Using small molecule reagents to selectively modify epitopes based on their conformation

References

• Prusiner SB. Prions. Proc Natl Acad Sci U S A 1998; 95:13363 - 83; http://dx.doi.org/10.1073/pnas.95.23.13363; PMID: 9811807
   PubMed Web of Science ®Google Scholar
• Stahl N, Baldwin M, Teplow DB, Hood LE, Beavis R, Chait B, et al. Cataloging post-translational modifications of the scrapie prion protein by mass spectrometry. In: Prusiner SB, Collinge J, Powell J, Anderton B, eds. Prion diseases of humans and animals. New York: Ellis Horwood, 1992:361-79.
   Google Scholar
• Safar J, Wille H, Itri V, Groth D, Serban H, Torchia M, et al. Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 1998; 4:1157 - 65; http://dx.doi.org/10.1038/2654; PMID: 9771749
   PubMed Web of Science ®Google Scholar
• Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991; 30:7672 - 80; http://dx.doi.org/10.1021/bi00245a003; PMID: 1678278
   PubMed Web of Science ®Google Scholar
• Onisko BC, Silva CJ, Requena JR. Methods to differentiate protein conformers Application number 20060110785. 2006.
   Google Scholar
• Carter JM, Dynin I, Erickson ML, Onisko BC, Requena JR, Silva CJP. 1.8 Conformation-dependent covalent modification of PrP. Prion2009 September 23-25, 2009 Porto Carras, Chalkidiki Greece Book of Abstracts, 2009:54.
   Google Scholar
• Lehto MT, Peery HE, Cashman NR. Current and future molecular diagnostics for prion diseases. Expert Rev Mol Diagn 2006; 6:597 - 611; http://dx.doi.org/10.1586/14737159.6.4.597; PMID: 16824033
   PubMed Web of Science ®Google Scholar
• Williamson RA, Peretz D, Pinilla C, Ball H, Bastidas RB, Rozenshteyn R, et al. Mapping the prion protein using recombinant antibodies. J Virol 1998; 72:9413 - 8; PMID: 9765500
   PubMed Web of Science ®Google Scholar
• Miller BT, Collins TJ, Rogers ME, Kurosky A. Peptide biotinylation with amine-reactive esters: differential side chain reactivity. Peptides 1997; 18:1585 - 95; http://dx.doi.org/10.1016/S0196-9781(97)00225-8; PMID: 9437720
   PubMed Web of Science ®Google Scholar
• Anjaneyulu PS, Staros JV. Reactions of N-hydroxysulfosuccinimide active esters. Int J Pept Protein Res 1987; 30:117 - 24; http://dx.doi.org/10.1111/j.1399-3011.1987.tb03319.x; PMID: 3667072
   PubMedGoogle Scholar
• Onisko B, Fernández EG, Freire ML, Schwarz A, Baier M, Camiña F, et al. Probing PrPSc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate. Biochemistry 2005; 44:10100 - 9; http://dx.doi.org/10.1021/bi0501582; PMID: 16042387
   PubMed Web of Science ®Google Scholar
• Pimenova T, Nazabal A, Roschitzki B, Seebacher J, Rinner O, Zenobi R. Epitope mapping on bovine prion protein using chemical cross-linking and mass spectrometry. J Mass Spectrom 2008; 43:185 - 95; http://dx.doi.org/10.1002/jms.1280; PMID: 17924399
   PubMed Web of Science ®Google Scholar
• Kouassi GK, Irudayaraj J. A nanoparticle-based immobilization assay for prion-kinetics study. J Nanobiotechnology 2006; 4:8; http://dx.doi.org/10.1186/1477-3155-4-8; PMID: 16916458
   PubMedGoogle Scholar
• Bibby DF, Gill AC, Kirby L, Farquhar CF, Bruce ME, Garson JA. Application of a novel in vitro selection technique to isolate and characterise high affinity DNA aptamers binding mammalian prion proteins. J Virol Methods 2008; 151:107 - 15; http://dx.doi.org/10.1016/j.jviromet.2008.03.013; PMID: 18433888
   PubMed Web of Science ®Google Scholar
• Kascsak RJ, Rubenstein R, Merz PA, Tonna-DeMasi M, Fersko R, Carp RI, et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 1987; 61:3688 - 93; PMID: 2446004
   PubMed Web of Science ®Google Scholar
• Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009; 457:1128 - 32; http://dx.doi.org/10.1038/nature07761; PMID: 19242475
   PubMed Web of Science ®Google Scholar
• Maddison BC, Whitelam GC, Gough KC. Cellular prion protein in ovine milk. Biochem Biophys Res Commun 2007; 353:195 - 9; http://dx.doi.org/10.1016/j.bbrc.2006.12.006; PMID: 17174270
   PubMed Web of Science ®Google Scholar
• Novitskaya V, Makarava N, Bellon A, Bocharova OV, Bronstein IB, Williamson RA, et al. Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J Biol Chem 2006; 281:15536 - 45; http://dx.doi.org/10.1074/jbc.M601349200; PMID: 16569635
   PubMed Web of Science ®Google Scholar
• Spinner DS, Kascsak RB, Lafauci G, Meeker HC, Ye X, Flory MJ, et al. CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fibrils. J Leukoc Biol 2007; 81:1374 - 85; http://dx.doi.org/10.1189/jlb.1106665; PMID: 17379700
   PubMed Web of Science ®Google Scholar
• Dumpitak C. Untersuchungen zu Struktur und Funktion von Polysacchariden und alterungsassoziierten Proteinmodifikationen bei Prionen. Dissertation. Düsseldorf: Heinrich-Heine-Universität, 2003.
   Google Scholar
• Prusiner SB. Prion Biology and Diseases. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press, 2004.
   Google Scholar
• Plummer TH Jr., Elder JH, Alexander S, Phelan AW, Tarentino AL. Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. J Biol Chem 1984; 259:10700 - 4; PMID: 6206060
   PubMed Web of Science ®Google Scholar
• Maley F, Trimble RB, Tarentino AL, Plummer TH Jr.. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal Biochem 1989; 180:195 - 204; http://dx.doi.org/10.1016/0003-2697(89)90115-2; PMID: 2510544
   PubMed Web of Science ®Google Scholar
• Tzaban S, Friedlander G, Schonberger O, Horonchik L, Yedidia Y, Shaked G, et al. Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry 2002; 41:12868 - 75; http://dx.doi.org/10.1021/bi025958g; PMID: 12379130
   PubMed Web of Science ®Google Scholar
• Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, et al. The most infectious prion protein particles. Nature 2005; 437:257 - 61; http://dx.doi.org/10.1038/nature03989; PMID: 16148934
   PubMed Web of Science ®Google Scholar
• Zou WQ, Langeveld J, Xiao X, Chen S, McGeer PL, Yuan J, et al. PrP conformational transitions alter species preference of a PrP-specific antibody. J Biol Chem 2010; 285:13874 - 84; http://dx.doi.org/10.1074/jbc.M109.088831; PMID: 20194495
   PubMed Web of Science ®Google Scholar
• Kascsak R. Reiterating the epitope specificity of prion-specific mAb 3F4. J Biol Chem 2010; 285:le5, author reply le6.
   Google Scholar
• Bolton DC, Seligman SJ, Bablanian G, Windsor D, Scala LJ, Kim KS, et al. Molecular location of a species-specific epitope on the hamster scrapie agent protein. J Virol 1991; 65:3667 - 75; PMID: 1710287
   PubMed Web of Science ®Google Scholar
• Bessen RA, Marsh RF. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 1992; 66:2096 - 101; PMID: 1347795
   PubMed Web of Science ®Google Scholar
• Bessen RA, Marsh RF. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 1994; 68:7859 - 68; PMID: 7966576
   PubMed Web of Science ®Google Scholar
• Peretz D, Scott MR, Groth D, Williamson RA, Burton DR, Cohen FE, et al. Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci 2001; 10:854 - 63; http://dx.doi.org/10.1110/ps.39201; PMID: 11274476
   PubMed Web of Science ®Google Scholar
• Gong B, Ramos A, Vázquez-Fernández E, Silva CJ, Alonso J, Liu Z, et al. Probing structural differences between PrP(C) and PrP(Sc) by surface nitration and acetylation: evidence of conformational change in the C-terminus. Biochemistry 2011; 50:4963 - 72; http://dx.doi.org/10.1021/bi102073j; PMID: 21526750
   PubMed Web of Science ®Google Scholar
• Neises B, Steglich W. Simple Method for the Esterification of Carboxylic Acids. Angew Chem Int Ed Engl 1978; 17:522 - 4; http://dx.doi.org/10.1002/anie.197805221
   Web of Science ®Google Scholar
• Che FY, Fricker LD. Quantitative peptidomics of mouse pituitary: comparison of different stable isotopic tags. J Mass Spectrom 2005; 40:238 - 49; http://dx.doi.org/10.1002/jms.743; PMID: 15706629
   PubMed Web of Science ®Google Scholar
• Flinta C, Persson B, Jörnvall H, von Heijne G. Sequence determinants of cytosolic N-terminal protein processing. Eur J Biochem 1986; 154:193 - 6; http://dx.doi.org/10.1111/j.1432-1033.1986.tb09378.x; PMID: 3080313
   PubMedGoogle Scholar
• Atarashi R, Moore RA, Sim VL, Hughson AG, Dorward DW, Onwubiko HA, et al. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat Methods 2007; 4:645 - 50; http://dx.doi.org/10.1038/nmeth1066; PMID: 17643109
   PubMed Web of Science ®Google Scholar
• Sambrook J, Fritsch EF, Maniatis T. Molecular Cloning. A laboratory Manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press, 1989.
   Google Scholar
• Kimberlin RH, Walker C. Characteristics of a short incubation model of scrapie in the golden hamster. J Gen Virol 1977; 34:295 - 304; http://dx.doi.org/10.1099/0022-1317-34-2-295; PMID: 402439
   PubMed Web of Science ®Google Scholar
• Marsh RF, Kimberlin RH. Comparison of scrapie and transmissible mink encephalopathy in hamsters. II. Clinical signs, pathology, and pathogenesis. J Infect Dis 1975; 131:104 - 10; http://dx.doi.org/10.1093/infdis/131.2.104; PMID: 1167884
   PubMed Web of Science ®Google Scholar
• Bessen RA, Marsh RF. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J Gen Virol 1992; 73:329 - 34; http://dx.doi.org/10.1099/0022-1317-73-2-329; PMID: 1531675
   PubMed Web of Science ®Google Scholar
• Zlotnik I, Rennie JC. Further observations on the experimental transmission of scrapie from sheep and goats to laboratory mice. J Comp Pathol 1963; 73:150 - 62; PMID: 14003830
   PubMed Web of Science ®Google Scholar
• Prusiner SB, Groth D, Serban A, Stahl N, Gabizon R. Attempts to restore scrapie prion infectivity after exposure to protein denaturants. Proc Natl Acad Sci U S A 1993; 90:2793 - 7; http://dx.doi.org/10.1073/pnas.90.7.2793; PMID: 8464892
   PubMed Web of Science ®Google Scholar