메뉴 건너뛰기




Volumn 4, Issue 2, 2013, Pages 310-320

The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms

Author keywords

Alzheimer's disease; amyloid ; missense mutation; molecular dynamics simulations

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; MUTANT PROTEIN; NEW DRUG; OLIGOMER;

EID: 84874091627     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn300149j     Document Type: Article
Times cited : (37)

References (62)
  • 1
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-β precursor protein: Integrating structure with biological function
    • Reinhard, C., Hebert, S. S., and De Strooper, B. (2005) The amyloid-β precursor protein: integrating structure with biological function EMBO J. 24, 3996-4006
    • (2005) EMBO J. , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • Medicine -The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. and Selkoe, D. J. (2002) Medicine-The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A. and Higgins, G. A. (1992) Alzheimer's disease: the amyloid cascade hypothesis Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 5
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., and LaDu, M. J. (2002) Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability J. Biol. Chem. 277, 32046-32053
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 6
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe, D. J. (1999) Translating cell biology into therapeutic advances in Alzheimer's disease Nature 399, A23-A31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 7
    • 0028945660 scopus 로고
    • Evidence That Aβ42 Is the Real Culprit in Alzheimers-Disease
    • Younkin, S. G. (1995) Evidence That Aβ42 Is the Real Culprit in Alzheimers-Disease Ann. Neurol. 37, 287-288
    • (1995) Ann. Neurol. , vol.37 , pp. 287-288
    • Younkin, S.G.1
  • 9
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy -Implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. (2003) Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy- Implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease J. Biol. Chem. 278, 46179-46187
    • (2003) J. Biol. Chem. , vol.278 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5    Nagao, M.6    Shimizu, T.7    Shirasawa, T.8
  • 11
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • Grabowski, T. J., Cho, H. S., Vonsattel, J. P. G., Rebeck, G. W., and Greenberg, S. M. (2001) Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy Ann. Neurol. 49, 697-705
    • (2001) Ann. Neurol. , vol.49 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.G.3    Rebeck, G.W.4    Greenberg, S.M.5
  • 15
    • 84954358028 scopus 로고    scopus 로고
    • Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences
    • Yang, M. F. and Teplow, D. B. (2008) Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences J. Mol. Biol. 384, 450-464
    • (2008) J. Mol. Biol. , vol.384 , pp. 450-464
    • Yang, M.F.1    Teplow, D.B.2
  • 16
    • 33645396508 scopus 로고    scopus 로고
    • All-atom molecular dynamics studies of the full-length β-amyloid peptides
    • Luttmann, E. and Fels, G. (2006) All-atom molecular dynamics studies of the full-length β-amyloid peptides Chem. Phys. 323, 138-147
    • (2006) Chem. Phys. , vol.323 , pp. 138-147
    • Luttmann, E.1    Fels, G.2
  • 17
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's peptides Aβ 40 and 42 adopt distinct conformations in water: A combined MD/NMR study
    • Sgourakis, N. G., Yan, Y. L., McCallum, S. A., Wang, C. Y., and Garcia, A. E. (2007) The Alzheimer's peptides Aβ 40 and 42 adopt distinct conformations in water: A combined MD/NMR study J. Mol. Biol. 368, 1448-1457
    • (2007) J. Mol. Biol. , vol.368 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.L.2    McCallum, S.A.3    Wang, C.Y.4    Garcia, A.E.5
  • 18
    • 33845802653 scopus 로고    scopus 로고
    • Characterizations of distinct amyloidogenic conformations of the Aβ(1-40) and (1-42) peptides
    • Lim, K. H., Collver, H. H., Le, Y. T. H., Nagchowdhuri, P., and Kenney, J. M. (2007) Characterizations of distinct amyloidogenic conformations of the Aβ(1-40) and (1-42) peptides Biochem. Biophys. Res. Commun. 353, 443-449
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 443-449
    • Lim, K.H.1    Collver, H.H.2    Le, Y.T.H.3    Nagchowdhuri, P.4    Kenney, J.M.5
  • 20
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-Protein Assembly and Alzheimer Disease
    • Roychaudhuri, R., Yang, M., Hoshi, M. M., and Teplow, D. B. (2009) Amyloid beta-Protein Assembly and Alzheimer Disease J. Biol. Chem. 284, 4749-4753
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 21
    • 41749084194 scopus 로고    scopus 로고
    • Amyloid-β E22Δ variant induces synaptic alteration in mouse hippocampal slices
    • Takuma, H., Teraoka, R., Mori, H., and Tomiyama, T. (2008) Amyloid-β E22Δ variant induces synaptic alteration in mouse hippocampal slices NeuroReport 19, 615
    • (2008) NeuroReport , vol.19 , pp. 615
    • Takuma, H.1    Teraoka, R.2    Mori, H.3    Tomiyama, T.4
  • 22
    • 79955038897 scopus 로고    scopus 로고
    • The Osaka FAD Mutation E22Δ Leads to Formation of a Previously Unknown Type of Amyloid β Fibrils and Modulates Aβ Neurotoxicity Fibrillization and Neurotoxicity of E22Δ Variants of Aβ
    • Ovchinnikova, O. Y., Finder, V. H., Vodopivec, I., Nitsch, R. M., and Glockshuber, R. (2011) The Osaka FAD Mutation E22Δ Leads to Formation of a Previously Unknown Type of Amyloid β Fibrils and Modulates Aβ Neurotoxicity Fibrillization and Neurotoxicity of E22Δ Variants of Aβ J. Mol. Biol. 408, 780-791
    • (2011) J. Mol. Biol. , vol.408 , pp. 780-791
    • Ovchinnikova, O.Y.1    Finder, V.H.2    Vodopivec, I.3    Nitsch, R.M.4    Glockshuber, R.5
  • 24
    • 77950617631 scopus 로고    scopus 로고
    • A mouse model of amyloid-β oligomers: Their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo
    • Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., and Yamashita, T. (2010) A mouse model of amyloid-β oligomers: their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo J. Neurosci. 30, 4845-4856
    • (2010) J. Neurosci. , vol.30 , pp. 4845-4856
    • Tomiyama, T.1    Matsuyama, S.2    Iso, H.3    Umeda, T.4    Takuma, H.5    Ohnishi, K.6    Ishibashi, K.7    Teraoka, R.8    Sakama, N.9    Yamashita, T.10
  • 25
    • 80052205634 scopus 로고    scopus 로고
    • Structural dynamics of the Δe22 (Osaka) familial Alzheimer's disease-linked amyloid β-protein
    • Inayathullah, M. and Teplow, D. B. (2011) Structural dynamics of the ΔE22 (Osaka) familial Alzheimer's disease-linked amyloid β-protein Amyloid 1-12
    • (2011) Amyloid , pp. 1-12
    • Inayathullah, M.1    Teplow, D.B.2
  • 26
    • 84861142911 scopus 로고    scopus 로고
    • Alzheimer's Disease Amyloid β-Protein Mutations and Deletions That Define Neuronal Binding/Internalization As Early Stage Nonfibrillar/Fibrillar Aggregates and Late Stage Fibrils
    • Poduslo, J. F., Howell, K. G., Olson, N. C., Ramirez-Alvarado, M., and Kandimalla, K. K. (2012) Alzheimer's Disease Amyloid β-Protein Mutations and Deletions That Define Neuronal Binding/Internalization As Early Stage Nonfibrillar/Fibrillar Aggregates and Late Stage Fibrils Biochemistry 51, 3993-4003
    • (2012) Biochemistry , vol.51 , pp. 3993-4003
    • Poduslo, J.F.1    Howell, K.G.2    Olson, N.C.3    Ramirez-Alvarado, M.4    Kandimalla, K.K.5
  • 27
    • 79952938717 scopus 로고    scopus 로고
    • The Japanese Mutant Aβ (ΔE22-Aβ(1-39)) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ(1-40) into Atypical Fibrils by Δe22-Aβ(1-39)
    • Cloe, A. L., Orgel, J. P. R. O., Sachleben, J. R., Tycko, R., and Meredith, S. C. (2011) The Japanese Mutant Aβ (ΔE22-Aβ(1-39)) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ(1-40) into Atypical Fibrils by ΔE22-Aβ(1-39) Biochemistry 50, 2026-2039
    • (2011) Biochemistry , vol.50 , pp. 2026-2039
    • Cloe, A.L.1    Orgel, J.P.R.O.2    Sachleben, J.R.3    Tycko, R.4    Meredith, S.C.5
  • 30
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid β-protein fibrillogenesis
    • Teplow, D. B. (1998) Structural and kinetic features of amyloid β-protein fibrillogenesis Amyloid\ 5, 121-142
    • (1998) Amyloid\ , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 31
    • 0028981219 scopus 로고
    • Structure-Activity Analyses of β-Amyloid Peptides -Contributions of the β25-35 Region to Aggregation and Neurotoxicity
    • Pike, C. J., Walencewiczwasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., and Cotman, C. W. (1995) Structure-Activity Analyses of β-Amyloid Peptides-Contributions of the β25-35 Region to Aggregation and Neurotoxicity J. Neurochem. 64, 253-265
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewiczwasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 32
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure -Pattern-Recognition of Hydrogen-Bonded and Geometrical Features
    • Kabsch, W. and Sander, C. (1983) Dictionary of Protein Secondary Structure-Pattern-Recognition of Hydrogen-Bonded and Geometrical Features Biopolymers 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 38
    • 33845570428 scopus 로고    scopus 로고
    • Dynamics of Asp23-Lys28 salt-bridge formation in Aβ(10-35) monomers
    • Tarus, B., Straub, J. E., and Thirumalai, D. (2006) Dynamics of Asp23-Lys28 salt-bridge formation in Aβ(10-35) monomers J. Am. Chem. Soc. 128, 16159-16168
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16159-16168
    • Tarus, B.1    Straub, J.E.2    Thirumalai, D.3
  • 39
    • 61949475048 scopus 로고    scopus 로고
    • Influence of Preformed Asp23-Lys28 Salt Bridge on the Conformational Fluctuations of Monomers and Dimers of A beta Peptides with Implications for Rates of Fibril Formation
    • Reddy, G., Straub, J. E., and Thirumalai, D. (2009) Influence of Preformed Asp23-Lys28 Salt Bridge on the Conformational Fluctuations of Monomers and Dimers of A beta Peptides with Implications for Rates of Fibril Formation J. Phys. Chem B. 113, 1162-1172
    • (2009) J. Phys. Chem B. , vol.113 , pp. 1162-1172
    • Reddy, G.1    Straub, J.E.2    Thirumalai, D.3
  • 40
    • 82555173714 scopus 로고    scopus 로고
    • Amyloid-β peptide structure in aqueous solution varies with fragment size
    • Wise-Scira, O., Xu, L., Kitahara, T., Perry, G., and Coskuner, O. (2011) Amyloid-β peptide structure in aqueous solution varies with fragment size J. Chem. Phys. 135, 205101
    • (2011) J. Chem. Phys. , vol.135 , pp. 205101
    • Wise-Scira, O.1    Xu, L.2    Kitahara, T.3    Perry, G.4    Coskuner, O.5
  • 41
    • 78650863624 scopus 로고    scopus 로고
    • Atomic-Level Characterization of the Ensemble of the Aβ(1-42) Monomer in Water Using Unbiased Molecular Dynamics Simulations and Spectral Algorithms
    • Sgourakis, N. G., Merced-Serrano, M., Boutsidis, C., Drineas, P., Du, Z. M., Wang, C. Y., and Garcia, A. E. (2011) Atomic-Level Characterization of the Ensemble of the Aβ(1-42) Monomer in Water Using Unbiased Molecular Dynamics Simulations and Spectral Algorithms J. Mol. Biol. 405, 570-583
    • (2011) J. Mol. Biol. , vol.405 , pp. 570-583
    • Sgourakis, N.G.1    Merced-Serrano, M.2    Boutsidis, C.3    Drineas, P.4    Du, Z.M.5    Wang, C.Y.6    Garcia, A.E.7
  • 43
    • 48549095605 scopus 로고    scopus 로고
    • Comparative Molecular Dynamics Studies of Wild-Type and Oxidized Forms of Full-Length Alzheimer Amyloid β-Peptides Aβ(1-40) and Aβ(1-42)
    • Triguero, L., Singh, R., and Prabhakar, R. (2008) Comparative Molecular Dynamics Studies of Wild-Type and Oxidized Forms of Full-Length Alzheimer Amyloid β-Peptides Aβ(1-40) and Aβ(1-42) J. Phys. Chem. B 112, 7123-7131
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7123-7131
    • Triguero, L.1    Singh, R.2    Prabhakar, R.3
  • 44
    • 0027258525 scopus 로고
    • The Carboxy Terminus of the β-Amyloid Protein Is Critical for the Seeding of Amyloid Formation -Implications for the Pathogenesis of Alzheimers-Disease
    • Jarrett, J. T., Berger, E. P., and Lansbury, P. T. (1993) The Carboxy Terminus of the β-Amyloid Protein Is Critical for the Seeding of Amyloid Formation-Implications for the Pathogenesis of Alzheimers-Disease Biochemistry 32, 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 45
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., and Teplow, D. B. (1996) On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants Proc. Natl. Acad. Sci. U.S.A. 93, 1125-1129
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 48
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis -Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) Amyloid β-protein fibrillogenesis-Detection of a protofibrillar intermediate J. Biol. Chem. 272, 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
  • 49
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita, Y. and Okamoto, Y. (1999) Replica-exchange molecular dynamics method for protein folding Chem. Phys. Lett. 314, 141-151
    • (1999) Chem. Phys. Lett. , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 51
    • 32344451179 scopus 로고    scopus 로고
    • The α-to-β Conformational Transition of Alzheimer's Aβ-(1-42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of β Conformation Seeding
    • Tomaselli, S., Esposito, V., Vangone, P., van Nuland, N. A. J., Bonvin, A. M. J. J., Guerrini, R., Tancredi, T., Temussi, P. A., and Picone, D. (2006) The α-to-β Conformational Transition of Alzheimer's Aβ-(1-42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of β Conformation Seeding ChemBioChem 7, 257-267
    • (2006) ChemBioChem , vol.7 , pp. 257-267
    • Tomaselli, S.1    Esposito, V.2    Vangone, P.3    Van Nuland, N.A.J.4    Bonvin, A.M.J.J.5    Guerrini, R.6    Tancredi, T.7    Temussi, P.A.8    Picone, D.9
  • 52
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple amber force fields and development of improved protein backbone parameters
    • Simmerling, C., Hornak, V., Abel, R., Okur, A., Strockbine, B., and Roitberg, A. (2006) Comparison of multiple amber force fields and development of improved protein backbone parameters Proteins 65, 712-725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Simmerling, C.1    Hornak, V.2    Abel, R.3    Okur, A.4    Strockbine, B.5    Roitberg, A.6
  • 53
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Case, D. A., Onufriev, A., and Bashford, D. (2004) Exploring protein native states and large-scale conformational changes with a modified generalized born model Proteins 55, 383-394
    • (2004) Proteins , vol.55 , pp. 383-394
    • Case, D.A.1    Onufriev, A.2    Bashford, D.3
  • 54
    • 84865652373 scopus 로고    scopus 로고
    • Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics
    • Wise-Scira, O., Xu, L., Perry, G., and Coskuner, O. (2012) Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics J. Biol. Inorg. Chem. 17, 927-938
    • (2012) J. Biol. Inorg. Chem. , vol.17 , pp. 927-938
    • Wise-Scira, O.1    Xu, L.2    Perry, G.3    Coskuner, O.4
  • 55
    • 79960237265 scopus 로고    scopus 로고
    • Replica Temperatures for Uniform Exchange and Efficient Roundtrip Times in Explicit Solvent Parallel Tempering Simulations
    • Prakash, M. K., Barducci, A., and Parrinello, M. (2011) Replica Temperatures for Uniform Exchange and Efficient Roundtrip Times in Explicit Solvent Parallel Tempering Simulations J. Chem. Theory Comput. 7, 2025-2027
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 2025-2027
    • Prakash, M.K.1    Barducci, A.2    Parrinello, M.3
  • 58
    • 41549127613 scopus 로고    scopus 로고
    • A temperature predictor for parallel tempering simulations
    • van der Spoel, D. and Patriksson, A. (2008) A temperature predictor for parallel tempering simulations Phys. Chem. Chem. Phys. 10, 2073-2077
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2073-2077
    • Van Der Spoel, D.1    Patriksson, A.2
  • 60
    • 0028331255 scopus 로고
    • Normal-Mode Analysis of Protein Dynamics
    • Case, D. A. (1994) Normal-Mode Analysis of Protein Dynamics Curr. Opin. Struct. Biol. 4, 285-290
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 285-290
    • Case, D.A.1
  • 61
    • 0001351515 scopus 로고
    • Estimation of Absolute and Relative Entropies of Macromolecules Using the Covariance-Matrix
    • Schlitter, J. (1993) Estimation of Absolute and Relative Entropies of Macromolecules Using the Covariance-Matrix Chem. Phys. Lett. 215, 617-621
    • (1993) Chem. Phys. Lett. , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 62
    • 0037340909 scopus 로고    scopus 로고
    • MD simulation of protein-ligand interaction: Formation and dissociation of an insulin-phenol complex
    • Schlitter, J., Swegat, W., Kruger, P., and Wollmer, A. (2003) MD simulation of protein-ligand interaction: Formation and dissociation of an insulin-phenol complex Biophys. J. 84, 1493-1506
    • (2003) Biophys. J. , vol.84 , pp. 1493-1506
    • Schlitter, J.1    Swegat, W.2    Kruger, P.3    Wollmer, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.