Biochemical Analysis of Interaction between Kringle Domains of Plasminogen and Prion Proteins with Q167R Mutation |
Lee, Jeongmin
(Division of Zoonoses, Center for Immunology and Pathology, National Institute of Health, Korea Centers for Disease Control and Prevention)
Lee, Byoung Woo (Department of Genetic Engineering, Sungkyunkwan University) Kang, Hae-Eun (Division of Foreign Animal Disease, Animal and Plant Quarantine Agency) Choe, Kevine K. (Department of Pharmacy and Institute of Pharmaceutical Science and Technology, Hanyang University) Kwon, Moosik (Department of Genetic Engineering, Sungkyunkwan University) Ryou, Chongsuk (Department of Pharmacy and Institute of Pharmaceutical Science and Technology, Hanyang University) |
1 | Choi BR, Lee J, Kim SY, Yim I, Kim EH, Woo HJ. 2013. Prion protein conversion induced by trivalent iron in vesicular trafficking. Biochem. Biophys. Res. Commun. 432: 539-544. DOI |
2 | Scatchard G. 1949. The attractions of proteins for small molecules and ions. Ann. N. Y. Acad. Sci. 51: 660-672. DOI |
3 | Goldmann W, Hunter N, Smith G, Foster J, Hope J. 1994. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75: 989-995. DOI |
4 | Westaway D, Zuliani V, Cooper CM, Da Costa M, Neuman S, Jenny AL, et al. 1994. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev. 8: 959-969. DOI |
5 | Clousard C, Beaudry P, Elsen JM, Milan D, Dussaucy M, Bounneau C, et al. 1995. Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie. J. Gen. Virol. 76: 2097-2101. DOI |
6 | Bossers A, Schreuder BE, Muileman IH, Belt PB, Smits MA. 1996. PrP genotype contributes to determining survival times of sheep with natural scrapie. J. Gen. Virol. 77: 2669-2673. DOI |
7 | Ryou C, Prusiner SB, Legname G. 2003. Cooperative binding of dominant-negative prion protein to kringle domains. J. Mol. Biol. 329: 323-333. DOI |
8 | Maissen M, Roeckl C, Glatzel M, Goldmann W, Aguzzi A. 2001. Plasminogen binds to disease-associated prion protein of multiple species. Lancet 357: 2026-2028. DOI |
9 | Prusiner SB. 1998. Prions. Proc. Natl. Acad. Sci. USA 95: 13363-13383. DOI |
10 | Prusiner SB. 1991. Molecular biology of prion diseases. Science 252: 1515-1522. DOI |
11 | Zulianello L, Kaneko K, Scott M, Erpel S, Han D, Cohen FE, et al. 2000. Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J. Virol. 74: 4351-4360. DOI |
12 | Rogers M, Yehiely F, Scott M, Prusiner SB. 1993. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl. Acad. Sci. USA 90: 3182- 3186. DOI |
13 | Cohen FE, Pan K-M, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. 1994. Structural clues to prion replication. Science 264: 530-531. DOI |
14 | Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, et al. 1995. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83: 79-90. DOI |
15 | Kaneko K, Zulianello L, Scott M, Cooper CM, Wallace AC, James TL, et al. 1997. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94: 10069-10074. DOI |
16 | Peretz D, Williamson RA, Matsunaga Y, Serban H, Pinilla C, Bastidas RB, et al. 1997. A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273: 614-622. DOI |
17 | Mays CE, Ryou C. 2011. Plasminogen: a cellular protein cofactor for PrPSc propagation. Prion 5: 22-27. DOI |
18 | Cohen FE, Prusiner SB. 1998. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67: 793-819. DOI |
19 | Perrier V, Wallace AC, Kaneko K, Safar J, Prusiner SB, Cohen FE. 2000. Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc. Natl. Acad. Sci. USA 97: 6073-6078. DOI |
20 | Deleault NR, Piro JR, Walsh DJ, Wang F, Ma J, Geoghegan JC, et al. 2012. Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids. Proc. Natl. Acad. Sci. USA 109: 8546-8551. DOI |
21 | Shin W, Lee B, Hong S, Ryou C, Kwon M. 2008. Cloning and expression of a prion protein (PrP) gene from Korean bovine (Bos taurus coreanae) and production of rabbit antibovine PrP antibody. Biotechnol. Lett. 30: 1705-1711. DOI |
22 | Negredo C, Monks E, Sweeney T. 2007. A novel real-time ultrasonic method for prion protein detection using plasminogen as a capture molecule. BMC Biotechnol. 7: 43. DOI |
23 | Perrier V, Kaneko K, Safar J, Vergara J, Tremblay P, DeArmond SJ, et al. 2002. Dominant-negative inhibition of prion replication in transgenic mice. Proc. Natl. Acad. Sci. USA 99: 13079-13084. DOI |
24 | Shaked Y, Engelstein R, Gabizon R. 2002. The binding of prion proteins to serum components is affected by detergent extraction conditions. J. Neurochem. 82: 1-5. DOI |
25 | Warrens AN, Jones MD, Lechler RI. 1997. Splicing by overlap extension by PCR using asymmetric amplification: an improved technique for the generation of hybrid proteins of immunological interest. Gene 186: 29-35. DOI |
26 | Hunter N, Moore L, Hosie BD, Dingwall WS, Greig A. 1997. Association between natural scrapie and PrP genotype in a flock of Suffolk sheep in Scotland. Vet. Rec. 140: 59-63. DOI |
27 | Ryou C. 2007. Prions and prion diseases: fundamentals and mechanistic details. J. Microbiol. Biotechnol. 17: 1059-1070. |
28 | Mays CE, Ryou C. 2010. Plasminogen stimulates propagation of protease-resistant prion protein in vitro. FASEB J. 24: 5102-5112. DOI |
29 | Fischer MB, Roeckl C, Parizek P, Schwarz HP, Aguzzi A. 2000. Binding of disease-associated prion protein to plasminogen. Nature 408: 479-483. DOI |
30 | Belt PB, Muileman IH, Schreuder BEC, Ruijter JB, Gielkens ALJ, Smits MA. 1995. Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. J. Gen. Virol. 76: 509-517. DOI |
31 | Shibuya S, Higuchi J, Shin R-W, Tateishi J, Kitamoto T. 1998. Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease. Lancet 351: 419. |
32 | Shibuya S, Higuchi J, Shin R-W, Tateishi J, Kitamoto T. 1998. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 43: 826-828. DOI |
33 | Striebel JF, Race B, Meade-White KD, LaCasse R, Chesebro B. 2011. Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171. PLoS Pathog. 7: e1002275. DOI |
34 | Kuwajima K. 1995. Circular dichroism, pp. 115-135. In Shirley BA (ed.). Methods in Molecular Biology: Protein Stability and Folding: Theory and Practice. Humana Press, Totowa. USA. |
35 | Mehlhorn I, Groth D, Stockel J, Moffat B, Reilly D, Yansura D, et al. 1996. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35: 5528-5537. DOI |
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