Chapter Virtual Heritage e musei scientifici: il progetto “Beccari in 3D” per le Collezioni Botaniche del Museo di Storia Naturale dell’Università di Firenze

The 43rd UID conference, held in Genova, takes up the theme of ‘Dialogues’ as practice and debate on many fundamental topics in our social life, especially in these complex and not yet resolved times. The city of Genova offers the opportunity to ponder on the value of comparison and on the possibilities for the community, naturally focused on the aspects that concern us, as professors, researchers, disseminators of knowledge, or on all the possibile meanings of the discipline of representation and its dialogue with ‘others’, which we have broadly catalogued in three macro areas: History, Semiotics, Science / Technology. Therefore, “dialogue” as a profitable exchange based on a common language, without which it is impossible to comprehend and understand one another; and the graphic sign that connotes the conference is the precise transcription of this concept: the title ‘translated’ into signs, derived from the visual alphabet designed for the visual identity of the UID since 2017. There are many topics which refer to three macro sessions: - Witnessing (signs and history) - Communicating (signs and semiotics) - Experimenting (signs and sciences) Thanks to the different points of view, an exceptional resource of our disciplinary area, we want to try to outline the prevailing theoretical-operational synergies, the collaborative lines of an instrumental nature, the recent updates of the repertoires of images that attest and nourish the relations among representation, history, semiotics, sciences

REM: Automatic for the People

We present the result of a year-long effort to think, design, build, realize, and manage the robotic, autonomous REM observatory, placed since June 2003 on the cerro La Silla, ESO Chile. The various aspects of the management and control are here surveyed, with the nice ideas and the wrong dead ends we encountered under way. Now REM is offered to the international astronomical community, a real, schedulable telescope, automatic for the People

the rem observing software

The Rapid Eye Mount (REM) is a 60 cm robotic telescope located at La Silla, Chile. Its Observing Software (REMOS) is constituted by a set of distributed intercommunicating processes organized around a central manager. Together they grant the system safety, automatically schedule and perform observations with two simultaneous cameras of user-defined targets, and drive fast reaction to satellite alerts. Subsequent data reduction is left to pipelines managed by each camera

Direct m6A recognition by IMP1 underlays an alternative model of target selection for non-canonical methyl-readers

m6A methylation provides an essential layer of regulation in organismal development, and is aberrant in a range of cancers and neuro-pathologies. The information encoded by m6A methylation is integrated into existing RNA regulatory networks by RNA binding proteins that recognise methylated sites, the m6A readers. m6A readers include a well-characterised class of dedicated proteins, the YTH proteins, as well as a broader group of multi-functional regulators where recognition of m6A is only partially understood. Molecular insight in this recognition is essential to build a mechanistic understanding of global m6A regulation. In this study, we show that the reader IMP1 recognises the m6A using a dedicated hydrophobic platform that assembles on the methyl moiety, creating a stable high-affinity interaction. This recognition is conserved across evolution and independent from the underlying sequence context but is layered upon the strong sequence specificity of IMP1 for GGAC RNA. This leads us to propose a concept for m6A regulation where methylation plays a context-dependent role in the recognition of selected IMP1 targets that is dependent on the cellular concentration of available IMP1, differing from that observed for the YTH proteins

HIV-1 capsid is involved in post-nuclear entry steps

BACKGROUND: HIV-1 capsid influences viral uncoating and nuclear import. Some capsid is detected in the nucleus but it is unclear if it has any function. We reported that the antibiotic Coumermycin-A1 (C-A1) inhibits HIV-1 integration and that a capsid mutation confers resistance to C-A1, suggesting that capsid might affect post-nuclear entry steps. RESULTS: Here we report that C-A1 inhibits HIV-1 integration in a capsid-dependent way. Using molecular docking, we identify an extended binding pocket delimited by two adjacent capsid monomers where C-A1 is predicted to bind. Isothermal titration calorimetry confirmed that C-A1 binds to hexameric capsid. Cyclosporine washout assays in Jurkat CD4+ T cells expressing engineered human TRIMCyp showed that C-A1 causes faster and greater escape from TRIMCyp restriction. Sub-cellular fractionation showed that small amounts of capsid accumulated in the nuclei of infected cells and C-A1 reduced the nuclear capsid. A105S and N74D capsid mutant viruses did not accumulate capsid in the nucleus, irrespective of C-A1 treatment. Depletion of Nup153, a nucleoporin located at the nuclear side of the nuclear pore that binds to HIV-1 capsid, made the virus less susceptible to TRIMCyp restriction, suggesting that Nup153 may help maintain some integrity of the viral core in the nucleus. Furthermore C-A1 increased binding of CPSF6, a nuclear protein, to capsid. CONCLUSIONS: Our results indicate that capsid is involved in post-nuclear entry steps preceding integration

Understanding the Role of the Josephin Domain in the PolyUb Binding and Cleavage Properties of Ataxin-3

Ataxin-3, the disease protein in the neurodegenerative disorder Spinocerebellar Ataxia Type 3 or Machado Joseph disease, is a cysteine protease implicated in the ubiquitin proteasome pathway. It contains multiple ubiquitin binding sites through which it anchors polyubiquitin chains of different linkages that are then cleaved by the N-terminal catalytic (Josephin) domain. The properties of the ubiquitin interacting motifs (UIMs) in the C-terminus of ataxin-3 are well established. Very little is known, however, about how two recently identified ubiquitin-binding sites in the Josephin domain contribute to ubiquitin chain binding and cleavage. In the current study, we sought to define the specific contribution of the Josephin domain to the catalytic properties of ataxin-3 and assess how the topology and affinity of these binding sites modulate ataxin-3 activity. Using NMR we modeled the structure of diUb/Josephin complexes and showed that linkage preferences are imposed by the topology of the two binding sites. Enzymatic studies further helped us to determine a precise hierarchy between the sites. We establish that the structure of Josephin dictates specificity for K48-linked chains. Site 1, which is close to the active site, is indispensable for cleavage. Our studies open the way to understand better the cellular function of ataxin-3 and its link to pathology

The Domains of Human Nutrition: The Importance of Nutrition Education in Academia and Medical Schools

open28noHuman nutrition encompasses an extremely broad range of medical, social, commercial, and ethical domains and thus represents a wide, interdisciplinary scientific and cultural discipline. The high prevalence of both disease-related malnutrition and overweight/obesity represents an important risk factor for disease burden and mortality worldwide. It is the opinion of Federation of the Italian Nutrition Societies (FeSIN) that these two sides of the same coin, with their sociocultural background, are related to a low "nutritional culture" secondary, at least in part, to an insufficient academic training for health-care professionals (HCPs). Therefore, FeSIN created a study group, composed of delegates of all the federated societies and representing the different HCPs involved in human nutrition, with the aim of identifying and defining the domains of human nutrition in the attempt to more clearly define the cultural identity of human nutrition in an academically and professionally oriented perspective and to report the conclusions in a position paper. Three main domains of human nutrition, namely, basic nutrition, applied nutrition, and clinical nutrition, were identified. FeSIN has examined the areas of knowledge pertinent to human nutrition. Thirty-two items were identified, attributed to one or more of the three domains and ranked considering their diverse importance for academic training in the different domains of human nutrition. Finally, the study group proposed the attribution of the different areas of knowledge to the degree courses where training in human nutrition is deemed necessary (e.g., schools of medicine, biology, nursing, etc.). It is conceivable that, in the near future, a better integration of the professionals involved in the field of human nutrition will eventually occur based on the progressive consolidation of knowledge, competence, and skills in the different areas and domains of this discipline.openDonini, Lorenzo M; Leonardi, Francesco; Rondanelli, Mariangela; Banderali, Giuseppe; Battino, Maurizio; Bertoli, Enrico; Bordoni, Alessandra; Brighenti, Furio; Caccialanza, Riccardo; Cairella, Giulia; Caretto, Antonio; Cena, Hellas; Gambarara, Manuela; Gentile, Maria Gabriella; Giovannini, Marcello; Lucchin, Lucio; Migliaccio, Pietro; Nicastro, Francesco; Pasanisi, Fabrizio; Piretta, Luca; Radrizzani, Danilo; Roggi, Carla; Rotilio, Giuseppe; Scalfi, Luca; Vettor, Roberto; Vignati, Federico; Battistini, Nino C; Muscaritoli, MaurizioDonini, Lorenzo M; Leonardi, Francesco; Rondanelli, Mariangela; Banderali, Giuseppe; Battino, Maurizio; Bertoli, Enrico; Bordoni, Alessandra; Brighenti, Furio; Caccialanza, Riccardo; Cairella, Giulia; Caretto, Antonio; Cena, Hellas; Gambarara, Manuela; Gentile, Maria Gabriella; Giovannini, Marcello; Lucchin, Lucio; Migliaccio, Pietro; Nicastro, Francesco; Pasanisi, Fabrizio; Piretta, Luca; Radrizzani, Danilo; Roggi, Carla; Rotilio, Giuseppe; Scalfi, Luca; Vettor, Roberto; Vignati, Federico; Battistini, Nino C; Muscaritoli, Maurizi