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Scandinavian Journal of Immunology|August 26, 1998
Identification of a gliadin T-cell epitope in coeliac disease: general importance of gliadin deamidation for intestinal T-cell recognitionH Sjöström, K E Lundin, O Molberg, et al.
Diabetologia|April 24, 2004
Changes in expression of IL-1 beta influenced proteins in transplanted islets during development of diabetes in diabetes-prone BB ratsT Sparre, U Bjerre Christensen, C F Gotfredsen, et al.
Advances in Experimental Medicine and Biology|January 1, 1996
Characterisation of recombinant isoforms of birch pollen allergen Bet v 1M D Spangfort, H Ipsen, S H Sparholt, et al.
Biochemistry|February 25, 1999
Conserved residues and their role in the structure, function, and stability of acyl-coenzyme A binding proteinB B Kragelund, K Poulsen, K V Andersen, et al.
The Journal of Experimental Medicine|February 24, 2000
The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminaseH Arentz-Hansen, R Körner, O Molberg, et al.
The Journal of Biological Chemistry|September 20, 1997
Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3H H Wandall, H Hassan, E Mirgorodskaya, et al.
Nature Medicine|June 12, 1998
Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac diseaseO Molberg, S N Mcadam, R Körner, et al.
Diabetes|November 15, 2000
Cytokine- or chemically derived nitric oxide alters the expression of proteins detected by two-dimensional gel electrophoresis in neonatal rat islets of LangerhansN E John, H U Andersen, S J Fey, et al.
Diabetes|May 4, 2001
Proteome analysis of interleukin-1beta--induced changes in protein expression in rat islets of LangerhansP M Larsen, S J Fey, M R Larsen, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 13, 1999
A conotoxin from Conus textile with unusual posttranslational modifications reduces presynaptic Ca2+ influxA C Rigby, E Lucas-Meunier, D E Kalume, et al.
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