메뉴 건너뛰기




Volumn 1820, Issue 2, 2012, Pages 124-132

Inhibiting effect of α s1 -casein on Aβ 1-40 fibrillogenesis

Author keywords

Amyloid fibril; Beta peptide; Casein; Chaperone activity; Colloidal inhibition; Unstructured protein

Indexed keywords

ALPHA CASEIN; ALPHA S1 CASEIN; AMYLOID BETA PROTEIN[1-40]; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 84055185283     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.11.010     Document Type: Article
Times cited : (50)

References (59)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative diseases
    • C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative diseases Nat. Med. 10 2004 S10 S17
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 2
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • DOI 10.1016/j.bbapap.2003.12.008, PII S1570963904000020
    • V.N. Uversky, and A.L. Fink Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochim. Biophys. Acta 1698 2004 131 153 (Pubitemid 38591469)
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1698 , Issue.2 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 3
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • DOI 10.1016/j.bbadis.2004.08.004, PII S092544390400136X, The Biology and Pathobiology of Tau
    • M. Stefani Protien misfolding and aggregation: new examples in medicine and biology of the darkside of protein world Biochim. Biophys. Acta 1739 2004 5 25 (Pubitemid 39647706)
    • (2004) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1739 , Issue.1 , pp. 5-25
    • Stefani, M.1
  • 5
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • J.W. Kelly Mechanisms of amyloidogenesis Nat. Struct. Biol. 7 2000 824 826
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 6
    • 77955930429 scopus 로고    scopus 로고
    • Protein-protein interactions lading to aggregation: Perspectives on mechanism, significance and control
    • A.E. Habibi, D. Morshedi, N. Rezai-Ghaleh, M. Sabbaghian, and M. Nemat-Gorgani Protein-protein interactions lading to aggregation: perspectives on mechanism, significance and control J. Iran. Chem. Soc. 7 2010 521 544
    • (2010) J. Iran. Chem. Soc. , vol.7 , pp. 521-544
    • Habibi, A.E.1    Morshedi, D.2    Rezai-Ghaleh, N.3    Sabbaghian, M.4    Nemat-Gorgani, M.5
  • 7
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 8
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Aβ oligomers
    • M. Sakono, and T. Zako Amyloid oligomers: formation and toxicity of Aβ oligomers FEBS J. 277 2010 1348 1358
    • (2010) FEBS J. , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 9
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • V.N. Uversky Mysterious oligomerization of the amyloidogenic proteins FEBS J. 277 2010 2940 2953
    • (2010) FEBS J. , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 11
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • C.G. Glabe, Structural classification of toxic amyloid oligomers, J. Biol. Chem. 283 (200) 29639-29643.
    • J. Biol. Chem. , vol.283 , Issue.200 , pp. 29639-29643
    • Glabe, C.G.1
  • 13
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • J.D. Harper, S.S. Wong, C.M. Lieber, and P.T. Lansbury Jr. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy Chem. Biol. 4 1997 119 125 (Pubitemid 27161750)
    • (1997) Chemistry and Biology , vol.4 , Issue.2 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 14
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • DOI 10.1074/jbc.272.35.22364
    • D.M. Walsh, A. Lomakin, G.B. Benedeck, M.M. Comdrom, and D.B. Teplow Amyloid β-protein fibrillogenesis: detection of a protofibrillar intermediate J. Biol. Chem. 272 1997 22364 22372 (Pubitemid 27382873)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 15
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
    • DOI 10.1038/nsmb1345, PII NSMB1345
    • S. Chimon, M.A. Shaibat, C.R. Jones, D.C. Calero, B. Aizezi, and Y. Ishii Evidence of fibril-like b-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's b-amyloid Nat. Struct. Mol. Biol. 14 2007 1157 1164 (Pubitemid 350223342)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 17
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • M. Necula, L. Breydo, R. Kayed, S. Milton, and C.G. Glabe Small Molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways independent and distinct J. Biol. Chem. 282 2007 10311 10324 (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 19
    • 53049095484 scopus 로고    scopus 로고
    • In vitro perturbation of aggregation processes in β-amyloid peptides: A spectroscopy study
    • A. Sgarbossa, D. Buselli, and F. Lenci In vitro perturbation of aggregation processes in β-amyloid peptides: a spectroscopy study FEBS Lett. 582 2008 3288 3292
    • (2008) FEBS Lett. , vol.582 , pp. 3288-3292
    • Sgarbossa, A.1    Buselli, D.2    Lenci, F.3
  • 20
    • 0037860938 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions with small organic molecules
    • DOI 10.1002/anie.200200558
    • T. Berg Modulation of protein-protein interactions with small organic molecules Angew. Chem. Int. Ed. 42 2003 2462 2481 (Pubitemid 36753413)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.22 , pp. 2462-2481
    • Berg, T.1
  • 21
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
    • DOI 10.1523/JNEUROSCI.4391-04.2005
    • D.M. Walsh, M. Townsend, M.B. Podlisny, G.M. Shankar, J.V. Fadeeva, O. El Agnaf, D.M. Hartley, and D.J. Selkoe Certain inhibitors of synthetic amyloid b-peptide (Aβ) fibrillogenesis block oligomerization of natural A b and thereby rescue long-term potentiation J. Neurosci. 25 2005 2455 2462 (Pubitemid 40365155)
    • (2005) Journal of Neuroscience , vol.25 , Issue.10 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    El Agnaf, O.6    Hartley, D.M.7    Selkoe, D.J.8
  • 23
    • 79959977900 scopus 로고    scopus 로고
    • Rottlerin dissolves pre-formed protein amyloid: A study on hen egg white lysozyme
    • N. Sarkar, M. Kumar, and V.K. Dubey Rottlerin dissolves pre-formed protein amyloid: a study on hen egg white lysozyme Biochim. Biophys. Acta, General Subjects 1810 2011 809 814
    • (2011) Biochim. Biophys. Acta, General Subjects , vol.1810 , pp. 809-814
    • Sarkar, N.1    Kumar, M.2    Dubey, V.K.3
  • 24
    • 28244458451 scopus 로고    scopus 로고
    • Mechanisms of amyloid fibril self-assembly and inhibition: Model short peptides as a key research tool
    • DOI 10.1111/j.1742-4658.2005.05022.x
    • E. Gazit Mechanism of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool FEBS J. 272 2005 5971 5978 (Pubitemid 41713689)
    • (2005) FEBS Journal , vol.272 , Issue.23 , pp. 5971-5978
    • Gazit, E.1
  • 25
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • DOI 10.1111/j.1747-0285.2005.00318.x
    • Y. Porat, A. Abramowitz, and E. Gazit Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism Chem. Biol. Drug Des. 67 2006 27 37 (Pubitemid 43881385)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 26
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • DOI 10.1021/jm010533y
    • S.L. McGovern, E. Caselli, N. Grigorieff, and B.K. Shoichet A common mechanism underlying promiscuous inhibitors from virtual and high throughput screening J. Med. Chem. 45 2002 1712 1722 (Pubitemid 34293537)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.8 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 27
    • 33846054061 scopus 로고    scopus 로고
    • Disrupting β-amyloid aggregation for Alzheimer disease treatment
    • DOI 10.2174/156802607779318262
    • L.D. Estrada, and C. Soto Disrupting β-amyloid aggregation for Alzheimer disease treatment Curr. Top. Med. Chem. 7 2007 115 126 (Pubitemid 46062400)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.1 , pp. 115-126
    • Estrada, L.D.1    Soto, C.2
  • 29
    • 7444221875 scopus 로고    scopus 로고
    • Harnessing chaperons to generate small-molecule inhibitors of amyloid β aggregation
    • DOI 10.1126/science.1101262
    • J.E. Gestwicki, G. Crabtree, and I.A. Graef Harnessing chaperones to generate small-molecule inhibitors of amyloid β aggregation Science 306 2004 865 869 (Pubitemid 39446994)
    • (2004) Science , vol.306 , Issue.5697 , pp. 865-869
    • Gestwicki, J.E.1    Crabtree, G.R.2    Graef, I.A.3
  • 30
    • 25144471718 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants
    • DOI 10.1016/j.bbadis.2005.05.004, PII S0925443905000943
    • S.S.-S. Wang, Y.-T. Chen, and S.-W. Chou Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants Biochim. Biophys. Acta 1741 2005 307 313 (Pubitemid 41338676)
    • (2005) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1741 , Issue.3 , pp. 307-313
    • Wang, S.S.-S.1    Chen, Y.-T.2    Chou, S.-W.3
  • 31
    • 59649108278 scopus 로고    scopus 로고
    • Unraveling the mysteries of protein folding and misfolding
    • H. Ecroyd, and J.A. Carver Unraveling the mysteries of protein folding and misfolding IUBMB Life 60 2008 769 774
    • (2008) IUBMB Life , vol.60 , pp. 769-774
    • Ecroyd, H.1    Carver, J.A.2
  • 32
    • 0035783169 scopus 로고    scopus 로고
    • Review: Mechanism of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • A.P. Ben-Zvi, and P. Goloubinoff Review: mechanism of disaggregation and refolding of stable protein aggregates by molecular chaperones J. Struct. Biol. 135 2001 84 93
    • (2001) J. Struct. Biol. , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 35
    • 73649130269 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: Emerging role of molecular chaperones
    • R. Bandopaddhyay, and J. de Belleroche Pathogenesis of Parkinson's disease: emerging role of molecular chaperones Trends Mol. Med. 16 2010 27 36
    • (2010) Trends Mol. Med. , vol.16 , pp. 27-36
    • Bandopaddhyay, R.1    De Belleroche, J.2
  • 36
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperones network
    • F. Naberhaus α-Crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperones network Microbiol. Mol. Biol. Rev. 66 2002 64 93
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Naberhaus, F.1
  • 37
    • 0028366080 scopus 로고
    • Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding
    • H. Taguchi, Y. Makino, and M. Yoshida Monomeric chaperonin-60 and its 50-kda fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote folding J. Biol. Chem. 269 1994 8529 8534 (Pubitemid 24200279)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.11 , pp. 8529-8534
    • Taguchi, H.1    Makino, Y.2    Yoshida, M.3
  • 38
    • 33750000616 scopus 로고    scopus 로고
    • Folding on the Chaperone: Yield Enhancement Through Loose Binding
    • DOI 10.1016/j.jmb.2006.08.040, PII S0022283606010680
    • A.I. Jewett, and J.E. Shea Folding on the chaperone: yield enhancement through loose binding J. Mol. Biol. 363 2006 945 957 (Pubitemid 44573225)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.5 , pp. 945-957
    • Jewett, A.I.1    Shea, J.-E.2
  • 39
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • DOI 10.1016/S0958-6946(98)00040-5, PII S0958694698000405
    • D.S. Horne Casein interactions: casting light on the black boxes, the structure in dairy products Int. Dairy J. 8 1998 171 177 (Pubitemid 28436832)
    • (1998) International Dairy Journal , vol.8 , Issue.3 , pp. 171-177
    • Horne, D.S.1
  • 40
    • 74849105568 scopus 로고    scopus 로고
    • Caseins: Utilizing molecular chaperones properties to control protein aggregation in foods
    • 865-693
    • Y.H. Yong, and E.A. Foegeding Caseins: utilizing molecular chaperones properties to control protein aggregation in foods J. Agric. Food Chem. 58 2010 865-693
    • (2010) J. Agric. Food Chem. , vol.58
    • Yong, Y.H.1    Foegeding, E.A.2
  • 42
  • 44
    • 0014109212 scopus 로고
    • Spectroscopic determination of Tryptophan and Tyrosine in proteins
    • H. Edelhoch Spectroscopic determination of Tryptophan and Tyrosine in proteins Biochemistry 6 1967 1948 1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 45
    • 1542680924 scopus 로고    scopus 로고
    • Heat induced aggregation and gelation of casein submicelles
    • DOI 10.1016/j.idairyj.2003.09.003, PII S0958694603002218
    • M. Panouille', T. Nicolai, and D. Durand Heat induced aggregation and gelation of casein submicelles Int. Dairy J. 14 2004 297 303 (Pubitemid 38345652)
    • (2004) International Dairy Journal , vol.14 , Issue.4 , pp. 297-303
    • Panouille, M.1    Nicolai, T.2    Durand, D.3
  • 46
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equation
    • S.W. Provencher A constrained regularization method for inverting data represented by linear algebraic or integral equation Comput. Phys. Commun. 27 1982 213 277
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-277
    • Provencher, S.W.1
  • 47
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid beta-protein fibril assembly - Differential effects on alpha helix stabilization
    • Y. Fezoui, and D.B. Teplow Kinetic studies of amyloid beta-protein fibril assembly - Differential effects on 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
  • 48
    • 33745675123 scopus 로고    scopus 로고
    • The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy
    • DOI 10.1093/jb/mvj083
    • Y.R. Chen, H.B. Huang, C.L. Chyan, M.S. Shiao, T.H. Lin, and Y.C. Chen The effect of A beta conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy J. Biochem. 139 2006 733 740 (Pubitemid 43973920)
    • (2006) Journal of Biochemistry , vol.139 , Issue.4 , pp. 733-740
    • Chen, Y.R.1    Huang, H.B.2    Chyan, C.L.3    Shiao, M.S.4    Lin, T.H.5    Chen, Y.C.6
  • 49
    • 34250779284 scopus 로고    scopus 로고
    • Aggregation drives "misfolding" in protein amyloid fiber formation
    • DOI 10.1080/13506120701260059, PII 779685983
    • S. Xu Aggregation drives "misfolding" in amyloid fiber formation Amyloid 14 2007 119 131 (Pubitemid 46956916)
    • (2007) Amyloid , vol.14 , Issue.2 , pp. 119-131
    • Xu, S.1
  • 51
    • 26444556824 scopus 로고    scopus 로고
    • Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence
    • DOI 10.1021/bi0508284
    • S.K. Maji, J.J. Amsden, K.J. Rothschild, M.M. Condron, and D.B. Teplow Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence Biochemistry 44 2005 13365 13376 (Pubitemid 41429459)
    • (2005) Biochemistry , vol.44 , Issue.40 , pp. 13365-13376
    • Maji, S.K.1    Amsden, J.J.2    Rothschild, K.J.3    Condron, M.M.4    Teplow, D.B.5
  • 52
    • 0014216816 scopus 로고
    • Effect of pH on the phosphorescence of tryptophan, tyrosine, and proteins
    • T. Truong, R. Bersohn, P. Brumer, C.K. Luk, and T. Tao Effect of pH on the phosphorescence of tryptophan, tyrosine, and proteins J. Biol. Chem. 212 1995 2979 2985
    • (1995) J. Biol. Chem. , vol.212 , pp. 2979-2985
    • Truong, T.1    Bersohn, R.2    Brumer, P.3    Luk, C.K.4    Tao, T.5
  • 53
    • 80054842999 scopus 로고    scopus 로고
    • Recognizing and avoiding artifacts in atomic force microscopy imaging
    • C. Canale, B. Torre, D. Ricci, and P.C. Braga Recognizing and avoiding artifacts in atomic force microscopy imaging Methods Mol. Biol. 736 2011 31 43
    • (2011) Methods Mol. Biol. , vol.736 , pp. 31-43
    • Canale, C.1    Torre, B.2    Ricci, D.3    Braga, P.C.4
  • 54
    • 33846005437 scopus 로고    scopus 로고
    • Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
    • DOI 10.1016/j.jmb.2006.11.009, PII S0022283606015385
    • M. Fändrich Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibril J. Mol. Biol. 365 2007 1266 1270 (Pubitemid 46048846)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1266-1270
    • Fandrich, M.1
  • 55
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of amyloid β (1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action
    • DOI 10.1002/cbic.200700427
    • M. Bartolini, C. Bertucci, M.L. Bolognesi, A. Cavalli, C. Melchiorre, and V. Andrisano Insight into the kinetic of amyloid β (1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action Chembiochem 8 2007 2152 2161 (Pubitemid 350220767)
    • (2007) ChemBioChem , vol.8 , Issue.17 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 56
  • 57
    • 80053379382 scopus 로고    scopus 로고
    • Binding of the molecular chaperone αb-crystallin to Aβ amyloid fibrils inhibits fibril elongation
    • S.L. Shammas Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation Biophys. J. 101 2011 1681 1689
    • (2011) Biophys. J. , vol.101 , pp. 1681-1689
    • Shammas, S.L.1
  • 58
    • 34648819365 scopus 로고    scopus 로고
    • The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of α-synuclein aggregates
    • DOI 10.1111/j.1440-1789.2007.00803.x
    • K. Wakabayashi The Lewy body in Parkinson's disease: molecules implicated in the formation and degradation of α-synuclein aggregates Neuropathology 27 2007 494 506 (Pubitemid 47459715)
    • (2007) Neuropathology , vol.27 , Issue.5 , pp. 494-506
    • Wakabayashi, K.1    Tanji, K.2    Mori, F.3    Takahashi, H.4
  • 59
    • 0042027771 scopus 로고    scopus 로고
    • Polyglutamine diseases and molecular chaperones
    • DOI 10.1080/1521654032000114339
    • Y. Kimura, and A. Kakizuka Polyglutamine diseases and molecular chaperones IUBMB Life 55 2003 337 345 (Pubitemid 36975544)
    • (2003) IUBMB Life , vol.55 , Issue.6 , pp. 337-345
    • Kimura, Y.1    Kakizuka, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.