scispace - formally typeset
U

Udo Oppermann

Researcher at University of Oxford

Publications -  284
Citations -  18730

Udo Oppermann is an academic researcher from University of Oxford. The author has contributed to research in topics: Dehydrogenase & Reductase. The author has an hindex of 68, co-authored 269 publications receiving 16673 citations. Previous affiliations of Udo Oppermann include University of Marburg & National Institutes of Health.

Papers
More filters
Journal ArticleDOI

Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility

David M. Evans, +92 more
- 01 Aug 2011 - 
TL;DR: In this paper, the identification of three variants in the RUNX3, LTBR-TNFRSF1A and IL12B regions convincingly associated with ankylosing spondylitis (P < 5 x 10(-8) in the combined discovery and replication datasets) and a further four loci at PTGER4, TBKBP1, ANTXR2 and CARD9 that show strong association across all their datasets (p < 5x 10(-6) overall, with support in each of the three datasets studied).
Journal ArticleDOI

Protein production and purification.

Susanne Gräslund, +86 more
- 01 Feb 2008 - 
TL;DR: This review presents methods that could be applied at the outset of any project, a prioritized list of alternate strategies and a list of pitfalls that trip many new investigators.
Journal ArticleDOI

Medium- and short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes

TL;DR: The conserved fold and nucleotide binding emphasize the role of SDRs as scaffolds for an NAD(P)(H) redox sensor system, of importance to control metabolic routes, transcription and signalling.
Journal ArticleDOI

Short-chain dehydrogenases/reductases (SDR): the 2002 update.

TL;DR: A catalytic tetrad of Asn-Ser-Tyr-Lys residues is established, which presumably form the framework for a proton relay system including the 2'-OH of the nicotinamide ribose, similar to the mechanism found in horse liver ADH.