 2D-gels. To shed light on the role of some of these proteins, their temporal appearance was monitored over 5 wee

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e06d14aa530c35dac59c09b4aebbc599
https://doi.org/10.1016/j.plantsci.2005.11.012

Engineering of Barley α-Amylase

Autor: Birte Svensson, S. Bozonnet, T.-J. Kim, Peter Kresten Nielsen, Birgit C. Bønsager, Kristian Sass Bak-Jensen, Birte Kramhøft

Publikováno v: Biocatalysis and Biotransformation. 21:209-214

Protein engineering of barley α-amylase addressed the roles of Ca2+ in activity and inhibition by barley α-amylase/subtilisin inhibitor (BASI), multiple attach in polysaccharide hydrolysis, secondary starch binding sites, and BASI hot spots in AMY2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a9ade7f9c38fade48111829e002481b
https://doi.org/10.1080/10242470310001618564

Barley α-amylase Met53 situated at the high-affinity subsite −2 belongs to a substrate binding motif in the β→α loop 2 of the catalytic (β/α)8-barrel and is critical for activity and substrate specificity

Autor: Kristian Sass Bak-Jensen, Birte Svensson, Haruhide Mori

Publikováno v: European Journal of Biochemistry. 269:5377-5390

Met53 in barley α-amylase 1 (AMY1) is situated at the high-affinity subsite -2. While Met53 is unique to plant α-amylases, the adjacent Tyr52 stacks onto substrate at subsite - I and is essentially invariant in glycoside hydrolase family 13. These

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::839604e7f8c4e91510883397034769f2
https://doi.org/10.1046/j.1432-1033.2002.03185.x