Advanced searches left 3/3

Point Mutation - DOAJ

Summarized by Plex Scholar
Last Updated: 24 June 2022

* If you want to update the article please login/register

S645C Point Mutation Suppresses Degradation of EGFR to Promote Progression of Glioblastoma

Results We investigated the anti-tumor activity and safety of gefitinib and osimertinib in cells in this study. We also found an oncogenic substituted mutation of EGFRu2014S645C. Conclusion The mutation causes a resistance to gefitinib, but it does not lead to osimertinib therapy, but it does offer the possibility for osimertinib therapy. The study reveals a new oncogenic mutation that leads to gefitinib resistance but provides guidance on the precise treatment of individual patients with the EGFR S645C mutation.

Source link: https://doi.org/10.3389/fonc.2022.904383


The Human SCN9AR185H Point Mutation Induces Pain Hypersensitivity and Spontaneous Pain in Mice

Several SCN9A gain-of-function mutations have been identified in patients with small fiber neuropathy with chronic pain, including the R185H mutation. We have developed the Scn9aR185H mutant mouse model using the CRISPR/Cas9 technology in order to determine the effects of R185H mutation on pain tolerance. The Scn9aR185H mutant mice have no cell changes in the dorsal root ganglia bearing sensory nerve cell bodies, nor do growth or global health status change. Importantly, the mutant animals displayed spontaneous pain when compared in the conditioned place preference assay. Our findings indicate that Scn9aR185H mice have a pain phenotype, indicating that the SCN9AR185H mutation found in patients with chronic pain contributes to their symptoms. We therefore have genetic evidence for the fact that this mutation in the Nav1. 7 channel plays a significant role in nociception and pain in patients with SFN who have this mutation.

Source link: https://doi.org/10.3389/fnmol.2022.913990


A Murine Point Mutation of Sgpl1 Skin Is Enriched With Vγ6 IL17-Producing Cell and Revealed With Hyperpigmentation After Imiquimod Treatment

Sgpl1 knock-out mice in various organs were seen in this mutation, but M467K mutation mice survived for more than six weeks, with M467K mutation mice being stable under SPF conditions for more than six weeks. After imiquimod therapy, we also established that the IL17a-producing V3B36+ cell was enriched in Sgpl1M467K skin and caused severe pathology. Interestingly, hyperchromic plaque developed in the mutant mice one month after Imiquimod therapy, but not in the controls, which looked like the skin disease present in Sgpl1 deficient patients. Therefore, our findings show that Sgpl1M467K point mutation mice successfully modelled a human disease after being treated with Imiquimod. u03b3T cells in the skin, and IL17 mystery Vu03b36 T cells were also increased by Sgpl1 deficiency, contributing to skin pathology.

Source link: https://doi.org/10.3389/fimmu.2022.728455


Trichoderma reesei complete genome sequence, repeat-induced point mutation, and partitioning of CAZyme gene clusters

Abstract Background Trichoderma reesei QM6a is a model fungus for a wide variety of physiological conditions, including plant cell wall degradation, industrial production of enzymes, light responses, conidiation, polyketide biosynthesis, and plant-u2013fungal interactions. On both tandem and unlinked duplicated sequences, we show that sexual crossing quickly promoted cytosine-to-thymine point mutations. T. reesei has evolved a robust repeat-triggered point mutation system to produce AT-rich sequences, with longer AT-rich blocks containing more RIP mutations, according to bioinformatic research. T. reesei's ubiquitous distribution of AT-rich blocks links to genome-wide partitions with gene clusters, explaining why clustering of genes has been found not to influence gene expression. Conclusion This fungus-rich blocks' incorporation of ancestral gene clusters by AT-rich blocks may increase flexibility that are environmentally beneficial in this fungus-rich soils and other natural habitats.

Source link: https://doi.org/10.1186/s13068-017-0825-x


A point mutation in the nucleotide exchange factor eIF2B constitutively activates the integrated stress response by allosteric modulation

Stressors reprogram the cellular proteome by inciting the integrated stress response in eukaryotic cells. We show how a single histidine to aspartate point mutation in eIF2-P binding can be reproduced by a single histidine to aspartate point mutation in eIF2B's u03b2 subunit mimics the effects of eIF2-P binding by encouraging an I-State like conformation, resulting in the ISR's eIF2-P independent activation.

Source link: https://doi.org/10.7554/eLife.76171

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions