Choosing Whom to Trust: Autonomy versus Reliance on Others in Medical Decision Making among Plain Anabaptists

The idea of patients as autonomous agents dominates the medical ethics literature in Europe and America. I maintain that Plain Anabaptists allow their communities to influence medical therapy decisions more than the typical American does. They choose differently whom to trust. This is relevant to medical professionals interacting with them, especially when Plain Anabaptists make decisions at variance with standard medical recommendations. The typical American doctor will often mistake the area of disagreement, assuming that the presentation of more facts will sway the patient. However, the emphasis on community and acceptance of authority means that Plain Anabaptists will have a correspondingly different approach to decision making. It may be true that the patient does not have all relevant data or does not realize the relative trustworthiness of different information sources. Yet, often Plain Anabaptists will come to a different decision because of a different value system. They are making their own decision about who or what to trust. [Abstract by author

Plain Anabaptists and COVID-19: A Distinct Response to Government Restrictions?

Plain Anabaptists have a distinct way of relating to the government. Does that mean they would have distinct decision making processes in relation to government-promulgated public health restrictions regarding COVID-19? This essay argues that plain Anabaptist populations did not exhibit particularly unique decision-making and responses to COVID-19

Self-association studies of yeast TATA binding protein using an E. coli two-hybrid system

In eukaryotes the TATA binding protein (TBP) binds DNA at a TATA box promoter, recruits RNA polymerase II, and initiates transcription. In vitro studies have shown that transcription initiation may be regulated by self-association and oligomerization of TBP. The carboxy-terminal domain of TBP binds the DNA and is the largest part of the molecule, while the small amino terminal domain has an unknown function. We have used an Escherichia Coli two-hybrid system to study if the two domains of TBP exhibit any self-association in vivo. The pBT bait plasmid encoded the full length bacteriophage [lambda]cl protein for fusion with the inserted TBP gene, and the pTRG target plasmid encoded the amino terminal domain of an RNA polymerase II subunit and a linker region for protein fusion with the insert. Cells co-transformed with the two plasmids grew only if there was interaction between the TBP subunits. Such interaction allowed the [lambda]cl-TBP fusion protein to recruit the RNA polymerase-TEP fusion protein, initiating transcription of a carbenicillin resistance reporter gene and permitting cell growth. Using this system we found significant interaction between full-length TBP\u27s

Strength in Numbers? The Advantages of Multiple Rankings

Symposium: The Next Generation of Law School Rankings held April 15, 2005 at Indiana University School of Law-Bloomington

Strength in Numbers? The Advantages of Multiple Rankings

Symposium: The Next Generation of Law School Rankings held April 15, 2005 at Indiana University School of Law-Bloomington

Producing Textbook Sociology

The conservative role of the textbook in reproducing the dominant ideas of a disciplinary field is well known. The factors driving that content have remained almost entirely unexamined. Reviewing the universe of textbooks aimed at the American market between 1998 and 2004, we explore the persistence of the identification in American sociology textbooks of a paradigm in which structural functionalism, conflict theory, and symbolic interactionism are used to frame the theoretical core of the discipline. We examine how over time the textbook market produces both supply and demand pressures to reproduce content that is at odds with the mainstream of the profession. We draw upon in-depth interviews with recent textbook authors and their editors

On-chip generation of heralded photon-number states

Beyond the use of genuine monolithic integrated optical platforms, we report here a hybrid strategy enabling on-chip generation of configurable heralded two-photon states. More specifically, we combine two different fabrication techniques, \textit{i.e.}, non-linear waveguides on lithium niobate for efficient photon-pair generation and femtosecond-laser-direct-written waveguides on glass for photon manipulation. Through real-time device manipulation capabilities, a variety of path-coded heralded two-photon states can be produced, ranging from product to entangled states. Those states are engineered with high levels of purity, assessed by fidelities of 99.5$\pm$8\% and 95.0$\pm$8\%, respectively, obtained via quantum interferometric measurements. Our strategy therefore stands as a milestone for further exploiting entanglement-based protocols, relying on engineered quantum states, and enabled by scalable and compatible photonic circuits

Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family

The rate of protein evolution is determined by a combination of selective pressure on protein function and biophysical constraints on protein folding and structure. Determining the relative contributions of these properties is an unsolved problem in molecular evolution with broad implications for protein engineering and function prediction. As a case study, we examined the structural divergence of the rapidly evolving o-succinylbenzoate synthase (OSBS) family, which catalyzes a step in menaquinone synthesis in diverse microorganisms and plants. On average, the OSBS family is much more divergent than other protein families from the same set of species, with the most divergent family members sharing <15% sequence identity. Comparing 11 representative structures revealed that loss of quaternary structure and large deletions or insertions are associated with the family’s rapid evolution. Neither of these properties has been investigated in previous studies to identify factors that affect the rate of protein evolution. Intriguingly, one subfamily retained a multimeric quaternary structure and has small insertions and deletions compared with related enzymes that catalyze diverse reactions. Many proteins in this subfamily catalyze both OSBS and N-succinylamino acid racemization (NSAR). Retention of ancestral structural characteristics in the NSAR/OSBS subfamily suggests that the rate of protein evolution is not proportional to the capacity to evolve new protein functions. Instead, structural features that are conserved among proteins with diverse functions might contribute to the evolution of new functions

Caspase‐8 variant G regulates rheumatoid arthritis fibroblast‐like synoviocyte aggressive behavior

Objective: Fibroblast-like synoviocytes (FLS) play a pivotal role in rheumatoid arthritis (RA) by contributing to synovial inflammation and progressive joint damage. An imprinted epigenetic state is associated with the FLS aggressive phenotype. We identified CASP8 (encoding for caspase-8) as a differentially marked gene and evaluated its pathogenic role in RA FLSs. Methods: RA FLS lines were obtained from synovial tissues at arthroplasty and used at passage 5-8. Caspase-8 was silenced using small interfering RNA, and its effect was determined in cell adhesion, migration and invasion assays. Quantitative reverse transcription PCR and western blot were used to assess gene and protein expression, respectively. A caspase-8 selective inhibitor was used determine the role of enzymatic activity on FLS migration and invasion. Caspase-8 isoform transcripts and epigenetic marks in FLSs were analyzed in FLS public databases. Crystal structures of caspase-8B and G were determined. Results: Caspase-8 deficiency in RA FLSs reduced cell adhesion, migration, and invasion independent of its catalytic activity. Epigenetic and transcriptomic analyses of RA FLSs revealed that a specific caspase-8 isoform, variant G, is the dominant isoform expressed (~80% of total caspase-8) and induced by PDGF. The crystal structures of caspase-8 variant G and B were identical except for a unique unstructured 59 amino acid N-terminal domain in variant G. Selective knockdown of caspase-8G was solely responsible for the effects of caspase-8 on calpain activity and cell invasion in FLS. Conclusion: Blocking caspase-8 variant G could decrease cell invasion in diseases like RA without the potential deleterious effects of nonspecific caspase-8 inhibition