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.

Novel Single-Nucleotide Polymorphisms (SNPs) and Genetic Studies of the Shadow of Prion Protein () in Quails.

Prion diseases are a group of deadly neurodegenerative disorders caused by the accumulation of the normal prion protein (PrP) into misfolding pathological conformations (PrP). The PrP gene is essential for the development of prion diseases. Another candidate implicated in prion pathogenesis is the shadow of the prion protein () gene.

Assessment of the therapeutic potential of Hsp70 activator against prion diseases using and models.

Introduction: Prion diseases are deadly neurodegenerative disorders in both animals and humans, causing the destruction of neural tissue and inducing behavioral manifestations. Heat shock proteins (Hsps), act as molecular chaperones by supporting the appropriate folding of proteins and eliminating the misfolded proteins as well as playing a vital role in cell signaling transduction, cell cycle, and apoptosis control. SW02 is a potent activator of Hsp 70 kDa (Hsp70).

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.

First Report of Single Nucleotide Polymorphisms (SNPs) of the Leporine Shadow of Prion Protein Gene () and Absence of Nonsynonymous SNPs in the Open Reading Frame (ORF) in Rabbits.

Prion disorders are fatal infectious diseases that are caused by a buildup of pathogenic prion protein (PrP) in susceptible mammals. According to new findings, the shadow of prion protein (Sho) encoded by the shadow of prion protein gene () is associated with prion protein (PrP), promoting the progression of prion diseases. Although genetic polymorphisms in are associated with susceptibility to several prion diseases, genetic polymorphisms in the rabbit gene have not been investigated in depth.

The First Genetic Characterization of the Gene in Pekin Ducks ().

Prion diseases are fatal neurodegenerative disorders characterized by an accumulation of misfolded prion protein (PrP) in brain tissues. The shadow of prion protein (Sho) encoded by the shadow of prion protein gene () is involved in prion disease progress. The interaction between Sho and PrP accelerates the PrP conversion rate while the gene polymorphisms have been associated with prion disease susceptibility in several species.

Novel polymorphisms and genetic studies of the shadow of prion protein gene () in pheasants.

Background: Prion diseases in mammals are caused by the structural conversion of the natural prion protein (PrP) to a pathogenic isoform, the "scrapie form of prion protein (PrP)." Several studies reported that the shadow of prion protein (Sho), encoded by the shadow of prion protein gene (), is involved in prion disease development by accelerating the conformational conversion of PrP to PrP. Until now, genetic polymorphisms of the gene and the protein structure of Sho related to fragility to prion disease have not been investigated in pheasants, which are a species of poultry.

No Association between SARS-CoV-2 Infection and the Polymorphism of the Toll-like Receptor 7 () Gene in Female Population.

Coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a single-stranded RNA virus. Toll-like receptor 7 () recognizes single-stranded RNA viruses. The gene plays a critical role in the human innate and adaptive immune response to SARS-CoV-2 infections.

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.

Elevated E200K Somatic Mutation of the Prion Protein Gene () in the Brain Tissues of Patients with Sporadic Creutzfeldt-Jakob Disease (CJD).

Sporadic Creutzfeldt-Jakob disease (CJD) is a major human prion disease worldwide. CJD is a fatal neurodegenerative disease caused by an abnormal prion protein (PrP). To date, the exact etiology of sporadic CJD has not been fully elucidated.

Potential Therapeutic Use of Stem Cells for Prion Diseases.

Prion diseases are neurodegenerative disorders that are progressive, incurable, and deadly. The prion consists of PrP, the misfolded pathogenic isoform of the cellular prion protein (PrP). PrP is involved in a variety of physiological functions, including cellular proliferation, adhesion, differentiation, and neural development.

First report of a novel polymorphism and genetic characteristics of the leporine prion protein () gene.

Transmissible spongiform encephalopathies (TSEs) have been reported in a broad spectrum of hosts. The genetic polymorphisms and characteristics of the prion protein () gene have a vital impact on the development of TSEs. Notably, natural TSE infection cases have never been reported in rabbits, and genetic variations of the leporine gene have not been investigated to date.

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.

Prion infection modulates hematopoietic stem/progenitor cell fate through cell-autonomous and non-autonomous mechanisms.

Studies of PrP-derived prion disease generally focus on neurodegeneration. However, little is known regarding the modulation of hematopoietic stem progenitor cells (HSPCs) that express PrP in prion infection. Among bone marrow (BM) hematopoietic cells, hematopoietic stem cells (HSCs) strongly express PrP.

No association of prion protein gene () polymorphisms with susceptibility to the pandemic 2009 swine flu.

Background: The pandemic 2009 swine flu is a highly infectious respiratory disorder caused by H1N1 influenza A viruses. A recent study reported that knockout of the prion protein gene () induced susceptibility and lethality in influenza A virus-infected mice.

Objective: Thus, we examined the association between genetic variations of the gene and susceptibility to pandemic 2009 swine flu.

First report of structural characteristics and polymorphisms of the prion protein gene in raccoon dogs: The possibility of prion disease-resistance.

Prion diseases are fatal degenerative encephalopathies caused by misfolded prion protein (PrP) converted from normal prion protein (PrP). Previous studies have reported that genetic polymorphisms of the prion protein gene () play a critical role in susceptibility to prion diseases. In addition, prion disease-resistant animals showed unique structural features of prion protein (PrP) related to species-specific amino acids.

Creutzfeldt-Jakob Disease Incidence, South Korea, 2001-2019.

We found increasing trends of Creutzfeldt-Jakob disease (CJD) cases and annual incidence in South Korea during 2001-2019. We noted relatively low (5.7%) distribution of familial CJD.

Novel insertion/deletion polymorphisms and genetic features of the shadow of prion protein gene () in dogs, a prion-resistant animal.

Prion diseases are fatal infectious neurodegenerative disorders that are induced by misfolded prion protein (PrP). Previous studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene () plays a critical role in stimulating the conversion process of normal PrP (PrP) into PrP, and genetic polymorphisms of the gene are significantly related to susceptibility to prion diseases. Recent studies have reported that dogs show prion resistance, and there have been several attempts to identify resistance factors to prion diseases in dogs.

Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene in Pheasants.

Transmissible spongiform encephalopathies (TSEs) also known as prion diseases, are fatal neurodegenerative diseases. Prion diseases are caused by abnormal prion protein (PrP) derived from normal prion protein (PrP), which is encoded by the prion protein gene (). Prion diseases have been reported in several mammals.

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.

The First Evaluation of Proteinase K-Resistant Prion Protein (PrP) in Korean Appendix Specimens.

Prion diseases are fatal neurodegenerative disorders caused by the abnormal proteinase K-resistant prion protein (PrP). Since variant Creutzfeldt-Jakob disease (CJD) was first reported in the United Kingdom (UK) in 1996, the occurrence of variant CJD has been reported in over 10 countries. To date, variant CJD has not been reported in Korea.

Transcriptomic analysis identifies novel potential biomarkers and highlights cilium-related biological processes in the early stages of prion disease in mice.

Prion diseases are fatal and irreversible neurodegenerative diseases induced by the pathogenic form of the prion protein (PrP), which is converted from the benign form of the prion protein (PrP). These diseases are characterized by an extended asymptomatic incubation period accompanied by continuous conversion of PrP to PrP. However, to date, the mechanism governing the conversion to PrP in the initial stages of prion disease has not been fully elucidated.

The First Report of Polymorphisms and Genetic Characteristics of the Shadow of Prion Protein () in Prion Disease-Resistant Animal, Chickens.

Prion diseases are irreversible neurodegenerative disorders caused by the aggregated form of prion protein (PrP) derived from the normal form of prion protein (PrP). Previous studies have reported that shadow of prion protein (Sho) interacts with prion protein (PrP) and accelerates the conversion of PrP to PrP. In addition, genetic polymorphisms of the shadow of the prion protein gene () are related to the vulnerability of prion diseases in various hosts.

Novel Single Nucleotide Polymorphisms (SNPs) and Genetic Features of the Prion Protein Gene () in Quail ().

Prion diseases are fatal infectious diseases caused by conformational changes of a prion protein (PrP) derived from a normal prion protein (PrP). Prion diseases have been reported in several mammalian hosts but not in any birds, including the most popular poultry species, of which chickens showed some resistance to experimental prion infection. To identify the genetic polymorphisms in the quail prion protein gene (, polymerase chain reaction and DNA sequencing were performed with gene-specific primers in 164 quails.