Stephan Fischer

TL;DR: Modeling studies show that the covalently bound kringle 2 domain in full-length t-PA could interact with an extended hydrophobic groove in the catalytic domain, thus stabilizing the catalytically active conformation without unmasking the Ile276 amino terminus.

TL;DR: Comparisons with the structures of other serine proteinases that also possess Lys156, such as trypsin, factor Xa and human urokinase plasminogen activator (uPA), identify a set of secondary interactions which are required for Lys156 to fulfil this activating role.

TL;DR: The structure determination of the catalytic domain of tissue-type plasminogen activator (tPA) suggests that the side chain of Arg174 is flexible, and does not play a major role in the S4 specificity of tPA, but this residue would modulate S3 specificity, and may be exploited to fine tune the specificity and selectivity of t PA substrates and inhibitors.

TL;DR: It is shown that a fully humanized antibody to IL-1R3 can effectively control inflammation and disease mediated not only byIL-1 but also by IL-33 and IL-36, and concludes that in diseases driven by multiple cytokines, a single antagonistic agent such as a mAb to IL/hR3 is a therapeutic option with considerable translational benefit.

TL;DR: The ability of plasma clot penetration in relation to the achievement of a high in-vivo efficacy of fibrinspecific thrombolytic agents, especially when applied by bolus injection is discussed.