Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0140-6736(94)92257-8 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
VRK2 inhibits the replication of infectious bursal disease virus by phosphorylating RACK1 and suppressing apoptosis.
Int J Biol Macromol
January 2025
International Joint Research Center of National Animal Immunology, College of Veterinary Medicine, Henan Agricultural University, Zhengzhou 450046, Henan, PR China; Longhu Laboratory, Zhengzhou, Henan, PR China; Ministry of Education Key Laboratory for Animal Pathogens and Biosafety, Henan Agricultural University, Zhengzhou, PR China. Electronic address:
Infectious bursal disease (IBD) is an acute, highly contagious, and immunosuppressive avian disease caused by the infectious bursal disease virus (IBDV). Despite significant efforts, the lack of knowledge about host proteins that counteract IBDV replication has hindered progress in preventing and controlling IBD in chickens. This study identifies the mitochondria-associated protein vaccinia virus-related kinase 2 (VRK2) as an inhibitor of IBDV.
View Article and Find Full Text PDFSilver Electrodes Are Highly Selective for CO in CO Electroreduction due to Interplay between Voltage Dependent Kinetics and Thermodynamics.
J Phys Chem Lett
November 2024
Science Institute and Faculty of Physical Sciences, University of Iceland, 107 Reykjavík, Iceland.
Electrochemical reduction is a promising way to make use of CO as feedstock for generating renewable fuel and valuable chemicals. Several metals can be used as the electrocatalyst to generate CO and formic acid, but hydrogen formation is an unwanted side reaction that can even be dominant. The lack of selectivity is, in general, a significant problem, but silver-based electrocatalysts have been shown to be highly selective, with faradaic efficiency of CO production exceeding 90%, when the applied voltage is below -1 V vs RHE.
View Article and Find Full Text PDFStructural Basis for Voltage Gating and Dalfampridine Binding in the Shaker Potassium Channel.
bioRxiv
October 2024
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, 60637, USA.
Article Synopsis
- - The generation of action potentials in neurons relies on the activation of sodium and potassium channels, with Shaker potassium channels being crucial for regulating neuronal activity and a target for treating multiple sclerosis with the drug dalfampridine.
- - Research using AlphaFold2 has revealed a structural model of the closed Shaker potassium channel, showing how the voltage sensor's movement leads to pore opening through specific interactions between particular channel segments.
- - The study identifies critical aspects of the activation pathway and the binding of dalfampridine, offering insights that could guide the development of new drugs aimed at voltage-gated ion channels for neurological disorders.
Revealing a hidden conducting state by manipulating the intracellular domains in K10.1 exposes the coupling between two gating mechanisms.
Elife
September 2024
Oncophysiology Group. Max Planck Institute for Multidisciplinary Sciences, City Campus, Göttingen, Germany.
The family of potassium channels serves relevant physiological functions in both excitable and non-excitable cells, reflected in the massive consequences of mutations or pharmacological manipulation of their function. This group of channels shares structural homology with other voltage-gated K channels, but the mechanisms of gating in this family show significant differences with respect to the canonical electromechanical coupling in these molecules. In particular, the large intracellular domains of channels play a crucial role in gating that is still only partly understood.
View Article and Find Full Text PDFTurning a Kv channel into hot and cold receptor by perturbing its electromechanical coupling.
bioRxiv
August 2024
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, 60637, USA.
Voltage-dependent potassium channels (Kv) are extremely sensitive to membrane voltage and play a crucial role in membrane repolarization during action potentials. Kv channels undergo voltage-dependent transitions between closed states before opening. Despite all we have learned using electrophysiological methods and structural studies, we still lack a detailed picture of the energetics of the activation process.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!