Karl Barths Zwinglivorlesung 1922/23

Karl Barth’s Göttingen lecture on Zwingli from 1922/23 is a must-read. It is not only an excellent – though fragmentary – introduction to Zwingli – and Luther as well, especially concerning the debate on the Eucharist, but it also reveals much of Barth’s fundamental understanding of theology: as humans we do not own the truth, we can only search for it. As Barth said much later in his Bonn lecture on the Heidelberg Catechism of 1948: "We do not possess the Gospel of Jesus Christ as a dead good. We must beware of a capitalistic understanding of Christianity.

Karl Barth: Predigten 1911, hg. von Eberhard Busch und Beate Busch-Blum, 2015

No abstract available

Urs Hafner, Kult, Macht und Glaube: Eine kleine Geschichte des Zürcher Grossmünsters, 2007

No abstract available

Fritz Blanke – Lehrer und Forscher: Vortrag an der Mitgliederversammlung des Zwinglivereins 2012

In this address to the Zwingli Society in Zurich, Fritz Blanke (1900–1967) is remembered as a teacher and scholar, who educated several generations of Reformed theologians and historians, and set new standards for research as editor and commentator of Johann Georg Hamann and Huldrych Zwingli. Blanke made text come to life and reveal its relevance with utmost care and high erudition. It was essential to him that the text was elucidated whilst his personal ideas remained in the background. For this reason, his commentaries will remain indispensable

Alfred Borter, René Zihlmann, Urban Fink und Max Stierlin, Katholiken im Kanton Zürich, 2014

No abstract available

NASA's In-Space Manufacturing Project: Toward a Multimaterial Fabrication Laboratory for the International Space Station

uman space exploration to date has been limited to low Earth orbit and the moon. The International Space Station (ISS) provides a unique opportunity for NASA to partner with private industry for development and demonstration of the technologies needed to support exploration initiatives. One challenge that is critical to sustainable and safer exploration is the ability to manufacture and recycle materials in space. This paper provides an overview of NASA's in-space manufacturing (ISM) project, its past and current activities, and how technologies under development will ultimately culminate in a multimaterial fabrication laboratory ("ISM FabLab") to be deployed on the International Space Station in the early 2020s. ISM is a critical capability for the long endurance missions NASA seeks to undertake in the coming decades. An unanticipated failure that can be adapted for in low earth orbit, through a resupply launch or a return to earth, may instead result in a loss of mission while in transit to Mars. To have a suite of functional ISM capabilities that are compatible with NASA's exploration timeline, ISM must be equipped with the resources necessary to develop these technologies and deploy them for testing prior to the scheduled de-orbit of ISS in 2024. The paper provides a broad overview of ISM projects activities culminating with the Fabrication Laboratory for ISS. The FabLab will move NASA and private industry significantly closer to changing historical paradigms for human spaceflight where all materials used in space are launched from earth. While the current ISM FabLab will be tested on ISS, future systems are eventually intended for use in a deep space habitat or transit vehicle. The work of commercial companies funded under NASA's Small Business Innovative Research Program (SBIR) is also discussed, as these activities, from development of recyclable packaging for ISS to additive manufacturing capabilities for metals and electronics, could also potentially be infused into FabLab exploration capabilities as well

Elucidating the genomic history of commercially used Bacillus thuringiensis subsp. tenebrionis strain NB176

Bacillus thuringiensis subsp. tenebrionis (Btt) produces a coleopteran-specific crystal protoxin protein (Cry3Aa δ-endotoxin). After its discovery in 1982, the strain NB125 (DSM 5526) was eventually registered in 1990 to control the Colorado potato beetle (Leptinotarsa decemlineata). Gamma-irradiation of NB125 resulted in strain NB176-1 (DSM 5480) that exhibited higher cry3Aa production and became the active ingredient of the plant protection product Novodor® FC. Here, we report a comparative genome analysis of the parental strain NB125, its derivative NB176-1 and the current commercial production strain NB176. The entire genome sequences of the parental and derivative strains were deciphered by a hybrid de novo approach using short (Illumina) and long (Nanopore) read sequencing techniques. Genome assembly revealed a chromosome of 5.4 to 5.6 Mbp and six plasmids with a size range from 14.9 to 250.5 kbp for each strain. The major differences among the original NB125 and the derivative strains NB176-1 and NB176 were an additional copy of the cry3Aa gene, which translocated to another plasmid as well as a chromosomal deletion (~ 178 kbp) in NB176. The assembled genome sequences were further analyzed in silico for the presence of virulence and antimicrobial resistance (AMR) genes

Specific Sequences in the N-terminal Domain of Human Small Heat Shock Protein HSPB6 Dictate Preferential Heterooligomerization with the Orthologue HSPB1

Small heat-shock proteins (sHSPs) are a conserved group of molecular chaperones with important roles in cellular proteostasis. Although sHSPs are characterized by their small monomeric weight, they typically assemble into large polydisperse oligomers that vary in both size and shape but are principally composed of dimeric building blocks. These assemblies can include different sHSP orthologues, creating additional complexity that may affect chaperone activity. However, the structural and functional properties of such hetero-oligomers are poorly understood. We became interested in hetero-oligomer formation between human heat-shock protein family B (small) member 1 (HSPB1) and HSPB6, which are both highly expressed in skeletal muscle. When mixed in vitro, these two sHSPs form a polydisperse oligomer array composed solely of heterodimers, suggesting preferential association that is determined at the monomer level. Previously, we have shown that the sHSP N-terminal domains (NTDs), which have a high degree of intrinsic disorder, are essential for the biased formation. Here we employed iterative deletion mapping to elucidate how the NTD of HSPB6 influences its preferential association with HSPB1 and show that this region has multiple roles in this process. First, the highly conserved motif RLFDQXFG is necessary for subunit exchange among oligomers. Second, a site ∼20 residues downstream of this motif determines the size of the resultant hetero-oligomers. Third, a region unique to HSPB6 dictates the preferential formation of heterodimers. In conclusion, the disordered NTD of HSPB6 helps regulate the size and stability of hetero-oligomeric complexes, indicating that terminal sHSP regions define the assembly properties of these proteins

Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-Binding Motif

The androgen receptor (AR) is a ligand-activated transcription factor that is essential for prostate cancer development. It is activated by androgens through its ligand-binding domain (LBD), which consists predominantly of 11 α-helices. Upon ligand binding, the last helix is reorganized to an agonist conformation termed activator function-2 (AF-2) for coactivator binding. Several coactivators bind to the AF-2 pocket through conserved LXXLL or FXXLF sequences to enhance the activity of the receptor. Recently, a small compound-binding surface adjacent to AF-2 has been identified as an allosteric modulator of the AF-2 activity and is termed binding function-3 (BF-3). However, the role of BF-3 in vivo is currently unknown, and little is understood about what proteins can bind to it. Here we demonstrate that a duplicated GARRPR motif at the N terminus of the cochaperone Bag-1L functions through the BF-3 pocket. These findings are supported by the fact that a selective BF-3 inhibitor or mutations within the BF-3 pocket abolish the interaction between the GARRPR motif(s) and the BF-3. Conversely, amino acid exchanges in the two GARRPR motifs of Bag-1L can impair the interaction between Bag-1L and AR without altering the ability of Bag-1L to bind to chromatin. Furthermore, the mutant Bag-1L increases androgen-dependent activation of a subset of AR targets in a genome-wide transcriptome analysis, demonstrating a repressive function of the GARRPR/BF-3 interaction. We have therefore identified GARRPR as a novel BF-3 regulatory sequence important for fine-tuning the activity of the AR

Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease

We sought to identify new susceptibility loci for Alzheimer's disease through a staged association study (GERAD+) and by testing suggestive loci reported by the Alzheimer's Disease Genetic Consortium (ADGC) in a companion paper. We undertook a combined analysis of four genome-wide association datasets (stage 1) and identified ten newly associated variants with P ≤ 1 × 10−5. We tested these variants for association in an independent sample (stage 2). Three SNPs at two loci replicated and showed evidence for association in a further sample (stage 3). Meta-analyses of all data provided compelling evidence that ABCA7 (rs3764650, meta P = 4.5 × 10−17; including ADGC data, meta P = 5.0 × 10−21) and the MS4A gene cluster (rs610932, meta P = 1.8 × 10−14; including ADGC data, meta P = 1.2 × 10−16) are new Alzheimer's disease susceptibility loci. We also found independent evidence for association for three loci reported by the ADGC, which, when combined, showed genome-wide significance: CD2AP (GERAD+, P = 8.0 × 10−4; including ADGC data, meta P = 8.6 × 10−9), CD33 (GERAD+, P = 2.2 × 10−4; including ADGC data, meta P = 1.6 × 10−9) and EPHA1 (GERAD+, P = 3.4 × 10−4; including ADGC data, meta P = 6.0 × 10−10)