메뉴 건너뛰기




Volumn 273, Issue 6, 2006, Pages 1285-1299

Synthesis and structural characterization of a mimetic membrane-anchored prion protein

Author keywords

Conversion; GPI; Membranes; Prion; rafts

Indexed keywords

CYSTEINE; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN; PRION PROTEIN; RECOMBINANT PROTEIN;

EID: 33644747643     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05152.x     Document Type: Article
Times cited : (33)

References (65)
  • 1
    • 0023676109 scopus 로고
    • Purification and properties of the cellular and scrapie hamster prion proteins
    • Turk E Teplow D Hood L Prusiner S 1988 Purification and properties of the cellular and scrapie hamster prion proteins Eur J Biochem 176 21 30
    • (1988) Eur J Biochem , vol.176 , pp. 21-30
    • Turk, E.1    Teplow, D.2    Hood, L.3    Prusiner, S.4
  • 5
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N Borchelt DR Hsiao K Prusiner SB 1987 Scrapie prion protein contains a phosphatidylinositol glycolipid Cell 51 229 240
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 6
    • 0024434503 scopus 로고
    • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
    • Endo T Groth D Prusiner SB Kobata A 1989 Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein Biochemistry 28 8380 8388
    • (1989) Biochemistry , vol.28 , pp. 8380-8388
    • Endo, T.1    Groth, D.2    Prusiner, S.B.3    Kobata, A.4
  • 7
    • 0025944507 scopus 로고
    • 7-30 in water by infrared spectroscopy
    • ) Secondary structure analysis of the scrapie-associated protein PrP 2
    • Caughey BW Dong A Bhat KS Ernst D Hayes SF Caughey WS 1991 ) Secondary structure analysis of the scrapie-associated protein PrP 2 7-30 in water by infrared spectroscopy Biochemistry 30 7672 7680
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 10
    • 0034931126 scopus 로고    scopus 로고
    • Three-dimensional structures of prion proteins
    • Wuthrich K Riek R 2001 Three-dimensional structures of prion proteins Adv Protein Chem 57 55 82
    • (2001) Adv Protein Chem , vol.57 , pp. 55-82
    • Wuthrich, K.1    Riek, R.2
  • 11
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw MP McDermott JR Candy JM Lakey JH 1995 Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides Biochem Biophys Res Commun 214 993 999
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 15
    • 12144271772 scopus 로고    scopus 로고
    • NMR structure of the bovine prion protein isolated from healthy calf brains
    • Hornemann S Schorn C Wuthrich K 2004 NMR structure of the bovine prion protein isolated from healthy calf brains EMBO Rep 5 1159 1164
    • (2004) EMBO Rep , vol.5 , pp. 1159-1164
    • Hornemann, S.1    Schorn, C.2    Wuthrich, K.3
  • 16
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed beta-helices into trimers
    • Govaerts C Wille H Prusiner SB Cohen FE 2004 Evidence for assembly of prions with left-handed beta-helices into trimers Proc Natl Acad Sci USA 101 8342 8347
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 18
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng SL Huber MT Harris DA 1993 A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells J Biol Chem 268 15922 15928
    • (1993) J Biol Chem , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 19
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N Stein R Yanai A Friedlander G Taraboulos A 1997 Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform J Biol Chem 272 6324 6331
    • (1997) J Biol Chem , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 21
    • 0024545093 scopus 로고
    • Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells
    • Caughey B Race RE Ernst D Buchmeier MJ Chesebro B 1989 Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells J Virol 63 175 181
    • (1989) J Virol , vol.63 , pp. 175-181
    • Caughey, B.1    Race, R.E.2    Ernst, D.3    Buchmeier, M.J.4    Chesebro, B.5
  • 22
    • 0025876226 scopus 로고
    • N-Terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B Raymond GJ Ernst D Race RE 1991 N-Terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state J Virol 65 6597 6603
    • (1991) J Virol , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 23
    • 0030964917 scopus 로고    scopus 로고
    • COOH-Terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko K Vey M Scott M Pilkuhn S Cohen FE Prusiner SB 1997 COOH-Terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform Proc Natl Acad Sci USA 94 2333 2338
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 24
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris DA 1999 Cellular biology of prion diseases Clin Microbiol Rev 12 429 444
    • (1999) Clin Microbiol Rev , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 25
  • 27
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • [Published erratum (1995) J Cell Biol130, 501]
    • Taraboulos A Scott M Semenov A Avrahami D Laszlo L Prusiner S Avraham D 1995 Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform J Cell Biol 129 121 132. [Published erratum (1995) J Cell Biol130, 501.]
    • (1995) J Cell Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszlo, L.5    Prusiner, S.6    Avraham, D.7
  • 29
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt D Taraboulos A 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
  • 30
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey B Raymond G 1991 The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive J Biol Chem 266 18217 18223
    • (1991) J Biol Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.2
  • 31
    • 0033947543 scopus 로고    scopus 로고
    • Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy
    • Jeffrey M McGovern G Goodsir CM Brown KL Bruce ME 2000 Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy J Pathol 191 323 332
    • (2000) J Pathol , vol.191 , pp. 323-332
    • Jeffrey, M.1    McGovern, G.2    Goodsir, C.M.3    Brown, K.L.4    Bruce, M.E.5
  • 33
    • 0037465821 scopus 로고    scopus 로고
    • Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization
    • Kazlauskaite J Sanghera N Sylvester I Venien-Bryan C Pinheiro TJ 2003 Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization Biochemistry 42 3295 3304
    • (2003) Biochemistry , vol.42 , pp. 3295-3304
    • Kazlauskaite, J.1    Sanghera, N.2    Sylvester, I.3    Venien-Bryan, C.4    Pinheiro, T.J.5
  • 34
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera N Pinheiro TJ 2002 Binding of prion protein to lipid membranes and implications for prion conversion J Mol Biol 315 1241 1256
    • (2002) J Mol Biol , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 35
    • 4344632252 scopus 로고    scopus 로고
    • PrPC association with lipid rafts in the early secretory pathway stabilizes its cellular conformation
    • Sarnataro D Campana V Paladino S Stornaiuolo M Nitsch L Zurzolo C 2004 PrPC association with lipid rafts in the early secretory pathway stabilizes its cellular conformation Mol Biol Cell 15 4031 4042
    • (2004) Mol Biol Cell , vol.15 , pp. 4031-4042
    • Sarnataro, D.1    Campana, V.2    Paladino, S.3    Stornaiuolo, M.4    Nitsch, L.5    Zurzolo, C.6
  • 36
    • 2942595817 scopus 로고    scopus 로고
    • Characterization of recombinant, membrane-attached full-length prion protein
    • Eberl H Tittmann P Glockshuber R 2004 Characterization of recombinant, membrane-attached full-length prion protein J Biol Chem 279 25058 25065
    • (2004) J Biol Chem , vol.279 , pp. 25058-25065
    • Eberl, H.1    Tittmann, P.2    Glockshuber, R.3
  • 37
    • 0026780714 scopus 로고
    • Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid
    • Stahl N Baldwin MA Hecker R Pan KM Burlingame AL Prusiner SB 1992 Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid Biochemistry 31 5043 5053
    • (1992) Biochemistry , vol.31 , pp. 5043-5053
    • Stahl, N.1    Baldwin, M.A.2    Hecker, R.3    Pan, K.M.4    Burlingame, A.L.5    Prusiner, S.B.6
  • 39
    • 0242317908 scopus 로고    scopus 로고
    • Anchoring of glycosylphosphatidylinositol-proteins to liposomes
    • Nosjean O Roux B 2003 Anchoring of glycosylphosphatidylinositol-proteins to liposomes Methods Enzymol 372 216 232
    • (2003) Methods Enzymol , vol.372 , pp. 216-232
    • Nosjean, O.1    Roux, B.2
  • 40
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon AM Curnow P Booth PJ 2004 Membrane proteins, lipids and detergents: not just a soap opera Biochim Biophys Acta 1666 105 117
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 42
    • 4644372554 scopus 로고    scopus 로고
    • Raman optical activity demonstrates poly(1-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction
    • Blanch EW Gill AC Rhie AG Hope J Hecht L Nielsen K Barron LD 2004 Raman optical activity demonstrates poly(1-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction J Mol Biol 343 467 476
    • (2004) J Mol Biol , vol.343 , pp. 467-476
    • Blanch, E.W.1    Gill, A.C.2    Rhie, A.G.3    Hope, J.4    Hecht, L.5    Nielsen, K.6    Barron, L.D.7
  • 44
    • 0242662244 scopus 로고    scopus 로고
    • The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site
    • Zahn R 2003 The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site J Mol Biol 334 477 488
    • (2003) J Mol Biol , vol.334 , pp. 477-488
    • Zahn, R.1
  • 45
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231)
    • Riek R Hornemann S Wider G Glockshuber R Wuthrich K 1997 NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231) FEBS Lett 413 282 288
    • (1997) FEBS Lett , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 48
    • 0025976060 scopus 로고
    • Differences in the membrane interaction of scrapie amyloid precursor proteins in normal and scrapie- or Creutzfeldt-Jakob disease-infected brains
    • Safar J Ceroni M Gajdusek DC Gibbs CJ Jr. 1991 Differences in the membrane interaction of scrapie amyloid precursor proteins in normal and scrapie- or Creutzfeldt-Jakob disease-infected brains J Infect Dis 163 488 494
    • (1991) J Infect Dis , vol.163 , pp. 488-494
    • Safar, J.1    Ceroni, M.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 49
    • 0025339439 scopus 로고
    • Differential release of cellular and scrapie prion proteins from cellular membranes by phosphatidylinositol-specific phospholipase C
    • Stahl N Borchelt DR Prusiner SB 1990 Differential release of cellular and scrapie prion proteins from cellular membranes by phosphatidylinositol-specific phospholipase C Biochemistry 29 5405 5412
    • (1990) Biochemistry , vol.29 , pp. 5405-5412
    • Stahl, N.1    Borchelt, D.R.2    Prusiner, S.B.3
  • 50
    • 15544379325 scopus 로고    scopus 로고
    • Aggregation and fibrillization of prions in lipid membranes
    • Kazlauskaite J Pinheiro TJ 2005 Aggregation and fibrillization of prions in lipid membranes Biochem Soc Symp 211 222
    • (2005) Biochem Soc Symp , pp. 211-222
    • Kazlauskaite, J.1    Pinheiro, T.J.2
  • 51
    • 15244355224 scopus 로고    scopus 로고
    • Activation triggered by cellular prion is dependent on its endocytosis
    • ) Combined pharmacological, mutational and cell biology approaches indicate that p53-dependent caspase 3
    • Sunyach C Checler F 2005 ) Combined pharmacological, mutational and cell biology approaches indicate that p53-dependent caspase 3 activation triggered by cellular prion is dependent on its endocytosis J Neurochem 92 1399 1407
    • (2005) J Neurochem , vol.92 , pp. 1399-1407
    • Sunyach, C.1    Checler, F.2
  • 52
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein TR Kirsch D Kaufmann R 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.R.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 53
    • 0037385673 scopus 로고    scopus 로고
    • In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion
    • Kirby L Birkett CR Rudyk H Gilbert IH Hope J 2003 In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion J Gen Virol 84 1013 1020
    • (2003) J Gen Virol , vol.84 , pp. 1013-1020
    • Kirby, L.1    Birkett, C.R.2    Rudyk, H.3    Gilbert, I.H.4    Hope, J.5
  • 55
    • 33947457564 scopus 로고
    • The action of mineral acid on diethyl bis(hydroxymethy) malonate
    • Ferris A 1955 The action of mineral acid on diethyl bis(hydroxymethy) malonate J Org Chem 20 780 787
    • (1955) J Org Chem , vol.20 , pp. 780-787
    • Ferris, A.1
  • 56
    • 0001529587 scopus 로고
    • 3-Bromo-2-bromomethylpropyl glycosides in the preparation of double-chain bis-sulfide neo-glycolipids
    • Ansari AA Frejd T Magnusson G 1987 3-Bromo-2-bromomethylpropyl glycosides in the preparation of double-chain bis-sulfide neo-glycolipids Carbohydr Res 161 225 233
    • (1987) Carbohydr Res , vol.161 , pp. 225-233
    • Ansari, A.A.1    Frejd, T.2    Magnusson, G.3
  • 57
    • 0028501163 scopus 로고
    • Synthesis of double-chain bis-sulfone neoglycolipids of the 2′′-deoxyglobotriose, 3′′-deoxyglobotriose, 4′′-deoxyglobotriose, and 6′′-deoxyglobotriose
    • Zhang ZY Magnusson G 1994 Synthesis of double-chain bis-sulfone neoglycolipids of the 2′′-deoxyglobotriose, 3′′- deoxyglobotriose, 4′′-deoxyglobotriose, and 6′′- deoxyglobotriose Carbohydr Res 262 79 101
    • (1994) Carbohydr Res , vol.262 , pp. 79-101
    • Zhang, Z.Y.1    Magnusson, G.2
  • 59
    • 33751500224 scopus 로고
    • The synthesis of heterobifunctional linkers for the conjugation of ligands to molecular probes
    • Bertozzi CR Bednarski MD 1991 The synthesis of heterobifunctional linkers for the conjugation of ligands to molecular probes J Org Chem 56 4326 4329
    • (1991) J Org Chem , vol.56 , pp. 4326-4329
    • Bertozzi, C.R.1    Bednarski, M.D.2
  • 60
    • 33845550636 scopus 로고
    • Resolution of chiral alcohols with mandelic-acid
    • Whitesell JK Reynolds D 1983 Resolution of chiral alcohols with mandelic-acid J Org Chem 48 3548 3551
    • (1983) J Org Chem , vol.48 , pp. 3548-3551
    • Whitesell, J.K.1    Reynolds, D.2
  • 61
    • 0029022535 scopus 로고
    • Efficient synthesis of carbapenems via the oxalimide cyclization - Manipulation of protecting groups at the oxalimide stage
    • King SA Pipik B Thompson AS Decamp A Verhoeven TR 1995 Efficient synthesis of carbapenems via the oxalimide cyclization - manipulation of protecting groups at the oxalimide stage Tetrahedron Lett 36 4563 4566
    • (1995) Tetrahedron Lett , vol.36 , pp. 4563-4566
    • King, S.A.1    Pipik, B.2    Thompson, A.S.3    Decamp, A.4    Verhoeven, T.R.5
  • 62
    • 33748591880 scopus 로고    scopus 로고
    • Asymmetric syntheses of panclicins A-E via [2+2] cycloaddition of alkyl (trimethylsilyl) ketenes to a beta-silyloxyaldehyde
    • Kocienski PJ Pelotier B Pons JM Prideaux H 1998 Asymmetric syntheses of panclicins A-E via [2+2] cycloaddition of alkyl (trimethylsilyl) ketenes to a beta-silyloxyaldehyde J Chem Soc Perkin Trans 1 1373 1382
    • (1998) J Chem Soc Perkin Trans , vol.1 , pp. 1373-1382
    • Kocienski, P.J.1    Pelotier, B.2    Pons, J.M.3    Prideaux, H.4
  • 63
    • 0009520294 scopus 로고
    • Diethyl 3-iodopropynephosphonate - An alkylative beta-keto phosphonate equivalent
    • Poss AJ Belter RK 1987 Diethyl 3-iodopropynephosphonate - an alkylative beta-keto phosphonate equivalent J Org Chem 52 4810 4812
    • (1987) J Org Chem , vol.52 , pp. 4810-4812
    • Poss, A.J.1    Belter, R.K.2
  • 64
    • 0242380856 scopus 로고    scopus 로고
    • Extrusion technique to generate liposomes of defined size
    • Mui B Chow L Hope MJ 2003 Extrusion technique to generate liposomes of defined size Methods Enzymol 367 3 14
    • (2003) Methods Enzymol , vol.367 , pp. 3-14
    • Mui, B.1    Chow, L.2    Hope, M.J.3
  • 65
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler DM Susi H 1986 Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 469 487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.