Publications by authors named "Nils Schrader"

Background: High-dose long-term opioid therapy (LTOT) has been associated with increased mortality and hospitalizations. Therefore, the evidence-based German guideline on LTOT for chronic non-cancer pain (CNCP) recommends to only exceed the maximum daily dose (MDD) of opioids in exceptional cases. This study aimed to determine the portion of LTOT patients who exceeded the guideline-recommended MDD and identify predictors of exceeding in administrative claims data.

View Article and Find Full Text PDF

Introduction: The number of mHealth apps has increased rapidly during recent years. Literature suggests a number of problems and barriers to the adoption of mHealth apps, including issues such as validity, usability, as well as data privacy and security. Continuous quality assessment and assurance systems might help to overcome these barriers.

View Article and Find Full Text PDF

Background: Since fall 2020, mobile health (mHealth) apps have become an integral part of the German health care system. The belief that mHealth apps have the potential to make the health care system more efficient, close gaps in care, and improve the economic outcomes related to health is unwavering and already partially confirmed. Nevertheless, problems and barriers in the context of mHealth apps usually remain unconsidered.

View Article and Find Full Text PDF

In Germany, long-term opioid treatment (L-TOT) for chronic non-tumor pain (CNTP) is discussed as not being performed according to the German guideline on L-TOT for CNTP. In the present analysis, the occurrence and predictors of inappropriate care/overuse in a cohort of German insureds with L-TOT for CNTP by the presence of a contraindication with concurrent opioid analgesic (OA) therapy were investigated. We also analyzed whether prescribing physicians themselves diagnosed a contraindication.

View Article and Find Full Text PDF

Background: All over the world, development and usage of mobile health (mHealth) apps is increasing. While apps offer numerous opportunities to improve health care, there are associated problems that differ significantly from those of traditional health care services. Further investigations on the quality of mHealth apps are needed to address these problems.

View Article and Find Full Text PDF
Article Synopsis
  • Nucleoporin 153 (Nup153) is an important and flexible protein in nuclear pores, playing a key role in managing the interactions between transport receptors and their cargo.
  • Nup153 contains four zinc finger motifs, with the second one (Nup153ZnF2) having the strongest binding affinity to the protein Ran, and this interaction is unaffected by phosphorylation.
  • The crystal structure of the Nup153-ZnF2 and Ran complex shows a unique interface that prevents the formation of a Ran-importin-beta complex, suggesting Nup153 helps regulate Ran activity at the nuclear pore and aids in terminating import processes efficiently.
View Article and Find Full Text PDF

Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC). Nic96 binds the Nsp1 complex via its N domain and assembles into the NPC framework via its central and C domain. Here, we report the crystal structure of a large structural nucleoporin, Nic96 without its N domain (Nic96DeltaN).

View Article and Find Full Text PDF

The molybdenum cofactor (Moco) forms the catalytic site in all eukaryotic molybdenum enzymes and is synthesized by a multistep biosynthetic pathway. The mechanism of transfer, storage, and insertion of Moco into the appropriate apo-enzyme is poorly understood. In Chlamydomonas reinhardtii, a Moco carrier protein (MCP) has been identified and characterized recently.

View Article and Find Full Text PDF

Glycine is the major inhibitory neurotransmitter in the spinal cord and brain stem. Gephyrin is required to achieve a high concentration of glycine receptors (GlyRs) in the postsynaptic membrane, which is crucial for efficient glycinergic signal transduction. The interaction between gephyrin and the GlyR involves the E-domain of gephyrin and a cytoplasmic loop located between transmembrane segments three and four of the GlyR beta subunit.

View Article and Find Full Text PDF

Gephyrin is an essential and instructive molecule for the formation of inhibitory synapses. Gephyrin binds directly to the large cytoplasmic loop located between transmembrane helices three and four of the beta-subunit of the glycine receptor and to microtubules, thus promoting glycine receptor (GlyR) anchoring to the cytoskeleton and clustering in the postsynaptic membrane. Besides its structural role, gephyrin is involved in the biosynthesis of the molybdenum cofactor that is essential for all molybdenum-dependent enzymes in mammals.

View Article and Find Full Text PDF

The molybdenum cofactor (Moco) containing sulfite oxidase (SO) from Arabidopsis thaliana has recently been identified and biochemically characterized. The enzyme is found in peroxisomes and believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution. Plant SO (PSO) is homodimeric and homologous to animal SO, but contains only a single Moco domain without an additional redox center.

View Article and Find Full Text PDF

Gephyrin is an essential component of the postsynaptic cortical protein network of inhibitory synapses. Gephyrin-based scaffolds participate in the assembly as well as the dynamics of receptor clusters by connecting the cytoplasmic domains of glycine and GABA(A) receptor polypeptides to two cytoskeletal systems, microtubules and microfilaments. Although there is evidence for a physical linkage between gephyrin and microtubules, the interaction between gephyrin and microfilaments is not well understood so far.

View Article and Find Full Text PDF