J
Jörn M. Werner
Researcher at University of Southampton
Publications - 44
Citations - 1937
Jörn M. Werner is an academic researcher from University of Southampton. The author has contributed to research in topics: Protein structure & Major histocompatibility complex. The author has an hindex of 20, co-authored 43 publications receiving 1823 citations. Previous affiliations of Jörn M. Werner include University of Oxford.
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Journal ArticleDOI
Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders.
TL;DR: A model for the arrangement of fibrillin monomers in microfibrils that reconciles structural and antibody binding data is proposed, and a set of disease-causing mutations are described that provide the first clues to the specificity of cbEFG interactions.
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A peptide inhibitor of HIV-1 assembly in vitro.
Jana Sticht,Michael Humbert,Stuart C. Findlow,Jochen Bodem,Barbara Müller,Ursula Dietrich,Jörn M. Werner,Hans-Georg Kräusslich +7 more
TL;DR: A 12-mer peptide, capsid assembly inhibitor (CAI), that binds the capsid (CA) domain of Gag and inhibits assembly of immature- and mature-like capsid particles in vitro.
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Structural and functional properties of the human notch-1 ligand binding region.
Sophie Hambleton,N V Valeyev,A. Muranyi,V Knott,Jörn M. Werner,Andrew J. McMichael,Penny A. Handford,A K Downing +7 more
TL;DR: A model of the 36 EGF modules of the Notch extracellular domain is constructed that enables predictions to be made about the general role of calcium binding to this region and proposes this arrangement to be prototypical of a distinct class of EGF linkages.
Journal ArticleDOI
Localization and characterization of the hyaluronan-binding site on the Link module from human TSG-6
Jan D. Kahmann,Ronan O'Brien,Jörn M. Werner,Dick Heinegård,John E. Ladbury,Iain D. Campbell,Anthony J. Day +6 more
TL;DR: In TSG-6 a single Link module is sufficient for a high-affinity interaction with HA, and there is no evidence for the involvement of linear sequence motifs in HA binding.
Journal ArticleDOI
Molecular Recognition of Paxillin LD Motifs by the Focal Adhesion Targeting Domain
Maria K. Hoellerer,Martin E.M. Noble,Gilles Labesse,Iain D. Campbell,Jörn M. Werner,Stefan T. Arold +5 more
TL;DR: The molecular basis for the recognition of two paxillin LD motifs by the FA targeting (FAT) domain of FA kinase is determined using a combination of X-ray crystallography, solution NMR, and homology modeling.