The School and Its Many Pasts

History is not memory; both, however, affect the way we perceive the past. In recent years, an increasing number of studies have focused on memory in order to critically analyze shared narratives of the past and their implications. Memory studies not only allow us to expand our knowledge about the past, but also help us to define the way in which today’s people, social groups and public bodies look at it and interpret or re-interpret it. In this sense, school memory is not only of interest as a gateway to the school’s past but also as a tool to understand what they know or believe they know about the school of the past and how much what they know corresponds to reality or is influenced by prejudices and stereotypes deeply rooted in common sense. These volumes aim to address these complex issues and broaden the perspective from which the schooling phenomenon is analyzed to better understand the school and its many pasts

O Museu Nacional da Escola de Floren\ue7a (1929-1941)

Cette contribution vise \ue0 reconstruire l\u2019histoire du premier v\ue9ritable mus\ue9e de l\u2019\ue9cole italienne, le Museo Nazionale di Firenze (Mus\ue9e National de Florence), fond\ue9 en 1937 par Giovanni Cal\uf2 dans le b\ue2timent abritant la Facult\ue9 des sciences politiques et sociales, \ue0 via Laura, et en 1941 a \ue9t\ue9 transf\ue9r\ue9 au prestigieux Palais Gerini, si\ue8ge du Centre national de la didactique. Le mus\ue9e avait une cr\ue9ation troubl\ue9e. En fait, son premier noyau a \ue9t\ue9 constitu\ue9 par le Museo Didattico Nazionale (Mus\ue9e National de la Didactique), fond\ue9 par Cal\uf2 en 1929, dans le but de rassembler du mat\ue9riel re\ue7u d'\ue9coles et d'\ue9tablissements d'enseignement de tout le pays et expos\ue9 de mars \ue0 avril. 1925, dans les pavillons de la grande exposition nationale de didactique de Florence. La gen\ue8se de ce mus\ue9e est int\ue9ressante car il s\u2019inspirait initialement du mod\ue8le du mus\ue9e p\ue9dagogique de la fin du XIXe si\ue8cle, caract\ue9ris\ue9 comme un lieu de collecte de mat\ue9riel didactique produit dans les \ue9coles de tous les niveaux et un laboratoire de formation et de perfectionnement des enseignants. et plus tard, il est devenu un mus\ue9e d'\ue9cole. Son but \ue9tait de raconter l'histoire de l'\ue9cole et des \ue9tablissements d'enseignement, des temps anciens aux temps contemporains. Ils contenaient un centre de documentation attach\ue9 et une biblioth\ue8que sp\ue9cialis\ue9e, qui h\ue9ritent et am\ue9liorent les fonctions de formation et de mise \ue0 jour des enseignants

Hemorrhagic risk after intravenous thrombolysis for ischemic stroke in patients with cerebral microbleeds and white matter disease

Objectives: Aim of this study was to evaluate the association between cerebral microbleeds (CMBs) and white matter disease (WMD) with intracerebral hemorrhage (ICH) after intravenous thrombolysis (IVT) with rt-PA. We also evaluated whether CMBs characteristics and WMD burden correlate with symptomatic ICH and outcome. Methods: We included acute ischemic stroke (AIS) patients treated with IVT. The number and location of CMBs as well as severity of WMD were rated analyzing pre- or post-treatment MRI. Multivariable regression analysis was used to determine the impact of CMB and WMD on ICH subgroups and outcome measures. Results: 434 patients were included. CMBs were detected in 23.3% of them. ICH occurred in 34.7% of patients with CMBs. Independent predictors of parenchymal hemorrhage were the presence of CMBs (OR 2.724, 95% CI 1.360–5.464, p = 0.005) as well as cortical-subcortical stroke (OR 3.629, 95% CI 1.841–7.151, p < 0.001) and atherothrombotic stroke subtype (OR 3.381, 95% CI 1.335–8.566, p = 0.010). Either the presence, or number, and location of CMBs, as well as WMD, was not independently associated with the development of SICH. No independent association between the presence, number, or location of CMBs or WMD and outcome measures was observed. Conclusions: The results of our study suggest that the exclusion of eligible candidates to administration of IV rt-PA only on the basis of CMBs presence is not justified. The clinical decision should be weighed with a case-by-case approach. Additional data are needed to evaluate the benefit-risk profile of rt-PA in patients carrying numerous microbleeds

TEMPO-oxidized cellulose nanofibril/polyvalent cations hydrogels: a multifaceted view of network interactions and inner structure

In the last years, hydrogels from renewable biopolymers and low-cost row materials are a hot topic for biomedical applications. In this context, cellulose nanofibrils are considered suitable building blocks for the synthesis of many biocompatible products, with a variety of chemical-physical properties. Herein we report a multi-technique and multi-scale study, from the molecular to the nanometric length scale, of the sol-gel transition observed in aqueous solutions of TEMPO-oxidized nano-sized cellulose fibrils (TOCNFs), when in the presence of polyvalent cations (Mg2+ and Ca2+). We combine the data from Small Angle Neutron Scattering (SANS), which provide information about the inner structure of the nanofibril, with those from UV Resonant Raman (UVRR) spectroscopy, which is a sensitive probe of the intra- and inter-molecular interactions in the gel and the liquid state. The transition between the gel and the liquid phases is investigated as a function of the concentration of both TOCNFs and cations, the nature of the latter, and the pH at which the phenomenon is observed. SANS analysis reveals that ion concentration induces an anisotropic swelling in the nanofibrils which, at the same time, become more and more flexible. The nanofibrils flexibility is also dependent on TOCNF concentration and pH value. UVRR allows us to elucidate the structural organization and hydrogen-bonding properties of water in aqueous TOCNF dispersions and gels, showing how water molecules partially lose their typical bulk-like tetrahedral organization when ions are added, and the gel phase is formed

Vibrational dynamics changes of protein hydration water across the dynamic transition

The vibrational dynamics of protein hydration water has been studied by incoherent neutron scattering. Experiments on a sample of fully deuterated maltose binding protein allowed us to single out the hydration water susceptibility. The main inelastic features, corresponding to hydrogen-bond bending, hydrogen-bond stretching and librational excitations, have been followed over a temperature range extending from 50 to 300 K. It turns out that the temperature dependence of the hydrogen-bond stretching contribution is quite similar to that of the mean square displacements deduced by the quasielastic signal, thus suggesting a close relationship between the anharmonicity of longitudinal phonon-like motions and the onset of diffusive molecular dynamics. On the other hand, both hydrogen-bond bending and librational excitations show a temperature dependence consistent with a harmonic character over the whole temperature range

A large-area double rotating-crystal monochromator for time-focusing neutron instruments

We present the principle and the first prototypes of a double rotating-crystal monochromator, based on an assembly of smaller rotating elements. Such a device was developed as the key element to implement a parallel-beam modification of the time-focusing technique for neutron spectrometers. This concept is particularly promising for long-pulse sources and can bring specific advantages on continuous sources as well. Neutron tests performed on the first prototypes validate the mechanical reliability of the proposed design and the feasibility of a large-area double rotating-crystal monochromator based on this technology

The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors

The maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease Mpro to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the Mpro monomer-dimer equilibrium dissociation constant. Since the functional unit of Mpro is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (SAXS) to investigate the structural features of SARS-CoV-2 Mpro in solution as a function of protein concentration and temperature. A detailed thermodynamic picture of the monomer-dimer equilibrium is derived, together with the temperature-dependent value of the dissociation constant. SAXS is also used to study how the Mpro dissociation process is affected by small inhibitors selected by virtual screening. We find that these inhibitors affect dimerization and enzymatic activity to a different extent and sometimes in an opposite way, likely due to the different molecular mechanisms underlying the two processes. The Mpro residues that emerge as key to optimize both dissociation and enzymatic activity inhibition are discussed

Evidence of coexistence of change of caged dynamics at Tg and the dynamic transition at Td in solvated proteins

Mossbauer spectroscopy and neutron scattering measurements on proteins embedded in solvents including water and aqueous mixtures have emphasized the observation of the distinctive temperature dependence of the atomic mean square displacements, , commonly referred to as the dynamic transition at some temperature Td. At low temperatures, increases slowly, but it assume stronger temperature dependence after crossing Td, which depends on the time/frequency resolution of the spectrometer. Various authors have made connection of the dynamics of solvated proteins including the dynamic transition to that of glass-forming substances. Notwithstanding, no connection is made to the similar change of temperature dependence of obtained by quasielastic neutron scattering when crossing the glass transition temperature Tg, generally observed in inorganic, organic and polymeric glass-formers. Evidences are presented to show that such change of the temperature dependence of from neutron scattering at Tg is present in hydrated or solvated proteins, as well as in the solvents used unsurprisingly since the latter is just another organic glass-formers. The obtained by neutron scattering at not so low temperatures has contributions from the dissipation of molecules while caged by the anharmonic intermolecular potential at times before dissolution of cages by the onset of the Johari-Goldstein beta-relaxation. The universal change of at Tg of glass-formers had been rationalized by sensitivity to change in volume and entropy of the beta-relaxation, which is passed onto the dissipation of the caged molecules and its contribution to . The same rationalization applies to hydrated and solvated proteins for the observed change of at Tg.Comment: 28 pages, 10 figures, 1 Tabl

Antithrombotic medications and the etiology of intracerebral hemorrhage: MUCH-Italy.

23noOBJECTIVE: To test the hypothesis that the effect of antithrombotic medications on the risk of intracerebral hemorrhage (ICH) varies according to the location of the hematoma. METHODS: Consecutive patients with ICH were enrolled as part of the Multicenter Study on Cerebral Hemorrhage in Italy (MUCH-Italy). Multivariable logistic regression models served to examine whether risk factors for ICH and location of the hematoma (deep vs lobar) predict treatment-specific ICH subgroups (antiplatelets-related ICH and oral anticoagulants [OACs]-related ICH). RESULTS: A total of 870 (313 lobar ICH, 557 deep ICH) subjects were included. Of these, 223 (25.6%) were taking antiplatelets and 77 (8.8%) OACs at the time of stroke. The odds of antiplatelet-related ICH increased with aging (odds ratio [OR] 1.05; 95% confidence interval [CI] 1.03-1.07) and hypertension (OR 1.86; 95% CI 1.22-2.85) but had no relation with the anatomical location of ICH. Conversely, lobar location of the hematoma was associated with the subgroup of OAC-related ICH (OR 1.70; 95% CI 1.03-2.81) when compared to the subgroup of patients taking no antithrombotic medications. Within the subgroup of patients taking OACs, international normalized ratio (INR) values were higher in those with lobar ICH as compared to those with deep ICH (2.8 ± 1.1 vs 2.2 ± 0.8; p = 0.011). The proportion of patients with lobar hematoma increased with increasing intensity of anticoagulation, with a ∼2-fold increased odds of lobar compared to deep ICH (odds 2.17; p = 0.03) in those exposed to overanticoagulation (INR values >3.0). CONCLUSIONS: OACs, as opposed to antiplatelets, predispose to lobar location of brain hematomas according to a dose-response relationship.openopenPezzini, A; Grassi, M; Paciaroni, M; Zini, A; Silvestrelli, G; Del Zotto, E; Caso, V; Dell'Acqua, Ml; Giossi, A; Volonghi, I; Simone, Am; Lanari, A; Costa, P; Poli, L; Morotti, A; De Giuli, V; Pepe, D; Gamba, M; Ciccone, A; Ritelli, M; Colombi, M; Agnelli, G; Padovani, APezzini, Alessandro; Grassi, M; Paciaroni, M; Zini, A; Silvestrelli, G; Del Zotto, E; Caso, V; Dell'Acqua, Ml; Giossi, A; Volonghi, I; Simone, Am; Lanari, A; Costa, P; Poli, L; Morotti, A; De Giuli, V; Pepe, D; Gamba, M; Ciccone, A; Ritelli, M; Colombi, Marina; Agnelli, G; Padovani, Alessandr