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  1. 1
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity."
    Harris D.A., Falls D.L., Johnson F.A., Fischbach G.D.
    Proc. Natl. Acad. Sci. U.S.A. 88:7664-7668(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-51.
    Category: Sequences.
    Tissue: Brain.
    Source: UniProtKB/Swiss-Prot (reviewed).
  3. 3
    "Mr 42,000 ARIA: a protein that may regulate the accumulation of acetylcholine receptors at developing chick neuromuscular junctions."
    Falls D.L., Harris D.A., Johnson F.A., Morgan M.M., Corfas G., Fischbach G.D.
    Cold Spring Harb. Symp. Quant. Biol. 55:397-406(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    Cited for: STRUCTURE BY NMR OF 134-248.
    Category: Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  5. 5
    "Interactions of Cu2+ ions with chicken prion tandem repeats."
    Stanczak P., Luczkowski M., Juszczyk P., Grzonka Z., Kozlowski H.
    Dalton Trans 2004:2102-2107(2004) [PubMed] [Europe PMC] [Abstract]
    Annotation: Similar to human octapeptide fragments chicken tandem repeats exhibit a cooperative effect in binding Cu(2+) ions although chicken peptides are much less effective in metal ion coordinationImported.
    Source: GeneRIF:396452.

    This publication is mapped to 2 other entries.

  6. 6
    "Comparative analysis of the human and chicken prion protein copper binding regions at pH 6.5."
    Redecke L., Meyer-Klaucke W., Koker M., Clos J., Georgieva D., Genov N., Echner H., Kalbacher H., Perbandt M., Bredehorst R., Voelter W., Betzel C.
    J. Biol. Chem. 280:13987-13992(2005) [PubMed] [Europe PMC] [Abstract]
    Annotation: Data show that structure and coordination of human prion protein (PrP) copper binding sites are conserved in the pH 6.5-7.4 range and that chicken PrP hexarepeat motifs display homologous Cu(II) coordination at sub-stoichiometric copper concentrations.Imported.
    Source: GeneRIF:396452.

    This publication is mapped to 25 other entries.

  7. 7
    "Structure and stability of the CuII complexes with tandem repeats of the chicken prion."
    Stanczak P., Valensin D., Juszczyk P., Grzonka Z., Migliorini C., Molteni E., Valensin G., Gaggelli E., Kozlowski H.
    Biochemistry 44:12940-12954(2005) [PubMed] [Europe PMC] [Abstract]
    Annotation: PrP was found to be very similar to the mammalian protein although there is only 30% homology in the secondary structure; hexapeptide repeats might bind copper ions in two different ways depending on the number of repeats and metal/ligand molar ratioImported.
    Source: GeneRIF:396452.

    This publication is mapped to 2 other entries.

  8. 8
    "A comparative molecular dynamics study on thermostability of human and chicken prion proteins."
    Ji H.F., Zhang H.Y.
    Biochem. Biophys. Res. Commun. 359:790-794(2007) [PubMed] [Europe PMC] [Abstract]
    Annotation: thermostability of Human PrP(C) is comparable with that of chicken PrP(C)Imported.
    Source: GeneRIF:396452.

    This publication is mapped to 25 other entries.

  9. 9
    "Distribution of the cellular prion protein in the central nervous system of the chicken."
    Atoji Y., Ishiguro N.
    J. Chem. Neuroanat. 38:292-301(2009) [PubMed] [Europe PMC] [Abstract]
    Annotation: These findings suggest that PrP in the chicken CNS is localized in the dendrites and axons of neurons and that it is associated with certain sensory systems.Imported.
    Source: GeneRIF:396452.

    This publication is mapped to 2 other entries.

1 to 9 of 9  Show