Binnendifferenzierte Sachtexte als Unterstützung für den Erwerb von domänenspezifischen Wissensbeständen und Konzepten: Executive Summary

Les textes dans les livres d’école sont souvent trop difficiles même pour des élèves de niveau moyen. Pour des apprenants plus faibles et des enfants pour qui l’allemand est une langue seconde, ces textes sont trop exigeants sur le plan linguistique. La mise à disposition de textes de niveaux différenciés est dès lors une nécessité pour une école inclusive.Texts in the social sciences at schools are often difficult even for children with average scholastic abilities; weak learners or children who speak German as a second language are over-challenged. Consequently, internally differentiated texts – i.e. different versions of the same content – are necessary to create an inclusive learning environment.Sachtexte in Schulbüchern sind oft selbst für durchschnittlich begabte Kinder zu schwer; für schwächere Lernende und für Kinder mit Deutsch als Zweitsprache sind sie sprachlich überfordernd. Binnendifferenzierte Sachtexte sind deshalb eine Notwendigkeit für eine inklusive Schule.I testi contenuti nei libri scolastici sono spesso troppo difficili persino per gli allievi di livello medio; per gli studenti più deboli e per i bambini per i quali il tedesco è una seconda lingua, questi testi sono troppo esigenti dal punto di vista linguistico. L’offerta di testi che variano dal punto di vista della difficoltà di lettura diventa perciò una necessità per una scuola inclusiva.Il project „Texts tematics differenziads a l’intern sco med per sustegnair l’acquisiziun dal savair e da concepts da domenas specificas“ sa basa sin la constataziun che meds d’instruir e d‘emprender (ed ils texts tematics cuntegnids en quels) stattan anc adina en il center da l’instrucziun, ma na satisfan betg a las pretensiuns per in’instrucziun individualisanta. Questa constataziun stat en connex cun las exigenzas ad ina scola inclusiva ed a las consequenzas organisatoricas da la differenziaziun interna

Bioinformatic analysis of proteomics data

Most biochemical reactions in a cell are regulated by highly specialized proteins, which are the prime mediators of the cellular phenotype. Therefore the identification, quantitation and characterization of all proteins in a cell are of utmost importance to understand the molecular processes that mediate cellular physiology. With the advent of robust and reliable mass spectrometers that are able to analyze complex protein mixtures within a reasonable timeframe, the systematic analysis of all proteins in a cell becomes feasible. Besides the ongoing improvements of analytical hardware, standardized methods to analyze and study all proteins have to be developed that allow the generation of testable new hypothesis based on the enormous pre-existing amount of biological information. Here we discuss current strategies on how to gather, filter and analyze proteomic data sates using available software packages

Tricarbonyl­bis(tricyclo­hexyl­phosphine-κP)ruthenium(0) toluene solvate

The title compound, [Ru(C18H33P)2(CO)3]·C7H8, shows a distorted trigonal-bipyramdial coordination around the central Ru atom, with the two phosphine ligands occupying the axial positions. Two toluene mol­ecules per asymmetric unit with site-occupation factors of 0.5 are observed. One of them forces two of the CO ligands to enclose a wider C—Ru—C bond angle [127.5 (3)°] than in the solvent-free crystal structure of [Ru(PCy3)2(CO)3] (Cy is cyclo­hexyl)

Continuous Infusion of Escalated Doses of Amphotericin B Deoxycholate: An Open-Label Observational Study

Amphotericin B deoxycholate (AmB-d) remains a mainstay of antifungal therapy for immunocompromised patients, despite being associated with significant therapy-related toxicity. Because continuous infusion of AmB-d is better tolerated than traditional administration over 2-6 hours, we evaluated escalation of the AmB-d dose in 33 patients (31 of whom were neutropenic), for whom the initial dosage of AmB-d (1 mg/kg/day) was gradually increased to 2.0 mg/kg/day when renal function remained stable and the drug was tolerated. Dose escalation was possible without delay in 28 patients. Median duration of AmB-d therapy was 16 days (range, 7-72 days). Infusion-related reactions accompanied 2-fold decrease in creatine clearance was observed in 5 patients, and the decrease was dose-limiting in only 1 patient; no dialysis was required. In conclusion, continuous infusion of AmB-d escalated to 2.0 mg/kg/day seems not to cause additional impairment of vital organ functions and to be well tolerated by most patient

The ribosome receptors Mrx15 and Mba1 jointly organize cotranslational insertion and protein biogenesis in mitochondria

Mitochondrial gene expression in Saccharomyces cerevisiae is responsible for the production of highly hydrophobic subunits of the oxidative phosphorylation system. Membrane insertion occurs cotranslationally on membrane-bound mitochondrial ribosomes. Here, by employing a systematic mass spectrometry-based approach, we discovered the previously uncharacterized membrane protein Mrx15 that interacts via a soluble C-terminal domain with the large ribosomal subunit. Mrx15 contacts mitochondrial translation products during their synthesis and plays, together with the ribosome receptor Mba1, an overlapping role in cotranslational protein insertion. Taken together, our data reveal how these ribosome receptors organize membrane protein biogenesis in mitochondria

GPI anchor biosynthesis in yeast: phosphoethanolamine is attached to the α1,4-linked mannose of the complete precursor glycophospholipid

Cells synthesize the GPI anchor carbohydrate core by successively adding N-acetylglucosamine, three mannoses, and phosphoethanolamine (EtN-P) onto phosphatidylinositol, thus forming the complete GPI precursor lipid which is then added to proteins. Previously, we isolated a GPI deficient yeast mutant accumulating a GPI intermediate containing only two mannoses, suggesting that it has difficulty in adding the third, α1,2-linked Man of GPI anchors. The mutant thus displays a similar phenotype as the mammalian mutant cell line S1A-b having a mutation in the PIG-B gene. The yeast mutant, herein named gpi10-1, contains a mutation in YGL142C, a yeast homolog of the human PIG-B. YGL142C predicts a highly hydrophobic integral membrane protein which by sequence is related to ALG9, a yeast gene required for adding Man in α1,2 linkage to N-glycans. Whereas gpi10-1 cells grow at a normal rate and make normal amounts of GPI proteins, the microsomes of gpi10-1 are completely unable to add the third Man in an in vitro assay. Further analysis of the GPI intermediate accumulating in gpi10 shows it to have the structure Manα1-(EtNP-)Manα1-4G1cNα1-6(acyl)Inositol-P-lipid. The presence of EtN-P on the α1,4-linked Man of GPI anchors is typical of mammalian and a few other organisms but had not been observed in yeast GPI proteins. This additional EtN-P is not only found in the abnormal GPI intermediate of gpi10-1 but is equally present on the complete GPI precursor lipid of wild type cells. Thus, GPI biosynthesis in yeast and mammals proceeds similarly and differs from the pathway described for Trypanosoma brucei in several aspect

Chromosome organization by a conserved condensin-ParB system in the actinobacterium Corynebacterium glutamicum

Higher-order chromosome folding and segregation are tightly regulated in all domains of life. In bacteria, details on nucleoid organization regulatory mechanisms and function remain poorly characterized, especially in non-model species. Here, we investigate the role of DNA-partitioning protein ParB and SMC condensin complexes in the actinobacterium Corynebacterium glutamicum. Chromosome conformation capture reveals SMC-mediated long-range interactions around ten centromere-like parS sites clustered at the replication origin (oriC). At least one oriC-proximal parS site is necessary for reliable chromosome segregation. We use chromatin immunoprecipitation and photoactivated single-molecule localization microscopy to show the formation of distinct, parS-dependent ParB-nucleoprotein subclusters. We further show that SMC/ScpAB complexes, loaded via ParB at parS sites, mediate chromosomal inter-arm contacts (as previously shown in Bacillus subtilis). However, the MukBEF-like SMC complex MksBEFG does not contribute to chromosomal DNA-folding;instead, this complex is involved in plasmid maintenance and interacts with the polar oriC-tethering factor DivIVA. Our results complement current models of ParB-SMC/ScpAB crosstalk and show that some condensin complexes evolved functions that are apparently uncoupled from chromosome folding