50 Jahre Neubau Universitätsbibliothek Stuttgart 2011

T e i l 1 Impressum, Sponsoren - Seite 4 Stephan, Werner: Einleitung und Dank - Seite 9 Einfachheit in Form und Material - less is more: Klaus-Jürgen Zabel über den Bau der Universitätsbibliothek (Interview mit Ottmar Pertschi und Christiane Rambach) - Seite 13 Paulus, Stefan: Amerika als Vorbild? Anmerkungen zu den politischen und kulturhistorischen Bedingungen an (west)deutschen Universitäten in den 1950er Jahren - Seite 19 Hering, Jürgen: Max Kade und die Technische Hochschule Stuttgart - Seite 41 Becker, Norbert: Die Technische Hochschule Stuttgart und ihre Bibliothek in der Nachkriegszeit - Seite 63 T e i l 2 Rambach, Christiane: Eine Bibliothek sucht ihren Standort - Seite 75 T e i l 3 Rambach, Christiane: Architekten auf Reisen: "new standards in library design" in Stuttgart - Seite 97 T e i l 4 Philipp, Klaus Jan: Die Universitätsbibliothek im architekturgeschichtlichen Kontext - Seite 125 Huster-Braumann, Henriette: Maximilian Debus: die Universitätsbibliothek und ihre Schrift - Seite 145 T e i l 5 Jost, Holger; Stürzebecher, Jörg: Moderate Moderne: Innenraumgestaltung der Universitätsbibliothek Stuttgart - Seite 153 T e i l 6 Küster, Bärbel: Kunst und Konsens 1958 - 1962: zur Ankaufsgeschichte der Plastik von Hans Uhlmann für die Universitätsbibliothek Stuttgart - Seite 171 Szymczyk-Eggert, Elisabeth: Die Zweigbibliothek auf dem Campus in Stuttgart-Vaihingen: vom Provisorium zur Dauereinrichtung - Seite 191 T e i l 7 Stephan, Werner: Bibliotheken der Zukunft - Seite 221 T e i l 8 Anhang: Architekten der Universitätsbibliothek: Volkart, Zabel, Klauss und Koschlig (Christiane Rambach) - Seite 233 Richtfest am 31. Juli 1959 (Schwäbisches Stück zum Richtfest der THB am 31. Juli 1959 von Hans Volkart - Richtspruch des Zimmerpoliers der AG Kübler und Züblin zum Richtfest der Universitätsbibliothek am 31. Juli 1959) - Seite 237 "Es lebe die Bibliothek!" Interne Bibliothekseinweihung am 17. Februar 1962 - Seite 243 Skizzen (Gedanken zu einem Anbau an die Universitätsbibliothek Stuttgart von Klaus-Jürgen Zabel 2011 - Ihre Universitätsbibliothek zum Selberbauen von Stefan Pertschi) - Seite 247 Literatur zum Bau der Universitätsbibliothek Stuttgart (eine Auswahl - Christiane Rambach) - Seite 253 Abkürzungsverzeichnis, Abbildungsnachweise - Seite 258 Namen- und Sachregister (Ottmar Pertschi) - Seite 263 Autorenverzeichnis - S. 27

Isolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle Tick

Inhibitors of coagulation factors from blood-feeding animals display a wide variety of structural motifs and inhibition mechanisms. We have isolated a novel inhibitor from the cattle tick Boophilus microplus, one of the most widespread parasites of farm animals. The inhibitor, which we have termed boophilin, has been cloned and overexpressed in Escherichia coli. Mature boophilin is composed of two canonical Kunitz-type domains, and inhibits not only the major procoagulant enzyme, thrombin, but in addition, and by contrast to all other previously characterised natural thrombin inhibitors, significantly interferes with the proteolytic activity of other serine proteinases such as trypsin and plasmin. The crystal structure of the bovine α-thrombin·boophilin complex, refined at 2.35 Å resolution reveals a non-canonical binding mode to the proteinase. The N-terminal region of the mature inhibitor, Q16-R17-N18, binds in a parallel manner across the active site of the proteinase, with the guanidinium group of R17 anchored in the S1 pocket, while the C-terminal Kunitz domain is negatively charged and docks into the basic exosite I of thrombin. This binding mode resembles the previously characterised thrombin inhibitor, ornithodorin which, unlike boophilin, is composed of two distorted Kunitz modules. Unexpectedly, both boophilin domains adopt markedly different orientations when compared to those of ornithodorin, in its complex with thrombin. The N-terminal boophilin domain rotates 9° and is displaced by 6 Å, while the C-terminal domain rotates almost 6° accompanied by a 3 Å displacement. The reactive-site loop of the N-terminal Kunitz domain of boophilin with its P1 residue, K31, is fully solvent exposed and could thus bind a second trypsin-like proteinase without sterical restraints. This finding explains the formation of a ternary thrombin·boophilin·trypsin complex, and suggests a mechanism for prothrombinase inhibition in vivo

Inhibitors of benzamidine type influence the virulence properties of Porphyromonas gingivalis strains.

Synthetic inhibitors of benzamidine type have been found to have inhibiting effects on arginine specific cysteine proteinases of P. gingivalis. The purpose of our study was to assess the effects of these inhibitors on the virulence properties of two P. gingivalis strains, the reference strain ATCC 33277 and JH16-1, a clinical isolate obtained from a patient with severe periodontitis. The inhibitors tested were pentamidine, benzamidine, three bis-benzamidine derivatives with a pentamidine-related structure, one bis-benzamidine derivative with another structure, and one arginine derivative as a negative control, each in the concentrations of 2 μM and 20 μM. As virulence criteria the following parameters were determined : arginine-specific amidolytic activity, growth inhibition, hemagglutination of sheep erythrocytes, adherence to KB cells and immuno-phagocytosis including intracellular killing. Pentamidine and the bis-benzamidine derivatives with pentamidine-related structure showed the most remarkable effects on reduction of amidolytic activity by 35%, growth inhibition and reduced hemagglutination. Except for the arginine derivative all other inhibitors tested enhanced the phagocytosis capacities of granulocytes. No clear influence of the inhibitors on adherence of P. gingivalis to KB cells was seen. Although in vitro effects of the synthetic inhibitors of cysteine proteinases on virulence of P. gingivalis were observed further in vitro tests concerning immunomodulatory effects should be done before these substances are used for therapy in clinically controlled studies