AI Article Synopsis

  • HLA-A*24:393 is a variant of HLA-A*24:02:01:01.
  • The difference between the two variants is a single nucleotide change at position 376.
  • This change involves a substitution from the nucleotide G to A in exon 3.

Article Abstract

HLA-A*24:393 differs from HLA-A*24:02:01:01 by one nucleotide substitution at position 376 (G → A) in exon 3.

Download full-text PDF

Source
http://dx.doi.org/10.1111/tan.15690DOI Listing

Publication Analysis

Top Keywords

novel hla-a*24393
4
hla-a*24393 allele
4
allele identified
4
identified sanger
4
sanger dideoxy
4
dideoxy nucleotide
4
nucleotide sequencing
4
sequencing taiwanese
4
taiwanese individual
4
individual hla-a*24393
4

Similar Publications

In the last decade, the emergence of variant strains of avian orthoreovirus (ARV) has caused an enormous economic impact on the poultry industry across China and other countries. This study aimed to evaluate the molecular evolution of the ARV lineages detected in Chinese commercial broiler farms. Firstly, ARV isolation and identification of commercial broiler arthritis cases from different provinces in China from 2016 to 2021 were conducted.

View Article and Find Full Text PDF

Background: Colorectal cancer (CRC) is one of the most common cancers worldwide. The mechanisms underlying metastasis, which contributes to poor outcomes, remain elusive.

Methods: We used the Cancer Genome Atlas dataset to compare mRNA expression patterns of integrin α6 (ITGA6) and integrin β4 (ITGB4) in patients with CRC.

View Article and Find Full Text PDF

Importance: Sleep disorders and mild cognitive impairment (MCI) commonly coexist in older adults, increasing their risk of developing dementia. Long-term tai chi chuan has been proven to improve sleep quality in older adults. However, their adherence to extended training regimens can be challenging.

View Article and Find Full Text PDF

Rational design of redox active metal organic frameworks for mediated electron transfer of enzymes.

Mater Horiz

January 2025

Department of Material Sciences, Institute of Pure and Applied Sciences, University of Tsukuba, 1-1-1, Tennodai, Ibaraki 305-5358, Japan.

The efficient immobilization of redox mediators remains a major challenge in the design of mediated enzyme electrode platforms. In addition to stability, the ability of the redox-active material to mediate electron transfer from the active-site buried enzymes, such as flavin adenine dinucleotide-dependent glucose dehydrogenase (FADGDH) and lactate oxidase (LOx), is also crucial. Conventional immobilization techniques can be synthetically challenging, and immobilized mediators often exhibit limited durability, particularly in continuous operation.

View Article and Find Full Text PDF

Want 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!