899 research outputs found
S. Lévi : Le « tokharien B » langue de Koutcha
No full textMaspero Henri. S. Lévi : Le « tokharien B » langue de Koutcha. In: Bulletin de l'Ecole française d'Extrême-Orient. Tome 13, 1913. pp. 73-78
Homme libre – Homme livre: François Maspero
No full textThe blog post "Homme libre – Homme livre: François Maspero" explores the life and works of François Maspero, a notable French editor and writer. The author discusses the serendipitous timing of receiving a book about Maspero and learning of his death. The book, "François Maspero et les paysages humains," is described as a detailed tribute, covering Maspero\u27s literary contributions and personal experiences, including his time in Algeria. The post emphasizes the book\u27s value as a collection of testimonies and documents, providing insights into Maspero\u27s life, his publishing endeavors, and his influence on French intellectual and political scenes. The author also mentions Maspero\u27s role as a geographer, highlighting how his writings offer a unique perspective on human landscapes. Additionally, the post notes the limited recognition of Maspero in Germany and underscores the significance of his work in amplifying the voices of dissident movements in Eastern Europe during the 1970s.
Le billet de blog "Homme libre – Homme livre : François Maspero" explore la vie et les œuvres de François Maspero, un éditeur et écrivain français renommé. L\u27auteur évoque la coïncidence troublante entre la réception d\u27un livre sur Maspero et l\u27annonce de son décès. Le livre, "François Maspero et les paysages humains," est décrit comme un hommage exhaustif, détaillant les contributions littéraires de Maspero et ses expériences personnelles, y compris son séjour en Algérie. Le billet met en avant la valeur de cet ouvrage en tant que recueil de témoignages et de documents, offrant un aperçu de la vie de Maspero, de sa maison d\u27édition et de son influence sur les paysages intellectuels et politiques français. L\u27auteur souligne également le rôle de Maspero en tant que géographe, montrant comment ses écrits offrent une perspective unique sur les paysages humains. En outre, le billet note la reconnaissance limitée de Maspero en Allemagne et insiste sur l\u27importance de son travail dans l\u27amplification des voix des mouvements dissidents en Europe de l\u27Est durant les années 1970
Saggio sopra l\u27origine ed il progresso de\u27 costumi, e delle opinioni a\u27 medesimi pertinenti di Giacopo Stellini volgarizzato da Lodovico Valeriani
No full textMilano : presso Pirotta e Maspero stampatori-librai in S. Margherita, 1806
Segn.: a8 b-g4 1-12 13.
Legatura non coeva in cartone rigido con dorso in pelle
https://galileodiscovery.unipd.it/discovery/fulldisplay?context=L&vid=39UPD_INST:VU1&search_scope=MyInst_and_CI&tab=Everything&docid=alma99002552781020604
In vitro ubiquitination: self-ubiquitination, chain formation, and substrate ubiquitination assays
No full textUbiquitination of proteins in vitro has evolved as an indispensable tool for the functional analysis of this posttranslational modifi cation. In vitro ubiquitination is particularly helpful to study conjugation mechanisms. The effi ciency of the ubiquitination reaction depends in part on the quality of the enzymes utilized. Here we introduce the assay developed in our lab to study HECT E3 ligases. It involves bacterially expressed E1, His-tagged Ube2D3 (also called UbcH5c, the best E2 for Nedd4), untagged Nedd4, and untagged ubiquitin (Ub). As tags may impair specifi c activity of the enzymes or even interfere with the enzymatic reaction, they should be avoided, removed, or kept to a minimal size whenever possible, unless proven to be without consequence. The protocol described here is suitable for other E3 ligases capable of forming Ub chains as pseudo-product of the enzyme reaction. It is also adapted to include substrates. In this case, substrates should be tagged and purifi ed after the reaction is completed to allow the detection of the ubiquitinated products
Orthodontic treatment in a patient with cleidocranial dysostosis
No full textCleidocranial dysostosis is a rare congenital skeletal disorder, associated with clavicular hypoplasia or aplasia, delayed closure of cranial fontanels, brachycephalic skull, delayed exfoliation of primary dentition, eruption of permanent teeth, and multiple supernumerary and morphologic abnormalities of the maxilla and mandible. The disorder is caused by mutation in the CBFA1 gene, on the short arm of chromosome 6p21. The prevalence of cleidocranial dysostosis is estimated one per million, without sex or ethnic group predilection. The purpose of this paper is to describe the orthodontic treatment in a patient with cleidocranial dysostosis. Therapy may include removal of supernumerary teeth, surgical exposure of impacted teeth, and orthodontic treatment
SYNTHESIS, A. MASPERO, INCLUDING AN AB-INITIO XRPD STUDY OF CUDMNPZ HDMNPZ, -DIMETHYL--NITRO PIRAZOLE.
No full textSynthesis, characterization and XRPD studies of metal-organic frameworks containing 1,4 bis(4-pyrazolyl) and 1,4 bis(5-tetrazolyl)benzene ligands
No full textIn the last decade we have been deeply exploring the coordination chemistry of polydentate ligands possessing multiple donor sites. Nowadays we decided to increased the complexity of the polytopic N-ligands aiming at the formation of oligomeric and polymeric species with different functional properties.
Inspires to the 1,4-benzene-dicarboxylate (BDC) the ligand of the highly porous and capable of H2 sorption MOF-5 proposed by Yaghi et al., and planning to employ polytopic longer spacers possessing nitrogen coordination sites (with the possibility of an exobidentate coordination), we turned our attention to the 1,4-bis(5-tetrazolyl)benzene species (C8H6N8, H2btb).
After having tailored high-yield, cheap and atoxic syntheses for H2btb [1], we started coupling this ligand with a transition metal ions aiming at the formation of microcrystalline materials of well defined stoichiometry, structure and functional properties: nanoporosity, cooperative magnetism and catalytic activity.
The isolated materials shows a variety of stoichiometries, each one with its own peculiar structure: homoleptic species [Ag2(btb), Cu(btb) and Co(btb)], hydrated (or solvated) compounds [Co(btb)•2H2O and Zn(btb)•nDMF], and even hydroxo complexes [Cu2(μ3-OH)2(btb)]. These compounds are either dense or moderately porous and, therefore, they are not prone to gas sorption or storage, as originally targeted [2].
In this context, we decided to develop a new strategy to synthesized the analogous 1,4-bis(4-pyrazolyl)benzene (C12H10N4, H2bpb) [1] with the hope to obtain microporous and non-dense species with the coordination of the metal transition elements. Specifically, in our research, we have coupled these ligands with Ni, Cu, Zn, Hg to afford the species Ni(bpb), Zn(bpb), Cu2(bpb) and Hg(bpb). These species are isolated by solvothermal reaction and fully characterized by elemental and thermogravimetric analysis, IR spectroscopy and we attained their full structural characterization resorting to state-of-the-art powder diffraction methods, occasionally coupled to thermodiffractometry analysis.
Adsorption capacities are also studied with preliminary gas sorption analysis, towards N2, and showing attractive adsorption capacities of the compound Ni(bpb) and Zn(bpb) in agreement with their structural characterization that shows a very low density and regulars networks.
[1] A. Maspero, S. Galli, N. Masciocchi, G. Palmisano, Chem. Lett., 2008, in press.
[2] A.Maspero, S. Galli, V.Colombo, G.Peli, N.Masciocchi, S.Stagni, E.Barea, J.A.R. Navarro, Inorg. Chim. ACTA, 2008, in press
Deconstructing destruction: A rapid route to proteasomal fate
No full textIn this issue of Molecular Cell, Kiss et al.1 introduce UbiREAD, a technology that deciphers ubiquitin chain-mediated degradation in living cells, revealing a hierarchy where K48 chains of at least three ubiquitins drive rapid proteasomal degradation and branched K48/K63 chains follow substrate-anchored rules
Targeting HECT-type E3 ligases - insights from catalysis, regulation and inhibitors
No full textUbiquitination plays a pivotal role in most cellular processes and is critical for protein degradation and signalling. E3 ligases are the matchmakers in the ubiquitination cascade, responsible for substrate recognition and modification with specific polyubiquitin chains. Until recently, it was not clear how the catalytic activity of E3s is modulated, but major recent studies on HECT E3 ligases is filling this void. These enzymes appear to be held in a closed, inactive conformation, which is relieved by biochemical manoeuvres unique to each member, thus ensuring exquisite regulation and specificity of the enzymes. The new advances and their significance to the function of HECT E3s are described here, with a particular focus on the Nedd4 family members
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