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Volumn 28, Issue 6, 2003, Pages 955-963

Prion protein interactions with nucleic acid: Possible models for prion disease and prion function

Author keywords

BSE; DNA protein interactions; PrP; RNA; RNA protein interactions

Indexed keywords

CHAPERONE; NUCLEIC ACID; PRION PROTEIN;

EID: 0037409731     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023215207981     Document Type: Review
Times cited : (29)

References (90)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.1
  • 3
    • 0027958170 scopus 로고
    • Molecular biology of prion diseases
    • Weissman, C. 1994. Molecular biology of prion diseases. Trends Cell. Biol. 4:10-14.
    • (1994) Trends Cell. Biol. , vol.4 , pp. 10-14
    • Weissman, C.1
  • 5
    • 0002181235 scopus 로고    scopus 로고
    • An introduction to prion biology and diseases
    • Prusiner, S. (eds.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Prusiner, S. 1999. An introduction to prion biology and diseases. Pages 1-66, in Prusiner, S. (eds.), Prion Biology and Diseases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) Prion Biology and Diseases , pp. 1-66
    • Prusiner, S.1
  • 6
    • 0031080867 scopus 로고    scopus 로고
    • Prion protein and the transmissible spongiform encephalopathies
    • Caughey, B. and Chesebro, B. 1997. Prion protein and the transmissible spongiform encephalopathies. Trends Cell. Biol. 7:56-62.
    • (1997) Trends Cell. Biol. , vol.7 , pp. 56-62
    • Caughey, B.1    Chesebro, B.2
  • 7
  • 8
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G., Scott, M., Mastrianni, J., Gabizon, R., Torcia, M., Cohen, F., DeArmond, S., and Prusiner, S. 1995. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torcia, M.5    Cohen, F.6    DeArmond, S.7    Prusiner, S.8
  • 10
    • 0022971602 scopus 로고
    • Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues
    • Robakis, N., Sawh, P., Wolfe, G., Rubenstein, R., Carp, R., and Innis, M. 1986. Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues. Proc. Natl. Acad. Sci. USA 83:6377-6381.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6377-6381
    • Robakis, N.1    Sawh, P.2    Wolfe, G.3    Rubenstein, R.4    Carp, R.5    Innis, M.6
  • 12
    • 0025800143 scopus 로고
    • A 'unified' theory of prion propagation
    • Weissman, C. 1991. A 'unified' theory of prion propagation. Nature 352:679-683.
    • (1991) Nature , vol.352 , pp. 679-683
    • Weissman, C.1
  • 14
    • 0030786717 scopus 로고    scopus 로고
    • Prion research: The next frontiers
    • Aguzzi, A. and Weissmann, C. 2002. Prion research: The next frontiers. Nature 389:795-798.
    • (2002) Nature , vol.389 , pp. 795-798
    • Aguzzi, A.1    Weissmann, C.2
  • 15
    • 4243260098 scopus 로고    scopus 로고
    • Prion research accelerates
    • Borman, S. 1998. Prion research accelerates. Chem. Eng. News 76:22-29.
    • (1998) Chem. Eng. News , vol.76 , pp. 22-29
    • Borman, S.1
  • 16
    • 0023806142 scopus 로고
    • A modified host protein model of scrapie
    • Bolton, D. and Bendheim, P. 1988. A modified host protein model of scrapie. Ciba Found. Symp. 135:164-181.
    • (1988) Ciba Found. Symp. , vol.135 , pp. 164-181
    • Bolton, D.1    Bendheim, P.2
  • 17
    • 0003015566 scopus 로고    scopus 로고
    • Development of the prion concept
    • Prusiner, S. (eds.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Prusiner, S. 1999. Development of the prion concept. Pages 67-112, in Prusiner, S. (eds.), Prion Biology and Diseases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) Prion Biology and Diseases , pp. 67-112
    • Prusiner, S.1
  • 18
    • 0026604959 scopus 로고
    • Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis
    • Kellings, K., Meyer, N., Mirenda, C., Prusiner, S., and Riesner, D. 1992. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis. J. Gen. Virol. 73:1025-1029.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1025-1029
    • Kellings, K.1    Meyer, N.2    Mirenda, C.3    Prusiner, S.4    Riesner, D.5
  • 19
    • 0027758966 scopus 로고
    • Prions and nucleic acids: Search for "residual" nucleic acids and screening for mutations in the PrP-gene
    • Riesner, D., Kellings, K., Wiese, U., Wulfert, M., Mirenda, C., and Prusiner, S. 1993. Prions and nucleic acids: Search for "residual" nucleic acids and screening for mutations in the PrP-gene. Dev. Biol. Stand. 80:173-181.
    • (1993) Dev. Biol. Stand. , vol.80 , pp. 173-181
    • Riesner, D.1    Kellings, K.2    Wiese, U.3    Wulfert, M.4    Mirenda, C.5    Prusiner, S.6
  • 20
    • 0032472239 scopus 로고    scopus 로고
    • BSE and prions: Uncertainties about the agent
    • Chesebro, B. 1998. BSE and prions: Uncertainties about the agent. Science 279:42-43.
    • (1998) Science , vol.279 , pp. 42-43
    • Chesebro, B.1
  • 21
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectroscopy and amino acid sequencing
    • Stahl, N., Baldwin, M., Teplow, D., Hood, L., Gibson, B., Burlingame, A., and Prusiner, S. 1993. Structural studies of the scrapie prion protein using mass spectroscopy and amino acid sequencing. Biochemistry 32:1991-2002.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.2    Teplow, D.3    Hood, L.4    Gibson, B.5    Burlingame, A.6    Prusiner, S.7
  • 22
    • 0032758721 scopus 로고    scopus 로고
    • Prion rods contain an inert polysaccharide scaffold
    • Appel, T., Dumpitak, C., Matthiesen, U., and Riesner, D. 1999. Prion rods contain an inert polysaccharide scaffold. Biol. Chem. 380:1295-1306.
    • (1999) Biol. Chem. , vol.380 , pp. 1295-1306
    • Appel, T.1    Dumpitak, C.2    Matthiesen, U.3    Riesner, D.4
  • 23
    • 0032209164 scopus 로고    scopus 로고
    • Evidence that single-stranded DNA wrapped around the tubulofilamentous particles termed "nemaviruses" is the genome of the scrapie agent
    • Narang, H. 1998. Evidence that single-stranded DNA wrapped around the tubulofilamentous particles termed "nemaviruses" is the genome of the scrapie agent. Res. Virol. 149:375-382.
    • (1998) Res. Virol. , vol.149 , pp. 375-382
    • Narang, H.1
  • 24
    • 0001097996 scopus 로고    scopus 로고
    • Structural studies of prion proteins
    • Prusiner, S. (eds.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Cohen, F. and Prusiner, S. 1999. Structural studies of prion proteins. Pages 191-228, in Prusiner, S. (eds.), Prion Biology and Disease. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) Prion Biology and Disease , pp. 191-228
    • Cohen, F.1    Prusiner, S.2
  • 25
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill, A., Antoniou, M., and Collinge, J. 1999. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80:11-14.
    • (1999) J. Gen. Virol. , vol.80 , pp. 11-14
    • Hill, A.1    Antoniou, M.2    Collinge, J.3
  • 26
    • 0027509675 scopus 로고
    • Attempts to restore scrapie prion infectivity after exposure to protein denaturants
    • Prusiner, S., Groth, D., Serban, A., Stahl, N., and Gabizon, R. 1993. Attempts to restore scrapie prion infectivity after exposure to protein denaturants. Proc. Natl. Acad. Sci. USA 90:2793-2797.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2793-2797
    • Prusiner, S.1    Groth, D.2    Serban, A.3    Stahl, N.4    Gabizon, R.5
  • 27
    • 0033580818 scopus 로고    scopus 로고
    • Protease-resistant and detergent-insoluble prion protein is not neccessarily associated with prion infectivity
    • Shaked, G., Fridlander, G., Meiner, Z., Taraboulos, A., and Gabizon, R. 1999. Protease-resistant and detergent-insoluble prion protein is not neccessarily associated with prion infectivity. J. Biol. Chem. 274:17981-17986.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17981-17986
    • Shaked, G.1    Fridlander, G.2    Meiner, Z.3    Taraboulos, A.4    Gabizon, R.5
  • 28
    • 0027097965 scopus 로고
    • Relationship of protease-resistant protein, scrapie-associated fibrils and tubulofilamentous particles to the agent of spongiform encephalopathies
    • Narang, H. 1992. Relationship of protease-resistant protein, scrapie-associated fibrils and tubulofilamentous particles to the agent of spongiform encephalopathies. Res. Virol. 143:381-386.
    • (1992) Res. Virol. , vol.143 , pp. 381-386
    • Narang, H.1
  • 29
    • 0033542142 scopus 로고    scopus 로고
    • Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone
    • Saborio, G., Soto, C., Kascsak, R., Levy, E., Kascsak, R., Harris, D., and Frangione, B. 1999. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Com. 258: 470-475.
    • (1999) Biochem. Biophys. Res. Com. , vol.258 , pp. 470-475
    • Saborio, G.1    Soto, C.2    Kascsak, R.3    Levy, E.4    Kascsak, R.5    Harris, D.6    Frangione, B.7
  • 30
    • 0035253413 scopus 로고    scopus 로고
    • Pseudoknots in prion protein mRNAs confirmed by comparative sequence analysis and pattern searching
    • Barrette, I., Poisson, G., Gendron, P., and Major, F. 2001. Pseudoknots in prion protein mRNAs confirmed by comparative sequence analysis and pattern searching. Nucleic Acids Res. 29:753-758.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 753-758
    • Barrette, I.1    Poisson, G.2    Gendron, P.3    Major, F.4
  • 31
    • 0029908504 scopus 로고    scopus 로고
    • Protein secondary structural types are differentially coded on messenger RNA
    • Thanaraj, T. and Argos, P. 1996. Protein secondary structural types are differentially coded on messenger RNA. Protein Sci. 5:1973-1983.
    • (1996) Protein Sci. , vol.5 , pp. 1973-1983
    • Thanaraj, T.1    Argos, P.2
  • 33
    • 0035918202 scopus 로고    scopus 로고
    • Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus
    • Hölscher, C., Bach, U., and Dobberstein, B. 2001. Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus. J. Biol. Chem. 276:13388-13394.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13388-13394
    • Hölscher, C.1    Bach, U.2    Dobberstein, B.3
  • 34
    • 0036500554 scopus 로고    scopus 로고
    • Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes
    • Baron, G., Wehrly, K., Dorward, D., Chesebro, B., and Caughey, B. 2002. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO 21:1031-1040.
    • (2002) EMBO , vol.21 , pp. 1031-1040
    • Baron, G.1    Wehrly, K.2    Dorward, D.3    Chesebro, B.4    Caughey, B.5
  • 36
    • 0030896017 scopus 로고    scopus 로고
    • In vivo toxicity of prion protein in murine scrapie: Ultrastructural and immunogold studies
    • Jeffrey, M., Goodsir, C., Bruce, M., McBride, P., and Fraser, J. 1997. In vivo toxicity of prion protein in murine scrapie: ultrastructural and immunogold studies. Neuropathol. Appl. Neurobiol. 23:93-1001.
    • (1997) Neuropathol. Appl. Neurobiol. , vol.23 , pp. 93-1001
    • Jeffrey, M.1    Goodsir, C.2    Bruce, M.3    McBride, P.4    Fraser, J.5
  • 37
    • 0026472737 scopus 로고
    • Infection specific prion protein (PrP) accumulates on neuronal plasmalemma in scrapie infected mice
    • Jeffrey, M., Goodsir, C., Bruce, M., McBride, P., Scott, J., and Halliday, W. 1992. Infection specific prion protein (PrP) accumulates on neuronal plasmalemma in scrapie infected mice. Neurosci. Lett. 147:106-109.
    • (1992) Neurosci. Lett. , vol.147 , pp. 106-109
    • Jeffrey, M.1    Goodsir, C.2    Bruce, M.3    McBride, P.4    Scott, J.5    Halliday, W.6
  • 38
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D., Taraboulos, A., and Prusiner, S. 1992. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267:16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.1    Taraboulos, A.2    Prusiner, S.3
  • 39
    • 0025876226 scopus 로고
    • N-Terminal truncation of the scrapie-associated form of PrP by lysosomalprotease(s): Implications regarding the site of conversion to the protease-resistant state
    • Caughey, B., Raymond, G., Ernst, D., and Race, R. 1991. N-Terminal truncation of the scrapie-associated form of PrP by lysosomalprotease(s): Implications regarding the site of conversion to the protease-resistant state. J. Virol. 65:6597-6603.
    • (1991) J. Virol. , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.2    Ernst, D.3    Race, R.4
  • 43
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • Hornshaw, M., McDermott, J., and Candy, J. 1995. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Bioc. Biophys. Res. Commun. 207:621-629.
    • (1995) Bioc. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.1    McDermott, J.2    Candy, J.3
  • 46
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host protein in neurotoxicity of a prion protein fragment
    • Brown, D., Schmidt, B., and Kretzschmar, H. 1996. Role of microglia and host protein in neurotoxicity of a prion protein fragment. Nature 380:345-347.
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.1    Schmidt, B.2    Kretzschmar, H.3
  • 47
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • Korth, C., May, B., Cohen, F., and Prusiner, S. 2001. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. USA 98:9836-9841.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.2    Cohen, F.3    Prusiner, S.4
  • 51
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein, T., Kirsch, D., Kaufmann, R., and Riesner, D. 1998. Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry. Biol. Chem. 379:655-666.
    • (1998) Biol. Chem. , vol.379 , pp. 655-666
    • Klein, T.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 52
    • 0035957944 scopus 로고    scopus 로고
    • Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods
    • Shaked, G., Meiner, Z., Avraham, I., Taraboulos, A., and Gabizon, R. 2001. Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods. J. Biol. Chem. 276:14321-14328.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14321-14328
    • Shaked, G.1    Meiner, Z.2    Avraham, I.3    Taraboulos, A.4    Gabizon, R.5
  • 53
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-Sheet conformation and inhibits prion peptide aggregation
    • Cordeiro, Y., Machado, F., Juliano, L., Aparecida Juliano, M., Brentani, R., Foguel, D., and Silva, J. 2001. DNA converts cellular prion protein into the beta-Sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276: 49400-49409.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3    Aparecida Juliano, M.4    Brentani, R.5    Foguel, D.6    Silva, J.7
  • 56
    • 0031875169 scopus 로고    scopus 로고
    • Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution
    • Nandi, P. 1998. Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution. Arch. Virol. 143:1251-1263.
    • (1998) Arch. Virol. , vol.143 , pp. 1251-1263
    • Nandi, P.1
  • 57
    • 0032880060 scopus 로고    scopus 로고
    • Polymerization of murine recombinant prion protein in nucleic acid solution
    • Nandi, P. and Leclerc, E. 1999. Polymerization of murine recombinant prion protein in nucleic acid solution. Arch. Virol. 144:1751-1763.
    • (1999) Arch. Virol. , vol.144 , pp. 1751-1763
    • Nandi, P.1    Leclerc, E.2
  • 59
    • 0037383735 scopus 로고    scopus 로고
    • Concentration and removal of prion proteins from biological solutions
    • Zeiler, B., Adler, V., Kryukov, V., and Grossman, A. 2002. Concentration and removal of prion proteins from biological solutions. Biotech. Appl. Biochem., 37:173-182.
    • (2002) Biotech. Appl. Biochem. , vol.37 , pp. 173-182
    • Zeiler, B.1    Adler, V.2    Kryukov, V.3    Grossman, A.4
  • 60
    • 0032892505 scopus 로고    scopus 로고
    • Scrapie strain-specific interactions with endogenous murine leukemia virus
    • Carp, R., Meeker, H., Caruso, V., and Sersen, E. 1999. Scrapie strain-specific interactions with endogenous murine leukemia virus. J. Gen. Virol. 80:5-10.
    • (1999) J. Gen. Virol. , vol.80 , pp. 5-10
    • Carp, R.1    Meeker, H.2    Caruso, V.3    Sersen, E.4
  • 61
    • 0031766743 scopus 로고    scopus 로고
    • Analysis of the incubation periods, induction of obesity and histopathological changes in senescence-prone and senescenceresistant mice infected with various scrapie strains
    • Carp, R., Meeker, H., Sersen, E., and Kozlowski, P. 1998. Analysis of the incubation periods, induction of obesity and histopathological changes in senescence-prone and senescenceresistant mice infected with various scrapie strains. J. Gen. Virol. 79:2863-2869.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2863-2869
    • Carp, R.1    Meeker, H.2    Sersen, E.3    Kozlowski, P.4
  • 62
    • 0033777826 scopus 로고    scopus 로고
    • The role of prion peptide structure and aggregation in toxicity and membrane binding
    • Rymer, D. and Good, T. 2000. The role of prion peptide structure and aggregation in toxicity and membrane binding. J. Neurochem. 75:2536-2545.
    • (2000) J. Neurochem. , vol.75 , pp. 2536-2545
    • Rymer, D.1    Good, T.2
  • 68
    • 0029964280 scopus 로고    scopus 로고
    • Cytotoxicity of prion protein peptide (PrP106126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, A beta 25-35
    • Hope, J., Shearman, M., Baxter, H., Chong, A., Kelly, S., and Price, N. 1996. Cytotoxicity of prion protein peptide (PrP106126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, A beta 25-35. Neurodegeneration. 5: 1-11.
    • (1996) Neurodegeneration , vol.5 , pp. 1-11
    • Hope, J.1    Shearman, M.2    Baxter, H.3    Chong, A.4    Kelly, S.5    Price, N.6
  • 69
    • 0031457157 scopus 로고    scopus 로고
    • Interaction of prion peptide HuPrP106-126 with nucleic acid
    • Nandi, P. 1997. Interaction of prion peptide HuPrP106-126 with nucleic acid. Arch. Virol. 142:2537-2545.
    • (1997) Arch. Virol. , vol.142 , pp. 2537-2545
    • Nandi, P.1
  • 72
    • 0034682866 scopus 로고    scopus 로고
    • Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus
    • Li, R., Liu, T., Wong, B., Pan, T., Morillas, M., Swietnicki, W., O'Rourke, K., Gambetti, P., Surewicz, W., and Sy, M. 2000. Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. J. Mol. Biol. 301:567-573.
    • (2000) J. Mol. Biol. , vol.301 , pp. 567-573
    • Li, R.1    Liu, T.2    Wong, B.3    Pan, T.4    Morillas, M.5    Swietnicki, W.6    O'Rourke, K.7    Gambetti, P.8    Surewicz, W.9    Sy, M.10
  • 73
    • 0035088898 scopus 로고    scopus 로고
    • Murine recombinant prion protein induces ordered aggregation of linear nucleic acids to condensed globular structures
    • Nandi, P. and Sizaret, P. 2001. Murine recombinant prion protein induces ordered aggregation of linear nucleic acids to condensed globular structures. Arch. Virol. 146:327-345.
    • (2001) Arch. Virol. , vol.146 , pp. 327-345
    • Nandi, P.1    Sizaret, P.2
  • 74
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • Darlix, J., Lapadat-Tapolsky, M., de Rocquigny, H., and Roques, B. 1995. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses. J. Mol. Biol. 254:523-537.
    • (1995) J. Mol. Biol. , vol.254 , pp. 523-537
    • Darlix, J.1    Lapadat-Tapolsky, M.2    De Rocquigny, H.3    Roques, B.4
  • 78
    • 0028133360 scopus 로고
    • Cleavage of p15 protein in vitro by human immunodeficiency virus type 1 protease in RNA dependent
    • Sheng, N. and Erickson-Viitanen, S. 1994. Cleavage of p15 protein in vitro by human immunodeficiency virus type 1 protease in RNA dependent. J. Virol. 68:6207-6214.
    • (1994) J. Virol. , vol.68 , pp. 6207-6214
    • Sheng, N.1    Erickson-Viitanen, S.2
  • 79
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie protein propagation
    • Kaneko, K., Zulianello, L., Scott, M., Cooper, C., Wallace, A., James, T., Cohen, F., and Prusiner, S. 1997. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie protein propagation. Proc. Natl. Acad. Sci. USA 94:10069-10074.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3    Cooper, C.4    Wallace, A.5    James, T.6    Cohen, F.7    Prusiner, S.8
  • 80
    • 0034736063 scopus 로고    scopus 로고
    • Modeling a prion protein dimer: Predictions for fibril formation
    • Warwicker, J. 2000. Modeling a prion protein dimer: Predictions for fibril formation. Biochem. Biophys. Res. Commun. 278:646-652.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 646-652
    • Warwicker, J.1
  • 82
    • 0034869693 scopus 로고    scopus 로고
    • Crystal structure of the human prion protein reveals a mechanism for oligomerization
    • Knaus, K., Morillas, M., Swietnicki, W., Malone, M., Surewicz, W., and Yee, V. 2001. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat. Struct. Biol. 8:770-774.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 770-774
    • Knaus, K.1    Morillas, M.2    Swietnicki, W.3    Malone, M.4    Surewicz, W.5    Yee, V.6
  • 83
    • 0034603154 scopus 로고    scopus 로고
    • Adaptive recognition by nucleic acid aptamers
    • Hermann, T. and Patel, D. 2000. Adaptive recognition by nucleic acid aptamers. Science 287:820-825.
    • (2000) Science , vol.287 , pp. 820-825
    • Hermann, T.1    Patel, D.2
  • 84
    • 0033485558 scopus 로고    scopus 로고
    • Non-Watson-Crick base pairs in RNA-protein recognition
    • Hermann, T. and Westhof, E. 1999. Non-Watson-Crick base pairs in RNA-protein recognition. Chem. Biol. 6:R335-R343.
    • (1999) Chem. Biol. , vol.6
    • Hermann, T.1    Westhof, E.2
  • 85
    • 0002200325 scopus 로고    scopus 로고
    • RNA Interaction with small ligands and peptides
    • Pages in Cech, T. and Atkins, J. (eds.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Puglisi, J. and Williamson, J. 1999. RNA Interaction with small ligands and peptides. Pages in Cech, T. and Atkins, J. (eds.), The RNA World. 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 403-425.
    • (1999) The RNA World. 2nd Ed. , pp. 403-425
    • Puglisi, J.1    Williamson, J.2
  • 86
    • 0016753631 scopus 로고
    • Infectious etiology of neuritic (senile) plaques in mice
    • Wisniewski, H., Bruce, M., and Fraser, H. 1975. Infectious etiology of neuritic (senile) plaques in mice. Science 190:1108-1110.
    • (1975) Science , vol.190 , pp. 1108-1110
    • Wisniewski, H.1    Bruce, M.2    Fraser, H.3
  • 87
    • 0036289319 scopus 로고    scopus 로고
    • Selection of RNA aptamers to the Alzheimer's disease amyloid peptide
    • Ylera, F., Lurz, R., Erdmann, V., and Fürste, J. 2002. Selection of RNA aptamers to the Alzheimer's disease amyloid peptide. Biochem. Biophys. Res. Commun. 290:1583-1588.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 1583-1588
    • Ylera, F.1    Lurz, R.2    Erdmann, V.3    Fürste, J.4
  • 89
    • 0036707495 scopus 로고    scopus 로고
    • BetaAPP and furin mRNA concentrates in immature senile plaques in the brain of Alzheimer patients
    • Marcinkiewiczs, M. 2002. BetaAPP and furin mRNA concentrates in immature senile plaques in the brain of Alzheimer patients. J. Neuropathol. Exp. Neurol, 61:815-829.
    • (2002) J. Neuropathol. Exp. Neurol. , vol.61 , pp. 815-829
    • Marcinkiewiczs, M.1
  • 90
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E., and Mandelkow, E. 1996. RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399:344-349.
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.4    Mandelkow, E.5


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