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A. Heine
Researcher at Martin Luther University of Halle-Wittenberg
Publications - 7
Citations - 456
A. Heine is an academic researcher from Martin Luther University of Halle-Wittenberg. The author has contributed to research in topics: Carbonic anhydrase II & Sulfonamide. The author has an hindex of 3, co-authored 7 publications receiving 435 citations. Previous affiliations of A. Heine include University of Florence.
Papers
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Journal ArticleDOI
Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition
Alexander Weber,Angela Casini,A. Heine,Daniel Kuhn,Claudiu T. Supuran,and Andrea Scozzafava,Gerhard Klebe +6 more
TL;DR: An unexpected nanomolar affinity is demonstrated of the COX-2 specific arylsulfonamide-type celecoxib and valdecoxib for isoenzymes of the totally unrelated carbonic anhydrase (CA) family, such as CA I, II, IV, and IX, whereas the rofecoxib methyl sulfone-type has no effect.
ComponentDOI
Fragments Can Bind Either More Enthalpy or Entropy-Driven: Crystal Structures and Residual Hydration Pattern Suggest Why.
Journal ArticleDOI
Hydroxyethylene sulfones as a new scaffold to address aspartic proteases: design, synthesis, and structural characterization.
Edgar Specker,Jark Böttcher,A. Heine,Christoph A. Sotriffer,Hauke Lilie,Andreas Schoop,Gerhard Müller,Nils Griebenow,Gerhard Klebe +8 more
TL;DR: The stereoisomeric hydroxyethylene sulfones developed as novel scaffolds against aspartyl proteases against cathepsin D and beta-secretase did not reveal significant inhibition, most likely because the latter proteases require inverted configuration at the hydroxy group.
Patent
Crystal structure of blood coagulation factor XIIIa
Martin Hils,Ralf Pasternack,Christian Büchold,Johannes Weber,A. Heine,Gerhard Klebe,Martin Stieler +6 more
TL;DR: In this paper, the crystal forms of blood coagulation factor XIIIa, crystal structure information obtained from them, methods of preparing such crystal forms, their use for the identification and / or design of inhibitors of the factor, and methods for identifying, optimizing and designing compounds which should have the ability to interact with or inhibit the factor.