Aptamers to explore prion protein interactions with nucleic acids

Frontiers in Bioscience

Volumn 15, Issue 2, 2010, Pages 550-563

  Marc, Daniel ^a  

^a UR1282   (France)

Author keywords

Aptamers; Prion; PrP; Review; SELEX

Indexed keywords

SACCHAROMYCES CEREVISIAE;

APTAMER; NUCLEIC ACID;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PRION; PROTEIN BINDING; REVIEW; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; APTAMERS, NUCLEOTIDE; BINDING SITES; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEIC ACIDS; PRIONS; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 77951243963     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3633     Document Type: Article

References (123)

1. Aguzzi A, F. Baumann, J. Bremer: The prion's elusive reason for being. Annu Rev Neurosci 31, 439-477 (2008)
2. Alper T, W. A. Cramp, D. A. Haig, M. C. Clarke: Does the agent of scrapie replicate without nucleic acid? Nature 214, 764-766 (1967)
3. Gibbons R. A, G. D. Hunter: Nature of the scrapie agent. Nature 215, 1041-1043 (1967)
4. Griffith J. S: Self-replication and scrapie. Nature 215, 1043-1044 (1967)
5. Marsh R. F, J. S. Semancik, K. C. Medappa, R. P. Hanson, R. R. Rueckert: Scrapie and transmissible mink encephalopathy: search for infectious nucleic acid. J Virol 13, 993-996 (1974)
6. Hunter G. D, S. C. Collis, G. C. Millson, R. H. Kimberlin: Search for scrapie-specific RNA and attempts to detect an infectious DNA or RNA. J Gen Virol, 32, 157-162 (1976)
7. Alper T, D. A. Haig, M. C. Clarke: The scrapie agent: evidence against its dependence for replication on intrinsic nucleic acid. J Gen Virol 41, 503-516 (1978) (Pubitemid 9065343)
8. Ward R. L, D. D. Porter, J. G. Stevens: Nature of the scrapie agent: evidence against a viroid. J Virol 14, 1099-1103 (1974)
9. Diener T. O, M. P. McKinley, S. B. Prusiner: Viroids and prions. Proc Natl Acad Sci U S A 79, 5220-5224 (1982) (Pubitemid 12002189)
10. Bellinger-Kawahara C, T. O. Diener, M. P. McKinley, D. F. Groth, D. R. Smith, S. B. Prusiner: Purified scrapie prions resist inactivation by procedures that hydrolyze, modify, or shear nucleic acids. Virology 160, 271-274 (1987)
11. Prusiner S. B: Prions. Proc Natl Acad Sci U S A 95, 13363-13383 (1998) (Pubitemid 28525623)
12. Prusiner S. B: Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144 (1982) (Pubitemid 12089840)
13. Borras T, C. J. Gibbs, Jr.: Molecular hybridization studies with scrapie brain nucleic acids. I. Search for specific DNA sequences. Arch Virol 88, 67-78 (1986) (Pubitemid 16148607)
14. Sasaki K, K. Tanaka, M. Ito, H. Isomura, M. Horiuchi, N. Ishiguro, M. Shinagawa: Biological activity of subfractions from scrapie-associated fibrils. Virus Res 23, 241-251 (1992)
15. Aiken J. M, R. F. Marsh: The search for scrapie agent nucleic acid. Microbiol Rev 54, 242-246 (1990)
16. Oesch B, D. F. Groth, S. B. Prusiner, C. Weissmann: Search for a scrapie-specific nucleic acid: a progress report. Ciba Found Symp 135, 209-223 (1988)
17. Safar J. G, K. Kellings, A. Serban, D. Groth, J. E. Cleaver, S. B. Prusiner, D. Riesner: Search for a prionspecific nucleic acid. J Virol 79, 10796-10806 (2005)
18. Tuite M. F, B. S. Cox: Propagation of yeast prions. Nat Rev Mol Cell Biol 4, 878-890 (2003)
19. Tanaka M, P. Chien, N. Naber, R. Cooke, J. S. Weissman: Conformational variations in an infectious protein determine prion strain differences. Nature 428, 323-328 (2004) (Pubitemid 38418803)
20. Toyama B. H, M. J. Kelly, J. D. Gross, J. S. Weissman: The structural basis of yeast prion strain variants. Nature 449, 233-237 (2007) (Pubitemid 47402368)
21. Shewmaker F, R. B. Wickner, R. Tycko: Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci U S A 103, 19754-19759 (2006) (Pubitemid 46037503)
22. King C. Y, R. Diaz-Avalos: Protein-only transmission of three yeast prion strains. Nature 428, 319-323 (2004) (Pubitemid 38418802)
23. Cobb N. J, F. D. Sonnichsen, H. McHaourab, W. K. Surewicz: Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc Natl Acad Sci U S A 104, 18946-18951 (2007)
24. Cobb N. J, W. K. Surewicz: Prion strains under the magnifying glass. Nat Struct Mol Biol 14, 882-884 (2007) (Pubitemid 47525167)
25. Legname G, H. O. Nguyen, D. Peretz, F. E. Cohen, S. J. DeArmond, S. B. Prusiner: Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci U S A 103, 19105-19110 (2006) (Pubitemid 350002835)
26. Marc D, R. Mercey, F. Lantier: Scavenger, transducer, RNA chaperone? What ligands of the prion protein teach us about its function. Cell Mol Life Sci 64, 815-829 (2007) (Pubitemid 46597751)
27. Nandi P. K: Interaction of prion peptide HuPrP106-126 with nucleic acid. Arch Virol 142, 2537-2545 (1997)
28. Forloni G, N. Angeretti, R. Chiesa, E. Monzani, M. Salmona, O. Bugiani, F. Tagliavini: Neurotoxicity of a prion protein fragment. Nature 362, 543-546 (1993) (Pubitemid 23113029)
29. Selvaggini C, L. De Gioia, L. Cantu, E. Ghibaudi, L. Diomede, F. Passerini, G. Forloni, O. Bugiani, F. Tagliavini, M. Salmona: Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem Biophys Res Commun 194, 1380-1386 (1993) (Pubitemid 23255035)
30. Nandi P. K: Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution. Arch Virol 143, 1251-1263 (1998) (Pubitemid 28371590)
31. Ellington A. D, J.W. Szostak: In vitro selection of RNA molecules that bind specific ligands. Nature 346, 818-822 (1990)
32. Tuerk C, L. Gold: Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249, 505-510 (1990)
33. Bartel D. P: Re-creating an RNA replicase. In: The RNA World. Eds: Gesteland R. F, Cech T. R, Atkins J. F, Cold Spring Harbor Laboratory Press, NY (1999)
34. Lawrence M. S, D. P. Bartel: New ligase-derived RNA polymerase ribozymes. Rna 11, 1173-1180 (2005) (Pubitemid 41132389)
35. Piganeau N, V. Thuillier, M. Famulok: In vitro selection of allosteric ribozymes: theory and experimental validation. J Mol Biol 312, 1177-1190 (2001) (Pubitemid 32980333)
36. Salehi-Ashtiani K, A. Luptak, A. Litovchick, J. W. Szostak: A genomewide search for ribozymes reveals an HDV-like sequence in the human CPEB3 gene. Science 313, 1788-1792 (2006) (Pubitemid 44454155)
37. Shtatland T, S. C. Gill, B. E. Javornik, H. E. Johansson, B. S. Singer, O. C. Uhlenbeck, D. A. Zichi, L. Gold: Interactions of Escherichia coli RNA with bacteriophage MS2 coat protein: genomic SELEX. Nucleic Acids Res 28, E93 (2000)
38. Lorenz C, F. von Pelchrzim, R. Schroeder: Genomic systematic evolution of ligands by exponential enrichment (Genomic SELEX) for the identification of protein-binding RNAs independent of their expression levels. Nat Protoc 1, 2204-2212 (2006)
39. Yang Y, D. Yang, H. J. Schluesener, Z. Zhang: Advances in SELEX and application of aptamers in the central nervous system. Biomol Eng 24, 583-592 (2007) (Pubitemid 350137885)
40. Alvarez-Salas L. M: Nucleic acids as therapeutic agents. Curr Top Med Chem 8, 1379-1404 (2008)
41. Kaur G, I. Roy: Therapeutic applications of aptamers. Expert Opin Investig Drugs 17, 43-60 (2008) (Pubitemid 351578210)
42. Sterba K. M, S. G. Mackintosh, J. S. Blevins, B. K. Hurlburt, M. S. Smeltzer: Characterization of Staphylococcus aureus SarA binding sites. J Bacteriol 185, 4410-4417 (2003) (Pubitemid 36890487)
43. Liang X, T. J. Nazarenus, J. M. Stone: Identification of a consensus DNA-binding site for the Arabidopsis thaliana SBP domain transcription factor, AtSPL14, and binding kinetics by surface plasmon resonance. Biochemistry 47, 3645-3653 (2008) (Pubitemid 351431353)
44. Symensma T. L, L. Giver, M. Zapp, G. B. Takle, A. D. Ellington: RNA aptamers selected to bind human immunodeficiency virus type 1 Rev in vitro are Rev responsive in vivo. J Virol 70, 179-187 (1996) (Pubitemid 126508784)
45. Weiss S, D. Proske, M. Neumann, M. H. Groschup, H. A. Kretzschmar, M. Famulok, E. L. Winnacker: RNA aptamers specifically interact with the prion protein PrP. J Virol 71, 8790-8797 (1997) (Pubitemid 27446463)
46. Takemura K, P. Wang, I. Vorberg, W. Surewicz, S. A. Priola, A. Kanthasamy, R. Pottathil, S. G. Chen, S. Sreevatsan: DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity. Exp Biol Med (Maywood) 231, 204-214 (2006) (Pubitemid 43213458)
47. Sekiya S, F. Nishikawa, K. Noda, P. K. Kumar, T. Yokoyama, S. Nishikawa: In vitro selection of RNA aptamers against cellular and abnormal isoform of mouse prion protein. Nucleic Acids Symp Ser (Oxf) 361-362 (2005)
48. Mercey R, I. Lantier, M. C. Maurel, J. Grosclaude, F. Lantier, D. Marc: Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Arch Virol, 151:2197-214 (2006) (Pubitemid 44627756)
49. Bibby D. F, A. C. Gill, L. Kirby, C. F. Farquhar, M. E. Bruce, J. A. Garson: Application of a novel in vitro selection technique to isolate and characterise high affinity DNA aptamers binding mammalian prion proteins. J Virol Methods 151, 107-115 (2008)
50. Rhie A, L. Kirby, N. Sayer, R. Wellesley, P. Disterer, I. Sylvester, A. Gill, J. Hope, W. James, A. Tahiri-Alaoui: Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. J Biol Chem 278, 39697-39705 (2003) (Pubitemid 37248531)
51. Proske D, S. Gilch, F. Wopfner, H. M. Schatzl, E. L. Winnacker, M. Famulok: Prion-protein-specific aptamer reduces PrPSc formation. Chembiochem 3, 717-725 (2002) (Pubitemid 36004511)
52. Stoltenburg R, C. Reinemann, B. Strehlitz: SELEX- a (r)evolutionary method to generate high-affinity nucleic acid ligands. Biomol Eng 24, 381-403 (2007) (Pubitemid 47391579)
53. Ogasawara D, H. Hasegawa, K. Kaneko, K. Sode, K. Ikebukuro: Screening of DNA aptamer against mouse prion protein by competitive selection. Prion 1, 248-254 (2007)
54. Ellington A. D, J. W. Szostak: Selection in vitro of single-stranded DNA molecules that fold into specific ligand-binding structures. Nature 355, 850-852 (1992)
55. Nandi P. K, E. Leclerc: Polymerization of murine recombinant prion protein in nucleic acid solution. Arch Virol 144, 1751-1763 (1999) (Pubitemid 29490035)
56. Cordeiro Y, F. Machado, L. Juliano, M.A. Juliano, R. R. Brentani, D. Foguel, and J. L. Silva: DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J Biol Chem 276, 49400-49409 (2001)
57. Bera A, A.C. Roche, P. K. Nandi: Bending and unwinding of nucleic acid by prion protein. Biochemistry 46, 1320-1328 (2007) (Pubitemid 46208479)
58. Gabus C, S. Auxilien, C. Pechoux, D. Dormont, W. Swietnicki, M. Morillas, W. Surewicz, P. Nandi, J. L. Darlix: The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. J Mol Biol 307, 1011-1021 (2001) (Pubitemid 33031273)
59. Gabus C, E. Derrington, P. Leblanc, J. Chnaiderman, D. Dormont, W. Swietnicki, M. Morillas, W. K. Surewicz, D. Marc, P. Nandi, J. L. Darlix: The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. J Biol Chem 276, 19301-19309 (2001)
60. Adler V, B. Zeiler, V. Kryukov, R. Kascsak, R. Rubenstein, A. Grossman: Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro. J Mol Biol 332, 47-57 (2003) (Pubitemid 36999730)
61. Zeiler B, V. Adler, V. Kryukov, A. Grossman: Concentration and removal of prion proteins from biological solutions. Biotechnol Appl Biochem 37, 173-182 (2003) (Pubitemid 36399012)
62. Vasan V, P. Y. Mong, A. Grossman: Interaction of prion protein with small highly structured RNAs: detection and characterization of PrP-oligomers. Neurochem Res 31, 629-637 (2006) (Pubitemid 43886411)
63. Matsugami A, T. Mashima, F. Nishikawa, K. Murakami, S. Nishikawa, K. Noda, T. Yokoyama, M. Katahira: Structural analysis of r(GGA)4 found in RNA aptamer for bovine prion protein. Nucleic Acids Symp Ser (Oxf) 179-180 (2008)
64. Murakami K, F. Nishikawa, K. Noda, T. Yokoyama, S. Nishikawa: Anti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its beta isoform with high affinity. Prion 2, 73-80 (2008)
65. Nishikawa F, K. Murakami, K. Noda, T. Yokoyama, S. Nishikawa: Detection of structural changes of RNA aptamer containing GGA repeats under the ionic condition using the microchip electrophoresis. Nucleic Acids Symp Ser (Oxf), 397-398 (2007)
66. Sekiya S, K. Noda, F. Nishikawa, T. Yokoyama, P.K. Kumar, S. Nishikawa: Characterization and application of a novel RNA aptamer against the mouse prion protein. J Biochem 139, 383-390 (2006) (Pubitemid 43667102)
67. Keniry M. A: Quadruplex structures in nucleic acids. Biopolymers, 56:123-46 (2000) (Pubitemid 33115749)
68. Huppert J. L, A. Bugaut, S. Kumari, S. Balasubramanian: G-quadruplexes: the beginning and end of UTRs. Nucleic Acids Res 36, 6260-6268 (2008)
69. Gatto B, M. Palumbo, C. Sissi: Nucleic Acid aptamers based on the g-quadruplex structure: therapeutic and diagnostic potential. Curr Med Chem 16, 1248-1265 (2009)
70. Darnell J. C, K. B. Jensen, P. Jin, V. Brown, S. T. Warren, R. B. Darnell: Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell 107, 489-499 (2001) (Pubitemid 33152784)
71. Sayer N. M, M. Cubin, A. Rhie, M. Bullock, A. Tahiri-Alaoui, W. James: Structural determinants of conformationally selective, prion-binding aptamers. J Biol Chem 279, 13102-13109 (2004) (Pubitemid 38445888)
72. Shultzaberger R. K, T. D. Schneider: Using sequence logos and information analysis of Lrp DNA binding sites to investigate discrepanciesbetween natural selection and SELEX. Nucleic Acids Res 27, 882-887 (1999) (Pubitemid 29209378)
73. Hogan D. J, D. P. Riordan, A. P. Gerber, D. Herschlag, P. O. Brown: Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system. PLoS Biol 6, e255 (2008)
74. Wu H, A. Henras, G. Chanfreau, J. Feigon: Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III. Proc Natl Acad Sci U S A 101, 8307-8312 (2004) (Pubitemid 38736571)
75. Daugherty M. D, I. D'Orso, A. D. Frankel: A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. Mol Cell 31, 824-834 (2008)
76. Pan T, B. S. Wong, T. Liu, R. Li, R. B. Petersen, M. S. Sy: Cell-surface prion protein interacts with glycosaminoglycans. Biochem J 368, 81-90 (2002) (Pubitemid 35463411)
77. Rajendran K. S, P. D. Nagy: Characterization of the RNA-binding domains in the replicase proteins of tomato bushy stunt virus. J Virol 77, 9244-9258 (2003) (Pubitemid 37011021)
78. Lima L. M, Y. Cordeiro, L. W. Tinoco, A. F. Marques, C. L. Oliveira, S. Sampath, R. Kodali, G. Choi, D. Foguel, L. Torriani, B. Caughey, J. L Silva: Structural insights into the interaction between prion protein and nucleic acid. Biochemistry 45, 9180-9187 (2006) (Pubitemid 44156381)
79. Kovacs G. G, G. Trabattoni, J. A. Hainfellner, J. W. Ironside, R. S. Knight, H. Budka: Mutations of the prion protein gene phenotypic spectrum. J Neurol 249, 1567-1582 (2002) (Pubitemid 35477900)
80. Westaway D, P. A. Goodman, C. A. Mirenda, M. P. McKinley, G. A. Carlson, S. B. Prusiner: Distinct prion proteins in short and long scrapie incubation period mice. Cell 51, 651-662 (1987)
81. Laegreid W. W, M. L. Clawson, M. P. Heaton, B. T. Green, K. I. O'Rourke, D. P. Knowles: Scrapie resistance in ARQ sheep. J Virol 82, 10318-10320 (2008)
82. Hayashi H. K, T. Yokoyama, M. Takata, Y. Iwamaru, M. Imamura, Y. K. Ushiki, M. Shinagawa: The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie. Biochem Biophys Res Commun 328, 1024-1027 (2005) (Pubitemid 40238738)
83. Draper D. E: Themes in RNA-protein recognition. J Mol Biol 293, 255-270 (1999) (Pubitemid 29516168)
84. Shulman-Peleg A, M. Shatsky, R. Nussinov, H. J. Wolfson: Prediction of interacting single-stranded RNA bases by protein-binding patterns. J Mol Biol 379, 299-316 (2008)
85. Bokinsky G, L. G. Nivon, S. Liu, G. Chai, M. Hong, K. M. Weeks, X. Zhuang: Two distinct binding modes of a protein cofactor with its target RNA. J Mol Biol 361, 771-784 (2006) (Pubitemid 44175382)
86. Fairbrother W. G, R. F. Yeh, P. A. Sharp, C. B. Burge: Predictive identification of exonic splicing enhancers in human genes. Science 297, 1007-1013 (2002) (Pubitemid 34856033)
87. Liu J, G. D. Stormo: Combining SELEX with quantitative assays to rapidly obtain accurate models of protein-DNA interactions. Nucleic Acids Res 33, e141 (2005)
88. Roulet E, S. Busso, A. A. Camargo, A. J. Simpson, N. Mermod, P. Bucher: High-throughput SELEX SAGE method for quantitative modeling of transcription-factor binding sites. Nat Biotechnol 20, 831-835 (2002) (Pubitemid 34836762)
89. Ule J, K. Jensen, A. Mele, R. B. Darnell: CLIP: a method for identifying protein-RNA interaction sites in living cells. Methods 37, 376-386 (2005) (Pubitemid 41682508)
90. Licatalosi D. D, A. Mele, J. J. Fak, J. Ule, M. Kayikci, S. W. Chi, T. A. Clark, A. C. Schweitzer, J. E. Blume, X. Wang, J. C. Darnell, R. B. Darnell: HITS-CLIP yields genome-wide insights into brain alternative RNA processing. Nature 456, 464-469 (2008) (Pubitemid 352759008)
91. Guazzaroni M. E, T. Krell, P. Gutierrez del Arroyo, M. Velez, M. Jimenez, G. Rivas, J. L. Ramos: The transcriptional repressor TtgV recognizes a complex operator as a tetramer and induces convex DNA bending. J Mol Biol 369, 927-939 (2007) (Pubitemid 46759526)
92. Derrington E, C. Gabus, P. Leblanc, J. Chnaidermann, L. Grave, D. Dormont, W. Swietnicki, M. Morillas, D. Marc, P. Nandi, J. L. Darlix: PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. C R Acad Sci III 325, 17-23 (2002) (Pubitemid 34855196)
93. Gourine A. V, E. Llaudet, N. Dale, K. M. Spyer: ATP is a mediator of chemosensory transduction in the central nervous system. Nature 436, 108-111 (2005) (Pubitemid 40966194)
94. Mironov A. Jr., D. Latawiec, H. Wille, E. Bouzamondo-Bernstein, G. Legname, R.A. Williamson, D. Burton, S. J. DeArmond, S. B. Prusiner, P. J. Peters: Cytosolic prion protein in neurons. J Neurosci 23, 7183-7193 (2003) (Pubitemid 36975883)
95. Strom A, G. S. Wang, R. Reimer, D. T. Finegood, F. W. Scott: Pronounced cytosolic aggregation of cellular prion protein in pancreatic beta-cells in response to hyperglycemia. Lab Invest 87, 139-149 (2007)
96. Rybner C, S. Finel-Szermanski, M. Felin, T. Sahraoui, C. Rousseau, J. G. Fournier, A. P. Seve, J. Botti: The cellular prion protein: a new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells. J Cell Biochem 84, 408-419 (2002) (Pubitemid 34033299)
97. Stewart R. S, D. A. Harris: A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons. J Biol Chem 280, 15855-15864 (2005) (Pubitemid 40616707)
98. Hegde R. S, J. A. Mastrianni, M. R. Scott, K. A. DeFea, P. Tremblay, M. Torchia, S. J. DeArmond, S. B. Prusiner, V. R. Lingappa: A transmembrane form of the prion protein in neurodegenerative disease. Science 279, 827-834 (1998) (Pubitemid 28106269)
99. Kim S, T. J. Jeon, A. Oberai, D. Yang, J. J. Schmidt, J. U. Bowie: Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins. Proc Natl Acad Sci U S A 102, 14278-14283 (2005) (Pubitemid 41429689)
100. Mange A, C. Crozet, S. Lehmann, F. Beranger: Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin. J Cell Sci 117, 2411-2416 (2004) (Pubitemid 38807507)
101. W.Q. Zou, J. Zheng, D.M. Gray, P. Gambetti, and S.G. Chen: Antibody to DNA detects scrapie but not normal prion protein. Proc Natl Acad Sci U S A, 101:1380-5 (2004) (Pubitemid 38182697)
102. Gomes M. P, T. A. Millen, P. S. Ferreira, N. L. e Silva, T. C. Vieira, M. S. Almeida, J. L. Silva, Y. Cordeiro: Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells. J Biol Chem 283, 19616-19625 (2008)
103. Meijsing S. H, M. A. Pufall, A. Y. So, D. L. Bates, L. Chen, K. R. Yamamoto: DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 324, 407-410 (2009)
104. Korennykh A. V, P. F. Egea, A. A. Korostelev, J. Finer-Moore, C. Zhang, K. M. Shokat, R. M. Stroud, P. Walter: The unfolded protein response signals through high-order assembly of Ire1. Nature 457, 687-693 (2009)
105. Lee J. R, S. S. Lee, H. H. Jang, Y. M. Lee, J. H. Park, S. C. Park, J. C. Moon, S. K. Park, S. Y Kim, S. Y. Lee, H. B. Chae, Y. J. Jung, W. Y. Kim, M. R. Shin, G. W. Cheong, M. G. Kim, K. R. Kang, K. O. Lee, D. J. Yun: Heat-shock dependent oligomeric status alters the function of a plantspecific thioredoxin-like protein, AtTDX. Proc Natl Acad Sci U S A 106, 5978-5983 (2009)
106. Pan T, B. Chang, P. Wong, C. Li, R. Li, S.C. Kang, J.D. Robinson, A. R. Thompsett, P. Tein, S. Yin, G. Barnard, I. McConnell, D. R. Brown, T. Wisniewski, M. S. Sy: An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrP(Sc) aggregates. J Virol 79, 12355-12364 (2005) (Pubitemid 41346097)
107. Ogasawara D, N. S. Hachiya, K. Kaneko, K. Sode, K. Ikebukuro: Detection system based on the conformational change in an aptamer and its application to simple bound/free separation. Biosens Bioelectron 24, 1372-1376 (2008)
108. Gofflot S, M. Deprez, B. el Moualij, A. Osman, J.F. Thonnart, O. Hougrand, E. Heinen, W. Zorzi: Immunoquantitative PCR for prion protein detection in sporadic Creutzfeldt-Jakob disease. Clin Chem 51, 1605-1611 (2005) (Pubitemid 41233094)
109. Barletta J. M, D. C. Edelman, W. E. Highsmith, N. T. Constantine: Detection of ultra-low levels of pathologic prion protein in scrapie infected hamster brain homogenates using real-time immuno-PCR. J Virol Methods 127, 154-164 (2005) (Pubitemid 40828193)
110. Kouassi G. K, P. Wang, S. Sreevatan, J. Irudayaraj: Aptamer-mediated magnetic and gold-coated magnetic nanoparticles as detection assay for prion protein assessment. Biotechnol Prog 23, 1239-1244 (2007) (Pubitemid 47587100)
111. Deleault N. R, R. W. Lucassen, S. Supattapone: RNA molecules stimulate prion protein conversion. Nature 425, 717-720 (2003) (Pubitemid 37314314)
112. Samanta D, D. Mukhopadhyay, S. Chowdhury, J. Ghosh, S. Pal, A. Basu, A. Bhattacharya, A. Das, D. Das, C. DasGupta: Protein folding by domain V of Escherichia coli 23S rRNA: specificity of RNA-protein interactions. J Bacteriol 190, 3344-3352 (2008) (Pubitemid 351581430)
113. Tribouillard-Tanvier D, S. Dos Reis, F. Gug, C. Voisset, V. Beringue, R. Sabate, E. Kikovska, N. Talarek, S. Bach, C. Huang, N. Desban, S. J. Saupe, S. Supattapone, J. Y. Thuret, S. Chedin, D. Vilette, H. Galons, S. Sanyal, M. Blondel: Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs. PLoS ONE, 3, e2174 (2008)
114. Swietnicki W, M. Morillas, S. G. Chen, P. Gambetti, W. K. Surewicz: Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39, 424-431 (2000) (Pubitemid 30056478)
115. Hornemann S, R. Glockshuber: A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc Natl Acad Sci U S A 95, 6010-6014 (1998) (Pubitemid 28248955)
116. Yin S, X. Fan, S. Yu, C. Li, M. S. Sy: Binding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells. J Biol Chem 283, 5446-5454 (2008)
117. Cordeiro Y, J. L. Silva: The hypothesis of the catalytic action of nucleic acid on the conversion of prion protein. Protein Pept Lett 12, 251-255 (2005) (Pubitemid 40428415)
118. Marques A. F, Y. Cordeiro, J. L. Silva, L. M. Lima: Enhanced prion protein stability coupled to DNA recognition and milieu acidification. Biophys Chem 141, 135-139 (2009)
119. Bennett M. J, M. R. Sawaya, D. Eisenberg: Deposition diseases and 3D domain swapping. Structure 14, 811-824 (2006) (Pubitemid 43674098)
120. Whisstock J. C, S. P. Bottomley: Structural biology: Serpins' mystery solved. Nature 455, 1189-1190 (2008)
121. Beaudoin S, K. Goggin, C. Bissonnette, C. Grenier, X. Roucou: Aggresomes do not represent a general cellular response to protein misfolding in mammalian cells. BMC Cell Biol 9, 59 (2008)
122. White M. D, M. Farmer, I. Mirabile, S. Brandner, J. Collinge, G. R. Mallucci: Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease. Proc Natl Acad Sci U S A 105, 10238-10243 (2008)
123. Dyson H. J, P. E. Wright: Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6, 197-208 (2005) (Pubitemid 40314921)