Dallas Bower: a producer for television's early years, 1936-39

Having worked in the film industry as a sound technician and then director, Dallas Bower (1907-99) was appointed in 1936 as one of two senior producers at the start of the BBC Television service. Over the next three years Bower produced as well as directed many ground-breaking live programmes, including the opening-day broadcast on 2 November 1936; the BBC Television Demonstration Film (1937, his only surviving pre-war production); a modern-dress Julius Caesar (1938), in uniforms suggestive of a Fascist disctatorship; Act II of Tristan and Isolde (1938); Patrick Hamilton’s play Rope (1939), utilising extended single camera-shots camera-shots; numerous ballets, among them Checkmate (1938); and ambitious outside broadcasts from the film studios at Denham and Pinewood. Developing the working practices of producing for the theatre, film industry and radio, Bower was a key figure in defining the role of the creative television producer at the start of the medium. Among his innovations, according to his unpublished autobiographical fragment ‘Playback’ (written 1995), was the introduction of a drawn studio plan for the four cameras employed in all live broadcasts from Alexandra Palace. Using Bower’s writings (among them his 1936 book Plan for Cinema), his BECTU History Project interview, the BBC Written Archives and contemporary industry coverage, this article reconstructs the early development of the role of staff television producer in order to consider the questions of autonomy, agency and institutional constraints at the BBC in the pre-war years

The classical composers and recordings /

Van Elslander, Antoni

Madingley Hall : a short history and description of the hall and estate, their owners and occupiers /

Previous ed. 1961

MAA868, a novel FXI antibody with a unique binding mode, shows durable effects on markers of anticoagulation in humans

A large unmet medical need exists for safer antithrombotic drugs because all currently approved anticoagulant agents interfere with hemostasis, leading to an increased risk of bleeding. Genetic and pharmacologic evidence in humans and animals suggests that reducing factor XI (FXI) levels has the potential to effectively prevent and treat thrombosis with a minimal risk of bleeding. We generated a fully human antibody (MAA868) that binds the catalytic domain of both FXI (zymogen) and activated FXI. Our structural studies show that MAA868 traps FXI and activated FXI in an inactive, zymogen-like conformation, explaining its equally high binding affinity for both forms of the enzyme. This binding mode allows the enzyme to be neutralized before entering the coagulation process, revealing a particularly attractive anticoagulant profile of the antibody. MAA868 exhibited favorable anticoagulant activity in mice with a dose-dependent protection from carotid occlusion in a ferric chloride-induced thrombosis model. MAA868 also caused robust and sustained anticoagulant activity in cynomolgus monkeys as assessed by activated partial thromboplastin time without any evidence of bleeding. Based on these preclinical findings, we conducted a first-in-human study in healthy subjects and showed that single subcutaneous doses of MAA868 were safe and well tolerated. MAA868 resulted in dose- and time-dependent robust and sustained prolongation of activated partial thromboplastin time and FXI suppression for up to 4 weeks or longer, supporting further clinical investigation as a potential once-monthly subcutaneous anticoagulant therapy