메뉴 건너뛰기




Volumn 21, Issue 12, 2007, Pages 3279-3287

Ser170 controls the conformational multiplicity of the loop 166-175 in prion proteins: Implication for conversion and species barrier

Author keywords

Allosteric control; Elk; Flexibility; Molecular dynamics; Mouse

Indexed keywords

ASPARTIC ACID; HYBRID PROTEIN; PRION PROTEIN; SERINE; TRANSCRIPTION FACTOR ELK 1; SOLVENT;

EID: 35248848952     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-8292com     Document Type: Article
Times cited : (35)

References (51)
  • 4
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith, J. S. (1967) Self-replication and scrapie. Nature 215, 1043-1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 5
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper, T., Cramp, W. A., Haig, D. A., and Clarke, M. C. (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214, 764-766
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 6
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C., McKinley, M. P., and Prusiner, S. B. (1982) Identification of a protein that purifies with the scrapie prion. Science 218, 1309-1311
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 7
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed beta-helices into trimers
    • Govaerts, C., Wille, H., Prusiner, S. B., and Cohen, F. E. (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
  • 8
    • 4143067019 scopus 로고    scopus 로고
    • Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease
    • Armen, R. S., DeMarco, M. L., Alonso, D. O., and Daggett, V. (2004) Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proc. Natl. Acad. Sci. USA 101, 11622-11627
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11622-11627
    • Armen, R.S.1    DeMarco, M.L.2    Alonso, D.O.3    Daggett, V.4
  • 10
    • 0345598918 scopus 로고    scopus 로고
    • NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126
    • Kuwata, K., Matumoto, T., Cheng, H., Nagayama, K., James, T. L., and Roder, H. (2003) NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc. Natl. Acad. Sci. USA 100, 14790-14795
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14790-14795
    • Kuwata, K.1    Matumoto, T.2    Cheng, H.3    Nagayama, K.4    James, T.L.5    Roder, H.6
  • 11
    • 0032485810 scopus 로고    scopus 로고
    • Bistability and the species barrier in prion diseases: Stepping across the threshold or not
    • Laurent, M. (1998) Bistability and the species barrier in prion diseases: stepping across the threshold or not. Biophys. Chem. 72, 211-222
    • (1998) Biophys. Chem , vol.72 , pp. 211-222
    • Laurent, M.1
  • 14
    • 17444393595 scopus 로고    scopus 로고
    • Transmission barriers for bovine, ovine, and human prions in transgenic mice
    • Scott, M. R., Peretz, D., Nguyen, H. O., Dearmond, S. J., and Prusiner, S. B. (2005) Transmission barriers for bovine, ovine, and human prions in transgenic mice. J. Virol. 79, 5259-5271
    • (2005) J. Virol , vol.79 , pp. 5259-5271
    • Scott, M.R.1    Peretz, D.2    Nguyen, H.O.3    Dearmond, S.J.4    Prusiner, S.B.5
  • 15
    • 0028782015 scopus 로고
    • Transmission of bovine spongiform encephalopathy and scrapie to mice: Strain variation and the species barrier
    • Bruce, M., Chree, A., McConnell, I., Foster, J., Pearson, G., and Fraser, H. (1994) Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philosoph. Trans.R. Soc. London 343, 405-411
    • (1994) Philosoph. Trans.R. Soc. London , vol.343 , pp. 405-411
    • Bruce, M.1    Chree, A.2    McConnell, I.3    Foster, J.4    Pearson, G.5    Fraser, H.6
  • 26
    • 0038377438 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies in non-domestic animals: Origin, transmission and risk factors
    • Williams, E. S., and Miller, M. W. (2003) Transmissible spongiform encephalopathies in non-domestic animals: origin, transmission and risk factors. Revue. Scientifique Technique (International Office of Epizootics) 22, 145-156
    • (2003) Revue. Scientifique Technique (International Office of Epizootics) , vol.22 , pp. 145-156
    • Williams, E.S.1    Miller, M.W.2
  • 29
    • 0036140263 scopus 로고    scopus 로고
    • Calculation of protein ionization equilibria with conformational sampling: PK(a) of a model leucine zipper, GCN4 and barnase
    • Gorfe, A. A., Ferrara, P., Caflisch, A., Marti, D. N., Bosshard, H. R., and Jelesarov, I. (2002) Calculation of protein ionization equilibria with conformational sampling: pK(a) of a model leucine zipper, GCN4 and barnase. Proteins 46, 41-60
    • (2002) Proteins , vol.46 , pp. 41-60
    • Gorfe, A.A.1    Ferrara, P.2    Caflisch, A.3    Marti, D.N.4    Bosshard, H.R.5    Jelesarov, I.6
  • 33
    • 26444552906 scopus 로고    scopus 로고
    • Functional plasticity in the substrate binding site of beta-secretase
    • Gorfe, A. A., and Caflisch, A. (2005) Functional plasticity in the substrate binding site of beta-secretase. Structure 13, 1487-1498
    • (2005) Structure , vol.13 , pp. 1487-1498
    • Gorfe, A.A.1    Caflisch, A.2
  • 34
    • 2442494894 scopus 로고    scopus 로고
    • Helix H1 of the prion protein is rather stable against environmental purturbations: Molcular dynamics of mutation and deletion variants of PrP
    • Santini, S., and Derreumaux, P. (2004) Helix H1 of the prion protein is rather stable against environmental purturbations: molcular dynamics of mutation and deletion variants of PrP(90-231) CMLS. Cell Mol. Life Sci. 61, 951-960
    • (2004) CMLS. Cell Mol. Life Sci , vol.61 , pp. 951-960
    • Santini, S.1    Derreumaux, P.2
  • 35
    • 0035199471 scopus 로고    scopus 로고
    • Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations
    • Gsponer, J., Ferrara, P., and Caflisch, A. (2001) Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations. J. Mol. Graphics Model. 20, 169-182
    • (2001) J. Mol. Graphics Model , vol.20 , pp. 169-182
    • Gsponer, J.1    Ferrara, P.2    Caflisch, A.3
  • 36
    • 0036708438 scopus 로고    scopus 로고
    • Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments
    • Dima, R. I., and Thirumalai, D. (2002) Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments. Biophys. J. 83, 1268-1280
    • (2002) Biophys. J , vol.83 , pp. 1268-1280
    • Dima, R.I.1    Thirumalai, D.2
  • 37
    • 0032546782 scopus 로고    scopus 로고
    • pi-Stacking interactions. Alive and well in proteins
    • McGaughey, G. B., Gagne, M., and Rappe, A. K. (1998) pi-Stacking interactions. Alive and well in proteins. J. Biol. Chem. 273, 15458-15463
    • (1998) J. Biol. Chem , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 39
    • 0032110683 scopus 로고    scopus 로고
    • Epidemiology of chronic wasting disease in captive Rocky Mountain elk
    • Miller, M. W., Wild, M. A., and Williams, E. S. (1998) Epidemiology of chronic wasting disease in captive Rocky Mountain elk. J. Wildlife Dis. 34, 532-538
    • (1998) J. Wildlife Dis , vol.34 , pp. 532-538
    • Miller, M.W.1    Wild, M.A.2    Williams, E.S.3
  • 42
    • 0037121267 scopus 로고    scopus 로고
    • Detection of PrP(CWD) in mule deer by immunohistochemistry of lymphoid tissues
    • Miller, M. W., and Williams, E. S. (2002) Detection of PrP(CWD) in mule deer by immunohistochemistry of lymphoid tissues. Vet. Rec. 151, 610-612
    • (2002) Vet. Rec , vol.151 , pp. 610-612
    • Miller, M.W.1    Williams, E.S.2
  • 43
    • 33750237759 scopus 로고    scopus 로고
    • Patterns of PrPCWD accumulation during the course of chronic wasting disease infection in orally inoculated mule deer (Odocoileus hemionus)
    • Fox, K. A., Jewell, J. E., Williams, E. S., and Miller, M. W. (2006) Patterns of PrPCWD accumulation during the course of chronic wasting disease infection in orally inoculated mule deer (Odocoileus hemionus). J. Gen. Virol. 87, 3451-3461
    • (2006) J. Gen. Virol , vol.87 , pp. 3451-3461
    • Fox, K.A.1    Jewell, J.E.2    Williams, E.S.3    Miller, M.W.4
  • 44
  • 47
    • 33751412846 scopus 로고    scopus 로고
    • Ovine prion protein variant A136R154L168Q171 increases resistance to experimental challenge with bovine spongiform encephalopathy agent
    • Goldmann, W., Houston, F., Stewart, P., Perucchini, M., Foster, J., and Hunter, N. (2006) Ovine prion protein variant A136R154L168Q171 increases resistance to experimental challenge with bovine spongiform encephalopathy agent. J. Gen. Virol. 87, 3741-3745
    • (2006) J. Gen. Virol , vol.87 , pp. 3741-3745
    • Goldmann, W.1    Houston, F.2    Stewart, P.3    Perucchini, M.4    Foster, J.5    Hunter, N.6
  • 48
    • 3142683624 scopus 로고    scopus 로고
    • Insight into the PrP->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants
    • Eghiaian, F., Grosclaude, J., Lesceu, S., Debey, P., Doublet, B., Treguer, E., Rezaei, H., and Knossow, M. (2004) Insight into the PrP->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants. Proc. Natl. Acad. Sci. USA 101, 10254-10259
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10254-10259
    • Eghiaian, F.1    Grosclaude, J.2    Lesceu, S.3    Debey, P.4    Doublet, B.5    Treguer, E.6    Rezaei, H.7    Knossow, M.8
  • 49
    • 0035805643 scopus 로고    scopus 로고
    • Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain
    • Horiuchi, M., Baron, G. S., Xiong, L. W., and Caughey, B. (2001) Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain. J. Biol. Chem. 276, 15489-15497
    • (2001) J. Biol. Chem , vol.276 , pp. 15489-15497
    • Horiuchi, M.1    Baron, G.S.2    Xiong, L.W.3    Caughey, B.4
  • 50
    • 0035853093 scopus 로고    scopus 로고
    • Mapping the early steps in the pH-induced conformational conversion of the prion protein
    • Alonso, D. O., DeArmond, S. J., Cohen, F. E., and Daggett, V. (2001) Mapping the early steps in the pH-induced conformational conversion of the prion protein. Proc. Natl. Acad. Sci.USA 98, 2985-2989
    • (2001) Proc. Natl. Acad. Sci.USA , vol.98 , pp. 2985-2989
    • Alonso, D.O.1    DeArmond, S.J.2    Cohen, F.E.3    Daggett, V.4
  • 51
    • 0034023961 scopus 로고    scopus 로고
    • New variant' Creutzfeldt-Jakob disease and bovine spongiform encephalopathy
    • Bruce, M. E. (2000) 'New variant' Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Nat. Med. 6, 258-259
    • (2000) Nat. Med , vol.6 , pp. 258-259
    • Bruce, M.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.