First Report of Polymorphisms and Genetic Characteristics of Protein Gene () in Cats.

Prion diseases are fatal neurodegenerative disorders caused by the misfolding of the normal cellular prion protein (PrP) into its infectious isoform (PrP). Although prion diseases in humans, sheep, goats, and cattle have been extensively studied, feline spongiform encephalopathy (FSE) remains poorly understood. Genetic factors, particularly polymorphisms in the prion protein gene () and protein gene (), have been linked to prion disease susceptibility in various species.

The first report of single nucleotide polymorphisms in the open reading frame of the prion-like protein gene in rabbits.

Background: Natural cases of prion disease have not been reported in rabbits, and prior attempts to identify a prion conversion agent have been unsuccessful. However, recent applications of prion seed amplifying experimental techniques have sparked renewed interest in the potential susceptibility of rabbits to prion disease infections. Among several factors related to prion disease, polymorphisms within the prion-like protein gene (), a member of the prion protein family, have been reported as significantly associated with disease susceptibility in various species.

The first report of polymorphisms of the prion protein gene () in Pekin ducks ().

Background: Prion diseases have been extensively reported in various mammalian species and are caused by a pathogenic prion protein (PrP), which is a misfolded version of cellular prion protein (PrP). Notably, no cases of prion disease have been reported in birds. Single nucleotide polymorphisms (SNPs) of the prion protein gene () that encodes PrP have been associated with susceptibility to prion diseases in several species.

Identification of a novel risk factor for chronic wasting disease (CWD) in elk: S100G single nucleotide polymorphism (SNP) of the prion protein gene (PRNP).

Prion diseases are fatal and malignant infectious encephalopathies induced by the pathogenic form of prion protein (PrP) originating from benign prion protein (PrP). A previous study reported that the M132L single nucleotide polymorphism (SNP) of the prion protein gene (PRNP) is associated with susceptibility to chronic wasting disease (CWD) in elk. However, a recent meta-analysis integrated previous studies that did not find an association between the M132L SNP and susceptibility to CWD.

Development of a chicken interferon-induced transmembrane protein 3 (IFITM3)-specific monoclonal antibody using phage display.

Interferon-induced transmembrane protein 3 (IFITM3) has potent antiviral activity against several viruses. Recent studies have reported that the chicken IFITM3 gene also plays a pivotal role in blocking viral replication, but these studies are considerably limited due to being conducted at the RNA level only. Thus, the development of a chicken IFITM3 protein-specific antibody is needed to validate the function of IFITM3 at the protein level.

Suppressing Halide Segregation in Wide-Band-Gap Mixed-Halide Perovskite Layers through Post-Hot Pressing.

Mixed-halide perovskites (MHPs) have attracted attention as suitable wide-band-gap candidate materials for tandem applications owing to their facile band-gap tuning. However, when smaller bromide ions are incorporated into iodides to tune the band gap, photoinduced halide segregation occurs, which leads to voltage deficit and photoinstability. Here, we propose an original post-hot pressing (PHP) treatment that suppresses halide segregation in MHPs with a band gap of 2.

Regulatory Single Nucleotide Polymorphism of the Bovine Gene Induces Differential Transcriptional Capacities of Hanwoo and Holstein Cattle.

Interferon-induced transmembrane protein 3 (IFITM3), a crucial effector of the host's innate immune system, prohibits an extensive range of viruses. Previous studies have reported that single nucleotide polymorphisms (SNPs) of the gene are associated with the expression level and length of the IFITM3 protein and can impact susceptibility to infectious viruses and the severity of infection with these viruses. However, there have been no studies on polymorphisms of the bovine gene.

Absence of proteinase K-resistant PrP in Korean Holstein cattle carrying potential bovine spongiform encephalopathy-related E211K somatic mutation.

Bovine spongiform encephalopathy (BSE) is a kind of prion disease caused by proteinase K-resistant prion protein (PrP ) in cattle. Although BSE has been reported worldwide, BSE-infected cases have never been reported in Korea. In a previous study, we identified BSE-related somatic mutation E211K in 3 Korean Holstein cattle.

The First Report of the Prion Protein Gene () Sequence in Pekin Ducks (): The Potential Prion Disease Susceptibility in Ducks.

Pathogenic prion protein (PrP), converted from normal prion protein (PrP), causes prion disease. Although prion disease has been reported in several mammalian species, chickens are known to show strong resistance to prion diseases. In addition to chickens, the domestic duck occupies a large proportion in the poultry industry and may be regarded as a potential resistant host against prion disease.

Genetic association between the rs12252 SNP of the interferon-induced transmembrane protein gene and influenza A virus infection in the Korean population.

Background: Interferon-induced transmembrane protein 3 (IFITM3) is a potent host antiviral effector protein that blocks the invasion of various viruses, including the influenza A virus (IAV). The C allele of the rs12252 single nucleotide polymorphism (SNP) shows vulnerability to the pandemic 2009 H1N1 IAV in European and Asian populations.

Objective: Here, we estimated the disease susceptibility of the rs12252 SNP with the pandemic 2009 H1N1 IAV infection in the Korean population.

Identification of the prion-related protein gene (PRNT) sequences in various species of the Cervidae family.

Chronic wasting disease (CWD) is caused by abnormal deleterious prion protein (PrP), and transmissible spongiform encephalopathy occurs in the Cervidae family. In recent studies, the susceptibility of prion disease has been affected by polymorphisms of the prion gene family. However, the study of the prion-related protein gene (PRNT) is rare, and the DNA sequence of this gene was not fully reported in all Cervidae families.

Genetic characteristics and polymorphisms in the chicken interferon-induced transmembrane protein (IFITM3) gene.

The interferon-induced transmembrane protein 3 (IFITM3) gene is classified as a small interferon-stimulated gene and is associated with a broad spectrum of antiviral functions against several fatal enveloped viruses, including influenza A viruses (IAVs). The rs12252 single nucleotide polymorphism (SNP) of the IFITM3 gene in humans was associated with susceptibility to H1N1 influenza in a 2009 pandemic. In addition, overexpression of the IFITM3 protein potently inhibits the highly pathogenic avian influenza H5N1 virus in ducks and chickens.

No polymorphisms in the coding region of the prion-like protein gene in Thoroughbred racehorses.

Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of an abnormal prion protein isoform (PrP), which is converted from the normal prion protein (PrP). Prion diseases have been reported in an extensive number of species but not in horses up to now; therefore, horses are known to be a species resistant to prion diseases. The prion-like protein gene () is closely located downstream of the prion protein gene () and the prion-like protein (Doppel) is a homologue with PrP.

Prion-like protein gene (PRND) polymorphisms associated with scrapie susceptibility in Korean native black goats.

The polymorphisms of the prion protein (PRNP) gene, which encodes normal prion proteins (PrP), are known to be involved in the susceptibility of prion diseases. The prion-like protein (Doppel) gene (PRND) is the paralog of the PRNP gene and is closely located downstream of the PRNP gene. In addition, the polymorphisms of PRND correlate with disease susceptibility in several animals.

The first report of genetic variations in the chicken prion protein gene.

Abnormal structural changes of the prion protein (PrP) are the cause of prion disease in a wide range of mammals. However, spontaneous infected cases have not been reported in chicken. Genetic variations of the prion protein gene (PRNP) may impact susceptibility to prion disease but have not been investigated thus far.

Discotic liquid crystalline hydrazone compounds: synthesis and mesomorphic properties.

[reaction: see text] 1,3,5-Trisacetoacetamidobenzene with three 1,3-diketo groups was synthesized by the reaction of 1,3,5-triaminobenzene with diketene. Discotic hydrazone compounds were prepared by the diazo coupling reaction between 1,3,5-trisacetoacetamidobenzene and diazonium salts of 4-alkyloxyphenylamines. The compounds existed in hydrazone forms exclusively, being stabilized by the intramolecular hydrogen bonds, and showed discotic nematic or columnar hexagonal mesophases.