Ionic channels belong to the group of the most important proteins. Not only do they enable transmembrane transport but they are also the key factors for proper cell function. Mutations changing their structure and functionality often lead to severe diseases called channelopathies. On the other hand, transmembrane channels are very difficult objects for experimental studies. Only 2% of experimentally identified structures are transmembrane proteins, while genomic studies show that transmembrane proteins make up 30% of all coded proteins. This gap could be diminished by bioinformatical methods which enable modeling unknown protein structures, functions, transmembrane location, and ligand binding. Several in silico methods dedicated to transmembrane proteins have been developed; some general methods could also be used. They provide the information unavailable from experiments. Current modeling tools use a variety of computational methods, which provide results of surprisingly high quality.
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http://dx.doi.org/10.1007/978-3-319-56895-9_2 | DOI Listing |
PLoS Genet
January 2025
Department of Pediatric and Adolescent Medicine, Mayo Clinic, 200 1st St. SW, Rochester, Minnesota 55905, United States of America.
Motor neuron diseases, such as amyotrophic lateral sclerosis (ALS) and progressive bulbar palsy, involve loss of muscle control resulting from death of motor neurons. Although the exact pathogenesis of these syndromes remains elusive, many are caused by genetically inherited mutations. Thus, it is valuable to identify additional genes that can impact motor neuron survival and function.
View Article and Find Full Text PDFPLoS One
January 2025
SLAC National Accelerator Laboratory, Stanford University, Stanford, California, United States of America.
Protein-Protein Interactions (PPIs) are a key interface between virus and host, and these interactions are important to both viral reprogramming of the host and to host restriction of viral infection. In particular, viral-host PPI networks can be used to further our understanding of the molecular mechanisms of tissue specificity, host range, and virulence. At higher scales, viral-host PPI screening could also be used to screen for small-molecule antivirals that interfere with essential viral-host interactions, or to explore how the PPI networks between interacting viral and host genomes co-evolve.
View Article and Find Full Text PDFPlant Physiol
January 2025
Department of Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546-0312, USA.
Omega (ω)-3 fatty acids (FAs) are essential components of cell membranes that also serve as precursors of numerous regulatory molecules. α-linolenic acid (ALA), one of the most important ω3 FAs in plants, is synthesized in both the plastid and extraplastidial compartments. FA Desaturase (FAD) 3 is an extraplastidial enzyme that converts linoleic acid (LA) to ALA.
View Article and Find Full Text PDFEndocrinology
January 2025
Thyroid Research Unit, Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, New York.
The pathogenesis of Thyroid Eye Disease (TED) has been suggested as due to signal enhancement in orbital fibroblasts as a result of autoantibody-induced, synergistic, interaction between the TSH receptor (TSHR) and the IGF-1 receptor (IGF-1R). This interaction has been explained by a "receptor cross talk", mediated via β-arrestin binding. Here, we have examined if this interaction can be mediated via direct receptor contact using modeling and experimental approaches.
View Article and Find Full Text PDFAdv Exp Med Biol
January 2025
Cancer Research UK Scotland Centre (Edinburgh), Institute of Genetics & Cancer, University of Edinburgh, Edinburgh, UK.
E-cadherin is a transmembrane protein and central component of adherens junctions (AJs). The extracellular domain of E-cadherin forms homotypic interactions with E-cadherin on adjacent cells, facilitating the formation of cell-cell adhesions, known as AJs, between neighbouring cells. The intracellular domain of E-cadherin interacts with α-, β- and p120-catenins, linking the AJs to the actin cytoskeleton.
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