메뉴 건너뛰기




Volumn 351, Issue 4, 2005, Pages 910-922

Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates

Author keywords

Aggregation intermediates; Disease; Misfolding; Oligomerisation; On pathway

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; CONGO RED; THIOFLAVINE;

EID: 23444447864     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.06.043     Document Type: Article
Times cited : (122)

References (53)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81 2003 678 699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 3
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • V.N. Uversky, and A.L. Fink Conformational constraints for amyloid fibrillation: the importance of being unfolded Bioch. Biophys. Acta 1698 2004 131 153
    • (2004) Bioch. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 4
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini, E. Giannoni, F. Chiti, F. Baroni, L. Formigli, and J. Zurdo Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 6
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • D.J. Selkoe Folding proteins in fatal ways Nature 426 2003 900 904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 7
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • J.D. Harper, S.S. Wong, C.M. Lieber, and P.T. Lansbury Observation of metastable Abeta amyloid protofibrils by atomic force microscopy Chem. Biol. 4 1997 119 125
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 8
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • J.D. Harper, C.M. Lieber, and P.T. Lansbury Jr Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein Chem. Biol. 4 1997 951 959
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 9
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • D.M. Walsh, A. Lomakin, G.B. Benedek, M.M. Condron, and D.B. Teplow Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate J. Biol. Chem. 272 1997 22364 22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 10
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • D.M. Walsh, D.M. Hartley, Y. Kusumoto, Y. Fezoui, M.M. Condron, and A. Lomakin Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates J. Biol. Chem. 274 1999 25945 25952
    • (1999) J. Biol. Chem. , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 12
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, J. Zurdo, E.J. Nettleton, C.M. Dobson, and C.V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein Sci. 9 2000 960 967
    • (2000) Protein Sci. , vol.9 , pp. 960-967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 13
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • K.A. Conway, J.D. Harper, and P.T. Lansbury Jr Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid Biochemistry 39 2000 2552 2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 14
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • T.R. Serio, A.G. Cashikar, A.S. Kowal, G.J. Sawicki, J.J. Moslehi, and L. Serpell Nucleated conformational conversion and the replication of conformational information by a prion determinant Science 289 2000 1317 1321
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 15
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • A. Quintas, D.C. Vaz, I. Cardoso, M.J.M. Saraiva, and R.M.M. Brito Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants J. Biol. Chem. 276 2001 27207 27213
    • (2001) J. Biol. Chem. , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.M.4    Brito, R.M.M.5
  • 17
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrillization
    • M.A. Poirier, H. Li, J. Macosko, S. Cail, M. Amzel, and C.A. Ross Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrillization J. Biol. Chem. 277 2002 41032 41037
    • (2002) J. Biol. Chem. , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    MacOsko, J.3    Cail, S.4    Amzel, M.5    Ross, C.A.6
  • 18
    • 11144353842 scopus 로고    scopus 로고
    • Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils
    • A. Relini, S. Torrassa, R. Rolandi, A. Gliozzi, C. Rosano, and C. Canale Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils J. Mol. Biol. 338 2004 943 957
    • (2004) J. Mol. Biol. , vol.338 , pp. 943-957
    • Relini, A.1    Torrassa, S.2    Rolandi, R.3    Gliozzi, A.4    Rosano, C.5    Canale, C.6
  • 19
    • 3342906956 scopus 로고    scopus 로고
    • Fibrillation of carrier protein albebetin and its biologically active constructs multiple oligomeric intermediates and pathways
    • L.A. Morozova-Roche, V. Zamotin, M. Malisauskas, A. Ohman, R. Chertkova, and M.A. Lavrikova Fibrillation of carrier protein albebetin and its biologically active constructs multiple oligomeric intermediates and pathways Biochemistry 43 2004 9610 9619
    • (2004) Biochemistry , vol.43 , pp. 9610-9619
    • Morozova-Roche, L.A.1    Zamotin, V.2    Malisauskas, M.3    Ohman, A.4    Chertkova, R.5    Lavrikova, M.A.6
  • 20
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • D.M. Hartley, D.M. Walsh, C.P. Ye, T. Diehl, S. Vasquez, and P.M. Vassilev Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons J. Neurosci. 19 1999 8876 8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6
  • 21
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • D.M. Walsh, and D.J. Selkoe Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration Protein Pept. Letters 11 2004 213 228
    • (2004) Protein Pept. Letters , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 22
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • M.D. Kirkitadze, G. Bitan, and D.B. Teplow Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies J. Neurosci. Res. 69 2002 567 577
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 23
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • G. Bitan, A. Lomakin, and D.B. Teplow Amyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins J. Biol. Chem. 276 2001 35176 35184
    • (2001) J. Biol. Chem. , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 25
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • A.E. Roher, M.O. Chaney, Y.M. Kuo, S.D. Webster, W.B. Stine, and L.J. Haverkamp Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease J. Biol. Chem. 271 1996 20631 20635
    • (1996) J. Biol. Chem. , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Kuo, Y.M.3    Webster, S.D.4    Stine, W.B.5    Haverkamp, L.J.6
  • 27
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • D.M. Walsh, B.P. Tseng, R.E. Rydel, M.B. Podlisny, and D.J. Selkoe The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain Biochemistry 39 2000 10831 10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 28
    • 1842790837 scopus 로고    scopus 로고
    • Aggregation of the acylphosphatase from Sulfolobus solfataricus: The folded and partially unfolded states can both be precursors for amyloid formation
    • G. Plakoutsi, N. Taddei, M. Stefani, and F. Chiti Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation J. Biol. Chem. 279 2004 14111 14119
    • (2004) J. Biol. Chem. , vol.279 , pp. 14111-14119
    • Plakoutsi, G.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 29
    • 0024351039 scopus 로고
    • Phenotypic characterization of the archaeal genus Sulfolobus: Comparison of five wild-type strains
    • D.W. Grogan Phenotypic characterization of the archaeal genus Sulfolobus: comparison of five wild-type strains J. Bacteriol. 171 1989 6710 6719
    • (1989) J. Bacteriol. , vol.171 , pp. 6710-6719
    • Grogan, D.W.1
  • 31
    • 0038043276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation
    • S. Srisailam, T.K. Kumar, D. Rajalingam, K.M. Kathir, H.S. Sheu, and F.J. Jan Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation J. Biol. Chem. 278 2003 17701 17709
    • (2003) J. Biol. Chem. , vol.278 , pp. 17701-17709
    • Srisailam, S.1    Kumar, T.K.2    Rajalingam, D.3    Kathir, K.M.4    Sheu, H.S.5    Jan, F.J.6
  • 32
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • C.J. Barrow, and M.G. Zagorski Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition Science 253 1991 179 182
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 33
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • F. Chiti, N. Taddei, M. Bucciantini, P. White, G. Ramponi, and C.M. Dobson Mutational analysis of the propensity for amyloid formation by a globular protein EMBO J. 19 2000 1441 1449
    • (2000) EMBO J. , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 34
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid beta-protein fibril assembly. Differential effects of alpha-helix stabilization
    • Y. Fezoui, and D.B. Teplow Kinetic studies of amyloid beta-protein fibril assembly. Differential effects of alpha-helix stabilization J. Biol. Chem. 277 2002 36948 36954
    • (2002) J. Biol. Chem. , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 35
    • 0042467550 scopus 로고    scopus 로고
    • Rationalisation of the effects of mutations on peptide and protein aggregation rates
    • F. Chiti, M. Stefani, N. Taddei, G. Ramponi, and C.M. Dobson Rationalisation of the effects of mutations on peptide and protein aggregation rates Nature 424 2003 805 808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 36
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes
    • L.A. Munishkina, C. Phelan, V.N. Uversky, and A.L. Fink Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes Biochemistry 42 2003 2720 2730
    • (2003) Biochemistry , vol.42 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 37
    • 33644562293 scopus 로고    scopus 로고
    • Structure, conformational stability and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
    • A. Corazza, C. Rosano, K. Pagano, V. Alverdi, G. Esposito, and C. Capanni Structure, conformational stability and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus Proteins: Struct. Funct. Genet 2005 In the press
    • (2005) Proteins: Struct. Funct. Genet
    • Corazza, A.1    Rosano, C.2    Pagano, K.3    Alverdi, V.4    Esposito, G.5    Capanni, C.6
  • 38
    • 0032830123 scopus 로고    scopus 로고
    • Monitoring protein assembly using quasielastic light scattering spectroscopy
    • A. Lomakin, G.B. Benedek, and D.B. Teplow Monitoring protein assembly using quasielastic light scattering spectroscopy Methods Enzymol. 309 1999 429 459
    • (1999) Methods Enzymol. , vol.309 , pp. 429-459
    • Lomakin, A.1    Benedek, G.B.2    Teplow, D.B.3
  • 39
    • 0142040121 scopus 로고    scopus 로고
    • Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein
    • F. Sokolowski, A.J. Modler, R. Masuch, D. Zirwer, M. Baier, and G. Lutsch Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein J. Biol. Chem. 278 2003 40481 40492
    • (2003) J. Biol. Chem. , vol.278 , pp. 40481-40492
    • Sokolowski, F.1    Modler, A.J.2    Masuch, R.3    Zirwer, D.4    Baier, M.5    Lutsch, G.6
  • 40
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • W.C. Johnson Jr Protein secondary structure and circular dichroism: a practical guide Proteins: Struct. Funct. Genet. 7 1990 205 214
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 205-214
    • Johnson, W.C.1    Jr2
  • 41
    • 0028063528 scopus 로고
    • Determination of protein tertiary structure class from circular dichroism spectra
    • S.Yu. Venyaminov, and K.S. Vassilenko Determination of protein tertiary structure class from circular dichroism spectra Anal. Biochem. 222 1994 176 184
    • (1994) Anal. Biochem. , vol.222 , pp. 176-184
    • Venyaminov, S.Yu.1    Vassilenko, K.S.2
  • 42
    • 3142745308 scopus 로고    scopus 로고
    • Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. a comparative analysis with other proteins from the same superfamily
    • F. Bemporad, C. Capanni, M. Calamai, M.L. Tutino, M. Stefani, and F. Chiti Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily Biochemistry 43 2004 9116 9126
    • (2004) Biochemistry , vol.43 , pp. 9116-9126
    • Bemporad, F.1    Capanni, C.2    Calamai, M.3    Tutino, M.L.4    Stefani, M.5    Chiti, F.6
  • 43
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • M.J. Volles, S.J. Lee, J.C. Rochet, M.D. Shtilerman, T.T. Ding, J.C. Kessler, and P.T. Lansbury Jr Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease Biochemistry 40 2001 7812 7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury Jr., P.T.7
  • 44
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • W.E. Klunk, J.W. Pettegrew, and D.J. Abraham Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation J. Histochem. Cytochem. 37 1989 1273 1281
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 45
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • H. LeVine III Quantification of beta-sheet amyloid fibril structures with thioflavin T Methods Enzymol. 309 1999 274 284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 46
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • J.J. Kremer, M.M. Pallitto, D.J. Sklansky, and R.M. Murphy Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes Biochemistry 39 2000 10309 10318
    • (2000) Biochemistry , vol.39 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 47
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN
    • P.O. Souillac, V.N. Uversky, and A.L. Fink Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN Biochemistry 42 2003 8094 8104
    • (2003) Biochemistry , vol.42 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3
  • 48
    • 3342902033 scopus 로고    scopus 로고
    • Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
    • J.S. Pedersen, G. Christensen, and D.E. Otzen Modulation of S6 fibrillation by unfolding rates and gatekeeper residues J. Mol. Biol. 341 2004 575 588
    • (2004) J. Mol. Biol. , vol.341 , pp. 575-588
    • Pedersen, J.S.1    Christensen, G.2    Otzen, D.E.3
  • 49
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
    • L. Bousset, N.H. Thomson, S.E. Radford, and R. Melki The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro EMBO J. 17 2002 2903 2911
    • (2002) EMBO J. , vol.17 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 50
    • 9144228981 scopus 로고    scopus 로고
    • Lithostathine quadruple helical filaments form proteinase-K resistant deposits in Creutzfeldt-Jakob disease
    • E. Laurine, C. Gregoire, M. Fandrich, S. Engemann, S. Marchal, and L. Thion Lithostathine quadruple helical filaments form proteinase-K resistant deposits in Creutzfeldt-Jakob disease J. Biol. Chem. 278 2003 51770 51778
    • (2003) J. Biol. Chem. , vol.278 , pp. 51770-51778
    • Laurine, E.1    Gregoire, C.2    Fandrich, M.3    Engemann, S.4    Marchal, S.5    Thion, L.6
  • 51
    • 0037291995 scopus 로고    scopus 로고
    • The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils
    • L. Bousset, F. Briki, J. Doucet, and R. Melki The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils J. Struct. Biol. 141 2003 132 142
    • (2003) J. Struct. Biol. , vol.141 , pp. 132-142
    • Bousset, L.1    Briki, F.2    Doucet, J.3    Melki, R.4
  • 52
    • 0017123760 scopus 로고
    • A new synthesis of benzoyl phosphate: A substrate for acyl phosphatase assay
    • G. Camici, G. Manao, G. Cappugi, and G. Ramponi A new synthesis of benzoyl phosphate: a substrate for acyl phosphatase assay Experientia 32 1976 535 536
    • (1976) Experientia , vol.32 , pp. 535-536
    • Camici, G.1    Manao, G.2    Cappugi, G.3    Ramponi, G.4
  • 53
    • 0029953734 scopus 로고    scopus 로고
    • Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: Role of Asn41, Thr42 and Thr46
    • N. Taddei, M. Stefani, F. Magherini, F. Chiti, A. Modesti, G. Raugei, and G. Ramponi Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42 and Thr46 Biochemistry 35 1996 7077 7083
    • (1996) Biochemistry , vol.35 , pp. 7077-7083
    • Taddei, N.1    Stefani, M.2    Magherini, F.3    Chiti, F.4    Modesti, A.5    Raugei, G.6    Ramponi, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.