Homogenization of the long-term global ozonesonde records

Póster presentado en: WMO Technical Conference on Meteorological and Environmental Instruments and Methods of Observation celebrada del 10 al 13 de octubre de 2022 en París

Defining the beats in the TV sitcom

The sitcom is distinguished from drama or soap opera by having what is described as a closed or “circular” narrative structure wherein the plot returns to the original stasis, defined by Curtis as the re-situation (1982). In my book Situation Comedy, Character, and Psychoanalysis: On the Couch with Lucy, Basil, and Kimmie (2018), I analysed character behaviour to argue that the protagonist, in their attempt to dispel or deny the incident that has triggered the story, shapes the narrative in a way that reflects the “entrapment” of the show’s characters, a defining characteristic of this form of comedy (Mills 2005; Mintz 1985). While I argued that the sitcom begins with character, I now extend that premise to posit that the comedy emerges from the character’s reaction/actions to events that threaten their sense of self articulated at an early stage of script development: the beat sheet. In this chapter, I critically examine a beat sheet from one of my own pilots, At the Bar (2016), to determine how beats inform the shape of the narrative structure in this form of comedy

Au-delà du principe d'identité (compréhension et être au monde)

NANTERRE-BU PARIS10 (920502102) / SudocSudocFranceGermanyFRD

The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly.

The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional solution structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The protein contains four alpha-helices that are structurally similar to the known type C MA structures. This similarity implies possible common assembly units and membrane-binding mechanisms for type C and B/D retroviruses. In addition to this, the interpretation of mutagenesis data has enabled us to identify, for the first time, the structural basis of a putative intracellular targeting motif