U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    PRNP prion protein [ Bos taurus (domestic cattle) ]

    Gene ID: 281427, updated on 4-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Post-transcriptional silencing of Bos taurus prion family genes and its impact on granulosa cell steroidogenesis.

    Post-transcriptional silencing of Bos taurus prion family genes and its impact on granulosa cell steroidogenesis.
    Pimenta JMBGA, Pires VMR, Nolasco S, Castelo-Branco P, Marques CC, Apolónio J, Azevedo R, Fernandes MT, Lopes-da-Costa L, Prates J, Pereira RMLN.

    03/19/2022
    Prion protein modulates endothelial to mesenchyme-like transition in trabecular meshwork cells: Implications for primary open angle glaucoma.

    Prion protein modulates endothelial to mesenchyme-like transition in trabecular meshwork cells: Implications for primary open angle glaucoma.
    Ashok A, Kang MH, Wise AS, Pattabiraman P, Johnson WM, Lonigro M, Ravikumar R, Rhee DJ, Singh N., Free PMC Article

    10/31/2020
    Deletion/insertion polymorphisms of the PRNP gene is associated with bovine spongiformencephalopathy.

    Deletion/insertion polymorphisms of the prion protein gene (PRNP) in gayal (Bos frontalis).
    Memon S, Li G, Xiong H, Wang L, Liu XY, Yuan M, Deng W, Xi D.

    02/16/2019
    Data suggest that the E211K prion protein provides the opportunity for future analysis of physiological changes over time.

    Effects of a naturally occurring amino acid substitution in bovine PrP: a model for inherited prion disease in a natural host species.
    Vrentas CE, Greenlee JJ, Foster GH, West J, Jahnke MM, Schmidt MT, Nicholson EM., Free PMC Article

    08/11/2018
    Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle

    Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle.
    Brunelle BW, O'Grady AM, Nicholson EM, Seabury CM., Free PMC Article

    07/8/2017
    the data indicate a four-rung beta-solenoid structure as a key feature for the architecture of infectious mammalian prions.

    The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy.
    Vázquez-Fernández E, Vos MR, Afanasyev P, Cebey L, Sevillano AM, Vidal E, Rosa I, Renault L, Ramos A, Peters PJ, Fernández JJ, van Heel M, Young HS, Requena JR, Wille H., Free PMC Article

    06/24/2017
    Insights into Chronic Wasting Disease and Bovine Spongiform Encephalopathy Species Barriers by Use of Real-Time Conversion

    Insights into Chronic Wasting Disease and Bovine Spongiform Encephalopathy Species Barriers by Use of Real-Time Conversion.
    Davenport KA, Henderson DM, Bian J, Telling GC, Mathiason CK, Hoover EA., Free PMC Article

    11/7/2015
    Misfolded structures, with nonnative beta-strands formed in the flexible N-terminal domain of PRNP were found in acidic pH simulations.

    Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH.
    Cheng CJ, Daggett V., Free PMC Article

    06/6/2015
    This work demonstrates that this isolate is transmissible, has a BSE-H phenotype when transmitted to cattle with the K211 polymorphism, and has molecular features that distinguish it from other cases of BSE-H described in the literature.

    Clinical and pathologic features of H-type bovine spongiform encephalopathy associated with E211K prion protein polymorphism.
    Greenlee JJ, Smith JD, West Greenlee MH, Nicholson EM., Free PMC Article

    02/14/2015
    Genetic characterization of PRNP promoter indel variations and the polymorphism of open reading frames (ORFs) of PRNP and bovine prion-like Shadoo (SPRN) genes, are reported.

    PRNP and SPRN genes polymorphism in atypical bovine spongiform encephalopathy cases diagnosed in Polish cattle.
    Gurgul A, Polak MP, Larska M, Słota E.

    06/29/2013
    data showed a differential timing of PrPC expression during early bovine development; the cell-specific expression of PrPC in bovine embryos was revealed to included the developing brain and spinal cord, peripheral nervous system, liver, and mesonephros

    Developmental expression of the cellular prion protein (PrP(C) ) in bovine embryos.
    Peralta OA, Huckle WR, Eyestone WH., Free PMC Article

    01/26/2013
    The centripetal spread of bovine spongiform encephalopathy prions along the autonomic nervous system to the central nervous system, starting already halfway in the incubation time, is reported.

    Spread of classic BSE prions from the gut via the peripheral nervous system to the brain.
    Kaatz M, Fast C, Ziegler U, Balkema-Buschmann A, Hammerschmidt B, Keller M, Oelschlegel A, McIntyre L, Groschup MH.

    12/8/2012
    The results indicate that certain negative feedback response elements are located in the 5' flanking region and intron1 of the PRNP gene, suggesting that regulation by transcription factors such as Sp1 and RP58 may contribute to the negative feedback mechanism of PRNP.

    The 5' flanking region and intron1 of the bovine prion protein gene (PRNP) are responsible for negative feedback regulation of the prion protein.
    Xue G, Aida Y, Onodera T, Sakudo A., Free PMC Article

    11/24/2012
    allele and haplotype segregation at the polymorphic sites within the promoter (23indel) and intron 1 (12indel) regions of the PRNP

    Abnormal segregation of alleles and haplotypes at the polymorphic site of the PRNP gene within promoter and intron 1 regions in Polish Holstein-Friesian cattle.
    Strychalski J, Czarnik U, Zabolewicz T., Free PMC Article

    11/17/2012
    PRNP gene variation in Pakistani cattle and buffaloes.

    PRNP gene variation in Pakistani cattle and buffaloes.
    Imran M, Mahmood S, Babar ME, Hussain R, Yousaf MZ, Abid NB, Lone KP.

    09/29/2012
    The Japanese and Canadian L-type bovine spongiform encephalopathy prions are identical to those from the European cases.

    Comparative analysis of Japanese and foreign L-type BSE prions.
    Masujin K, Miwa R, Okada H, Mohri S, Yokoyama T., Free PMC Article

    08/11/2012
    A significant relation between the investigated PRNP indel polymorphisms (23 and 12 bp indels), and susceptibility of Polish Holstein-Friesian cattle to classical bovine spongiform encephalopathy, is reported.

    Polymorphism of the prion protein gene (PRNP) in Polish cattle affected by classical bovine spongiform encephalopathy.
    Gurgul A, Czarnik U, Larska M, Polak MP, Strychalski J, Słota E.

    07/14/2012
    fibrils formed by the rabbit protein contain less beta-sheet structure and more alpha-helix structure than those formed by the proteins from human and cow

    Fibril formation of the rabbit/human/bovine prion proteins.
    Zhou Z, Yan X, Pan K, Chen J, Xie ZS, Xiao GF, Yang FQ, Liang Y., Free PMC Article

    07/7/2012
    these results identify a novel PrP(C)-interacting protein KCTD1 and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C).

    PrPC interacts with potassium channel tetramerization domain containing 1 (KCTD1) protein through the PrP(51-136) region containing octapeptide repeats.
    Huang T, Xu J, Xiang J, Lu Y, Chen R, Huang L, Xiao G, Sun G.

    03/24/2012
    Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster </= mouse < rabbit < bovine prion protein

    Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies.
    Julien O, Chatterjee S, Bjorndahl TC, Sweeting B, Acharya S, Semenchenko V, Chakrabartty A, Pai EF, Wishart DS, Sykes BD, Cashman NR.

    10/22/2011
    The polymorphisms of PRNP gene, including SNP in exon 3, 23-bp indel in promoter region, 12-bp indel in intron 1 in 2 Chinese indigenous cattle breeds of northeast China, were investigated.

    Polymorphism of the prion protein gene (PRNP) in two Chinese indigenous cattle breeds.
    Qin LH, Zhao YM, Bao YH, Bai WL, Chong J, Zhang GL, Zhang JB, Zhao ZH.

    10/15/2011
    The del/del genotype or at least its del allele may modulate the expression of PRNP at the 23-bp locus in the medulla oblongata of the cattle breeds studied.

    Evaluation of PRNP expression based on genotypes and alleles of two indel loci in the medulla oblongata of Japanese Black and Japanese Brown cattle.
    Msalya G, Shimogiri T, Ohno S, Okamoto S, Kawabe K, Minezawa M, Maeda Y., Free PMC Article

    09/17/2011
    PRNP haplotype is associated with classical bovine spongiform encephalopathy incidence in European Holstein cattle.

    PRNP haplotype associated with classical BSE incidence in European Holstein cattle.
    Murdoch BM, Clawson ML, Yue S, Basu U, McKay S, Settles M, Capoferri R, Laegreid WW, Williams JL, Moore SS., Free PMC Article

    02/26/2011
    The present study demonstrated that vector-based siRNA expression systems is an efficient approach to knockdown the PRNP gene expression in bovine fibroblast cells.

    Knockdown of the prion gene expression by RNA interference in bovine fibroblast cells.
    Wang S, Lv X, Zhang K, Lin T, Liu X, Yuan J, Dai Y, Li N.

    01/15/2011
    The interaction of the molecular chaperone Hsc70 (HSPA8) with recombinant PrP was investigated.

    The binding of the molecular chaperone Hsc70 to the prion protein PrP is modulated by pH and copper.
    Wilkins S, Choglay AA, Chapple JP, van der Spuy J, Rhie A, Birkett CR, Cheetham ME.

    10/4/2010
    firstprevious page of 3 nextlast