메뉴 건너뛰기




Volumn , Issue , 2008, Pages 1-39

NMR of amyloidogenic proteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84874067106     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (3)

References (139)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease.Annu Rev Biochem. 75,333-366
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways.Curr Opin Struct Biol.8,101-106
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 3
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo, E. H., Lansbury, P. T., Jr. and Kelly, J. W. (1999) Amyloid diseases: abnormal protein aggregation in neurodegeneration.Proc Natl Acad Sci U S A. 96,9989-9990
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 4
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003) Protein folding and misfolding.Nature. 426,884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 5
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen, F. E. and Kelly, J. W. (2003) Therapeutic approaches to protein-misfolding diseases.Nature. 426,905-909
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 6
    • 0033520495 scopus 로고    scopus 로고
    • An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils
    • Alexandrescu, A. T. and Rathgeb-Szabo, K. (1999) An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.J Mol Biol. 291,1191-1206
    • (1999) J Mol Biol , vol.291 , pp. 1191-1206
    • Alexandrescu, A.T.1    Rathgeb-Szabo, K.2
  • 7
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich, M., Fletcher, M. A. and Dobson, C. M. (2001) Amyloid fibrils from muscle myoglobin.Nature. 410,165-166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 9
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. (1999) Protein misfolding, evolution and disease.Trends Biochem Sci. 24, 329-332
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 11
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson, S. M., Wiseman, R. L., Sekijima, Y., Green, N. S., Adamski-Werner, S. L. and Kelly, J. W. (2005) Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses.Acc Chem Res.38,911-921
    • (2005) Acc Chem Res , vol.38 , pp. 911-921
    • Johnson, S.M.1    Wiseman, R.L.2    Sekijima, Y.3    Green, N.S.4    Adamski-Werner, S.L.5    Kelly, J.W.6
  • 13
    • 0037162520 scopus 로고    scopus 로고
    • Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties
    • Trinh, C. H., Smith, D. P., Kalverda, A. P., Phillips, S. E. and Radford, S. E. (2002) Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties.Proc Natl Acad Sci U S A. 99,9771-9776
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9771-9776
    • Trinh, C.H.1    Smith, D.P.2    Kalverda, A.P.3    Phillips, S.E.4    Radford, S.E.5
  • 14
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • Eliezer, D., Kutluay, E., Bussell, R., Jr. and Browne, G. (2001) Conformational properties of alpha-synuclein in its free and lipid-associated states.J Mol Biol. 307,1061-1073
    • (2001) J Mol Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, R.3    Browne, G.4
  • 16
    • 33845960266 scopus 로고    scopus 로고
    • Direct detection of transient alpha-helical states in islet amyloid polypeptide
    • Williamson, J. A. and Miranker, A. D. (2007) Direct detection of transient alpha-helical states in islet amyloid polypeptide.Protein Sci. 16,110-117
    • (2007) Protein Sci , vol.16 , pp. 110-117
    • Williamson, J.A.1    Miranker, A.D.2
  • 17
    • 0029156906 scopus 로고
    • Study of human calcitonin fibrillation by proton nuclear magnetic resonance spectroscopy
    • Kanaori, K. and Nosaka, A. Y. (1995) Study of human calcitonin fibrillation by proton nuclear magnetic resonance spectroscopy.Biochemistry. 34,12138-12143
    • (1995) Biochemistry , vol.34 , pp. 12138-12143
    • Kanaori, K.1    Nosaka, A.Y.2
  • 20
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid
    • Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B. and Ishii, Y. (2007) Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid.Nat Struct Mol Biol. 14,1157-1164
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 21
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira, S. T., Vieira, M. N. and De Felice, F. G. (2007) Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life.59,332-345
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 22
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury, P. T. and Lashuel, H. A. (2006) A century-old debate on protein aggregation and neurodegeneration enters the clinic.Nature. 443, 774-779
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 23
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A. and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease.Nat Med. 10 Suppl, S10-17
    • (2004) Nat Med. 10 Suppl , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 24
    • 0033065103 scopus 로고    scopus 로고
    • Agrin in Alzheimer's disease: Altered solubility and abnormal distribution within microvasculature and brain parenchyma
    • Donahue, J. E., Berzin, T. M., Rafii, M. S., Glass, D. J., Yancopoulos, G. D., Fallon, J. R. and Stopa, E. G. (1999) Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma.Proc Natl Acad Sci USA. 96,6468-6472
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6468-6472
    • Donahue, J.E.1    Berzin, T.M.2    Rafii, M.S.3    Glass, D.J.4    Yancopoulos, G.D.5    Fallon, J.R.6    Stopa, E.G.7
  • 25
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush, A. I. (2003) The metallobiology of Alzheimer's disease.Trends Neurosci. 26,207-214
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 27
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T. and Lansbury, P. T., Jr. (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature.418,291
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 28
    • 0028109336 scopus 로고
    • The US economic and social costs of Alzheimer's disease revisited
    • Ernst, R. L. and Hay, J. W. (1994) The US economic and social costs of Alzheimer's disease revisited.Am J Public Health. 84,1261-1264
    • (1994) Am J Public Health , vol.84 , pp. 1261-1264
    • Ernst, R.L.1    Hay, J.W.2
  • 29
    • 0036860349 scopus 로고    scopus 로고
    • Metal complexing agents as therapies for Alzheimer's disease
    • Bush, A. I. (2002) Metal complexing agents as therapies for Alzheimer's disease.NeurobiolAging. 23,1031-1038
    • (2002) Neurobiolaging , vol.23 , pp. 1031-1038
    • Bush, A.I.1
  • 30
    • 0033953066 scopus 로고    scopus 로고
    • Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain
    • Cotman, S. L., Halfter, W. and Cole, G. J. (2000) Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain.Mol Cell Neurosci. 15,183-198
    • (2000) Mol Cell Neurosci , vol.15 , pp. 183-198
    • Cotman, S.L.1    Halfter, W.2    Cole, G.J.3
  • 31
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, Notch, and the genesis and treatment of Alzheimer's disease
    • Selkoe, D. J. (2001) Presenilin, Notch, and the genesis and treatment of Alzheimer's disease.Proc Natl Acad Sci US A. 98,11039-11041
    • (2001) Proc Natl Acad Sci US A , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 32
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., Mclntire, T. M., Milton, S. C., Cotman, C. W. and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis.Science. 300,486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McLntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 34
    • 0036150971 scopus 로고    scopus 로고
    • The synucleins
    • REVIEWS3002
    • George, J. M. (2002) The synucleins.Genome Biol.3, REVIEWS3002
    • (2002) Genome Biol , vol.3
    • George, J.M.1
  • 35
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson, M. R. (2005) The biochemistry of Parkinson's disease.Annu Rev Biochem. 74,29-52
    • (2005) Annu Rev Biochem , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 37
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert, M. (2001) Alpha-synuclein and neurodegenerative diseases.Nat Rev Neurosci. 2,492-501
    • (2001) Nat Rev Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 38
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • Fink, A. L. (2006) The aggregation and fibrillation of alpha-synuclein.Acc Chem Res. 39, 628-634
    • (2006) Acc Chem Res , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 39
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E. and Lansbury, P. T., Jr. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.Proc Natl Acad Sci US A. 97,571-576
    • (2000) Proc Natl Acad Sci US A , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 41
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A. and Lansbury, P. T., Jr. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.Biochemistry. 35,13709-13715
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5
  • 42
    • 17044446282 scopus 로고    scopus 로고
    • NMR studies of structure and function of biological macromolecules (Nobel lecture)
    • Wuthrich, K. (2003) NMR studies of structure and function of biological macromolecules (Nobel lecture).Angew Chem Int Ed Engl. 42,3340-3363
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3340-3363
    • Wuthrich, K.1
  • 43
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle, D. R. (1996) Structural analysis of non-native states of proteins by NMR methods.Curr Opin Struct Biol.6, 24-30
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 44
    • 0035234662 scopus 로고    scopus 로고
    • An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A
    • Alexandrescu, A. T. (2001) An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.Pac Symp Biocomput,67-78
    • (2001) Pac Symp Biocomput , pp. 67-78
    • Alexandrescu, A.T.1
  • 45
    • 4744357287 scopus 로고    scopus 로고
    • Structural and dynamic studies of proteins by solid-state NMR spectroscopy: Rapid movement forward
    • McDermott, A. E. (2004) Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward.Curr Opin Struct Biol. 14,554-561
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 554-561
    • McDermott, A.E.1
  • 46
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko, R. (2006) Molecular structure of amyloid fibrils: insights from solid-state NMR.Q Rev Biophys. 39,1-55
    • (2006) Q Rev Biophys , vol.39 , pp. 1-55
    • Tycko, R.1
  • 48
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova, A. T., Yau, W. M. and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils.Biochemistry. 45,498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 50
    • 1542346922 scopus 로고    scopus 로고
    • Detection of amyloid plaques in mouse models of Alzheimer's disease by magnetic resonance imaging
    • Zhang, J., Yarowsky, P., Gordon, M. N., Di Carlo, G., Munireddy, S., van Zijl, P. C. and Mori, S. (2004) Detection of amyloid plaques in mouse models of Alzheimer's disease by magnetic resonance imaging.Magn ResonMed. 51,452-457
    • (2004) Magn Resonmed , vol.51 , pp. 452-457
    • Zhang, J.1    Yarowsky, P.2    Gordon, M.N.3    Di Carlo, G.4    Munireddy, S.5    Van Zijl, P.C.6    Mori, S.7
  • 52
    • 34447310291 scopus 로고    scopus 로고
    • Neuroimaging in dementia
    • Whitwell, J. L. and Jack, C. R., Jr. (2007) Neuroimaging in dementia.Neurol Clin. 25,843-857, viii
    • (2007) Neurol Clin , vol.25 , Issue.8 , pp. 843-857
    • Whitwell, J.L.1    Jack, C.R.2
  • 54
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
    • Cobb, N. J., Sonnichsen, F. D., McHaourab, H. and Surewicz, W. K. (2007) Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure.Proc Natl Acad Sci U S A. 104,18946-18951
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sonnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 55
    • 0028067152 scopus 로고
    • Protein stability parameters measured by hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L. and Englander, S. W. (1994) Protein stability parameters measured by hydrogen exchange.Proteins. 20,4-14
    • (1994) Proteins , vol.20 , pp. 4-14
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 56
  • 57
    • 0036306257 scopus 로고    scopus 로고
    • Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin
    • Liu, K., Kelly, J. W. and Wemmer, D. E. (2002) Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin.J Mol Biol. 320,821-832
    • (2002) J Mol Biol , vol.320 , pp. 821-832
    • Liu, K.1    Kelly, J.W.2    Wemmer, D.E.3
  • 60
    • 0344839082 scopus 로고    scopus 로고
    • Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: Implications for the pathology of familial amyotrophic lateral sclerosis
    • Shipp, E. L., Cantini, F., Bertini, I., Valentine, J. S. and Banci, L. (2003) Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.Biochemistry. 42,1890-1899
    • (2003) Biochemistry , vol.42 , pp. 1890-1899
    • Shipp, E.L.1    Cantini, F.2    Bertini, I.3    Valentine, J.S.4    Banci, L.5
  • 61
    • 0034984208 scopus 로고    scopus 로고
    • Nmr probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer, A. G., III. (2001) Nmr probes of molecular dynamics: overview and comparison with other techniques.Annu Rev Biophys Biomol Struct.30, 129-155
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 129-155
    • Palmer, A.G.1
  • 62
    • 0030602880 scopus 로고    scopus 로고
    • Accretion of structure in staphylococcal nuclease: An 15N NMR relaxation study
    • Alexandrescu, A. T., Jahnke, W., Wiltscheck, R. and Blommers, M. J. (1996) Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study.J Mol Biol. 260,570-587
    • (1996) J Mol Biol , vol.260 , pp. 570-587
    • Alexandrescu, A.T.1    Jahnke, W.2    Wiltscheck, R.3    Blommers, M.J.4
  • 63
    • 0029786948 scopus 로고    scopus 로고
    • A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease
    • Wang, Y. and Shortle, D. (1996) A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease.Protein Sci. 5,1898-1906
    • (1996) Protein Sci , vol.5 , pp. 1898-1906
    • Wang, Y.1    Shortle, D.2
  • 64
    • 0034645777 scopus 로고    scopus 로고
    • NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN
    • Alexandrescu, A. T., Lamour, F. P. and Jaravine, V. A. (2000) NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN. J Mol Biol.295,239-255
    • (2000) J Mol Biol , vol.295 , pp. 239-255
    • Alexandrescu, A.T.1    Lamour, F.P.2    Jaravine, V.A.3
  • 65
    • 48249099670 scopus 로고    scopus 로고
    • Hydrogen exchange of monomeric a-synuclein shows the unfolded structure is retained at physiological temperature and is independent of molecular crowding in Escherichia coli
    • press
    • Croke, R. L., Sallum, C. O., Watson, E. and Alexandrescu, A. T. (2008) Hydrogen exchange of monomeric a-synuclein shows the unfolded structure is retained at physiological temperature and is independent of molecular crowding in Escherichia coli.Protein Sci., in press.
    • (2008) Protein Sci
    • Croke, R.L.1    Sallum, C.O.2    Watson, E.3    Alexandrescu, A.T.4
  • 66
    • 0036240398 scopus 로고    scopus 로고
    • Structural properties of an amyloid precursor of beta(2)-microglobulin
    • McParland, V. J., Kalverda, A. P., Homans, S. W. and Radford, S. E. (2002) Structural properties of an amyloid precursor of beta(2)-microglobulin.Nat Struct Biol.9, 326-331
    • (2002) Nat Struct Biol , vol.9 , pp. 326-331
    • McParland, V.J.1    Kalverda, A.P.2    Homans, S.W.3    Radford, S.E.4
  • 67
    • 0036242430 scopus 로고    scopus 로고
    • Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange
    • Hoshino, M., Katou, H., Hagihara, Y., Hasegawa, K., Naiki, H. and Goto, Y. (2002) Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange.Nat Struct Biol.9, 332-336
    • (2002) Nat Struct Biol , vol.9 , pp. 332-336
    • Hoshino, M.1    Katou, H.2    Hagihara, Y.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 68
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study
    • Alexandrescu, A. T., Abeygunawardana, C. and Shortle, D. (1994) Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study.Biochemistry. 33,1063-1072
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 69
    • 0035173352 scopus 로고    scopus 로고
    • NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox)
    • Riek, R., Guntert, P., Dobeli, H., Wipf, B. and Wuthrich, K. (2001) NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox).Eur J Biochem. 268,5930-5936
    • (2001) Eur J Biochem , vol.268 , pp. 5930-5936
    • Riek, R.1    Guntert, P.2    Dobeli, H.3    Wipf, B.4    Wuthrich, K.5
  • 70
    • 12344328360 scopus 로고    scopus 로고
    • Residual structure in the repeat domain of tau: Echoes of microtubule binding and paired helical filament formation
    • Eliezer, D., Barre, P., Kobaslija, M., Chan, D., Li, X. and Heend, L. (2005) Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation.Biochemistry. 44,1026-1036
    • (2005) Biochemistry , vol.44 , pp. 1026-1036
    • Eliezer, D.1    Barre, P.2    Kobaslija, M.3    Chan, D.4    Li, X.5    Heend, L.6
  • 71
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions
    • Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E. and Zweckstetter, M. (2005) Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions.J Biol Chem. 280,24978-24986
    • (2005) J Biol Chem , vol.280 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    Von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 72
    • 0032530953 scopus 로고    scopus 로고
    • Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching?
    • Watson, A. A., Fairlie, D. P. and Craik, D. J. (1998) Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching?Biochemistry. 37,12700-12706
    • (1998) Biochemistry , vol.37 , pp. 12700-12706
    • Watson, A.A.1    Fairlie, D.P.2    Craik, D.J.3
  • 74
    • 33746265961 scopus 로고    scopus 로고
    • 15N relaxation study of the amyloid beta-peptide: Structural propensities and persistence length
    • Spec No
    • Danielsson, J., Andersson, A., Jarvet, J. and Graslund, A. (2006) 15N relaxation study of the amyloid beta-peptide: structural propensities and persistence length.Magn Reson Chem. 44 Spec No, S114-121
    • (2006) Magn Reson Chem , vol.44 , pp. S114-S121
    • Danielsson, J.1    Andersson, A.2    Jarvet, J.3    Graslund, A.4
  • 75
    • 33751106208 scopus 로고    scopus 로고
    • Abeta42 is more rigid than Abeta40 at the C terminus: Implications for Abeta aggregation and toxicity
    • Yan, Y. and Wang, C. (2006) Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity.J Mol Biol. 364,853-862
    • (2006) J Mol Biol , vol.364 , pp. 853-862
    • Yan, Y.1    Wang, C.2
  • 76
    • 33845665797 scopus 로고    scopus 로고
    • High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide
    • Danielsson, J., Pierattelli, R., Banci, L. and Graslund, A. (2007) High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide.FEBS J. 274,46-59
    • (2007) FEBS J , vol.274 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 77
    • 33746335362 scopus 로고    scopus 로고
    • NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease
    • Hou, L. and Zagorski, M. G. (2006) NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease.J Am Chem Soc. 128,9260-9261
    • (2006) J am Chem Soc , vol.128 , pp. 9260-9261
    • Hou, L.1    Zagorski, M.G.2
  • 78
    • 33746925586 scopus 로고    scopus 로고
    • Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13
    • Williamson, M. P., Suzuki, Y., Bourne, N. T. and Asakura, T. (2006) Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13.Biochem J.397,483-490
    • (2006) Biochem J , vol.397 , pp. 483-490
    • Williamson, M.P.1    Suzuki, Y.2    Bourne, N.T.3    Asakura, T.4
  • 79
    • 0344255649 scopus 로고    scopus 로고
    • Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide
    • Petkova, A. T., Buntkowsky, G., Dyda, F., Leapman, R. D., Yau, W. M. and Tycko, R. (2004) Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide.J Mol Biol. 335,247-260
    • (2004) J Mol Biol , vol.335 , pp. 247-260
    • Petkova, A.T.1    Buntkowsky, G.2    Dyda, F.3    Leapman, R.D.4    Yau, W.M.5    Tycko, R.6
  • 80
  • 81
    • 0033572813 scopus 로고    scopus 로고
    • Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth
    • McLaurin, J., Franklin, T., Zhang, X., Deng, J. and Fraser, P. E. (1999) Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth.Eur J Biochem. 266,1101-1110
    • (1999) Eur J Biochem , vol.266 , pp. 1101-1110
    • McLaurin, J.1    Franklin, T.2    Zhang, X.3    Deng, J.4    Fraser, P.E.5
  • 82
    • 34248586543 scopus 로고    scopus 로고
    • Abeta40 protects non-toxic Abeta42 monomer from aggregation
    • Yan, Y. and Wang, C. (2007) Abeta40 protects non-toxic Abeta42 monomer from aggregation.J Mol Biol. 369,909-916
    • (2007) J Mol Biol , vol.369 , pp. 909-916
    • Yan, Y.1    Wang, C.2
  • 83
    • 13444310701 scopus 로고    scopus 로고
    • Characterization of chemical exchange between soluble and aggregated states of beta-amyloid by solution-state NMR upon variation of salt conditions
    • Narayanan, S. and Reif, B. (2005) Characterization of chemical exchange between soluble and aggregated states of beta-amyloid by solution-state NMR upon variation of salt conditions.Biochemistry. 44,1444-1452
    • (2005) Biochemistry , vol.44 , pp. 1444-1452
    • Narayanan, S.1    Reif, B.2
  • 84
    • 33644538922 scopus 로고    scopus 로고
    • Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein
    • McNulty, B. C., Tripathy, A., Young, G. B., Charlton, L. M., Orans, J. and Pielak, G. J. (2006) Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein.Protein Sci. 15,602-608
    • (2006) Protein Sci , vol.15 , pp. 602-608
    • McNulty, B.C.1    Tripathy, A.2    Young, G.B.3    Charlton, L.M.4    Orans, J.5    Pielak, G.J.6
  • 86
    • 0035824545 scopus 로고    scopus 로고
    • Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein
    • Bussell, R., Jr. and Eliezer, D. (2001) Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein.J Biol Chem. 276,45996-46003
    • (2001) J Biol Chem , vol.276 , pp. 45996-46003
    • Bussell, R.1    Eliezer, D.2
  • 87
    • 29844433240 scopus 로고    scopus 로고
    • Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings
    • Bernado, P., Bertoncini, C. W., Griesinger, C., Zweckstetter, M. and Blackledge, M. (2005) Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings.J Am Chem Soc. 127,17968-17969
    • (2005) J am Chem Soc , vol.127 , pp. 17968-17969
    • Bernado, P.1    Bertoncini, C.W.2    Griesinger, C.3    Zweckstetter, M.4    Blackledge, M.5
  • 88
    • 33947362842 scopus 로고    scopus 로고
    • Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau
    • Cho, M. K., Kim, H. Y., Bernado, P., Fernandez, C. O., Blackledge, M. and Zweckstetter, M. (2007) Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau. J Am Chem Soc.129,3032-3033
    • (2007) J am Chem Soc , vol.129 , pp. 3032-3033
    • Cho, M.K.1    Kim, H.Y.2    Bernado, P.3    Fernandez, C.O.4    Blackledge, M.5    Zweckstetter, M.6
  • 89
    • 34548184125 scopus 로고    scopus 로고
    • Residual structure, backbone dynamics, and interactions within the synuclein family
    • Sung, Y. H. and Eliezer, D. (2007) Residual structure, backbone dynamics, and interactions within the synuclein family.J Mol Biol. 372,689-707
    • (2007) J Mol Biol , vol.372 , pp. 689-707
    • Sung, Y.H.1    Eliezer, D.2
  • 90
    • 12944304172 scopus 로고    scopus 로고
    • Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations
    • Dedmon, M. M., Lindorff-Larsen, K., Christodoulou, J., Vendruscolo, M. and Dobson, C. M. (2005) Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.J Am Chem Soc. 127,476-477
    • (2005) J am Chem Soc , vol.127 , pp. 476-477
    • Dedmon, M.M.1    Lindorff-Larsen, K.2    Christodoulou, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 91
    • 35548943472 scopus 로고    scopus 로고
    • Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement
    • Clore, G. M., Tang, C. and Iwahara, J. (2007) Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement.Curr Opin Struct Biol. 17,603-616
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 603-616
    • Clore, G.M.1    Tang, C.2    Iwahara, J.3
  • 93
    • 29544433937 scopus 로고    scopus 로고
    • Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder.J Mol Biol
    • McNulty, B. C., Young, G. B. and Pielak, G. J. (2006) Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder.J Mol Biol.355, 893-897
    • (2006) 355 , pp. 893-897
    • McNulty, B.C.1    Young, G.B.2    Pielak, G.J.3
  • 94
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation
    • Marsh, J. A., Singh, V. K., Jia, Z. and Forman-Kay, J. D. (2006) Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation.Protein Sci. 15,2795-2804
    • (2006) Protein Sci , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 95
    • 0031989849 scopus 로고    scopus 로고
    • Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme
    • Hwang, T. L., van Zijl, P. C. and Mori, S. (1998) Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme.J Biomol NMR. 11,221-226
    • (1998) J Biomol NMR , vol.11 , pp. 221-226
    • Hwang, T.L.1    Van Zijl, P.C.2    Mori, S.3
  • 96
    • 0042665956 scopus 로고    scopus 로고
    • Quantitative identification of the protonation state of histidines in vitro and in vivo
    • Shimba, N., Serber, Z., Ledwidge, R., Miller, S. M., Craik, C. S. and Dotsch, V. (2003) Quantitative identification of the protonation state of histidines in vitro and in vivo.Biochemistry.42, 9227-9234
    • (2003) Biochemistry , vol.42 , pp. 9227-9234
    • Shimba, N.1    Serber, Z.2    Ledwidge, R.3    Miller, S.M.4    Craik, C.S.5    Dotsch, V.6
  • 98
    • 33644847016 scopus 로고    scopus 로고
    • NMR mapping of copper binding sites in alpha-synuclein
    • Sung, Y. H., Rospigliosi, C. and Eliezer, D. (2006) NMR mapping of copper binding sites in alpha-synuclein.Biochim Biophys Acta. 1764,5-12
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 5-12
    • Sung, Y.H.1    Rospigliosi, C.2    Eliezer, D.3
  • 99
    • 33746633380 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement
    • Binolfi, A., Rasia, R. M., Bertoncini, C. W., Ceolin, M., Zweckstetter, M., Griesinger, C., Jovin, T. M. and Fernandez, C. O. (2006) Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement.J Am Chem Soc. 128,9893-9901
    • (2006) J am Chem Soc , vol.128 , pp. 9893-9901
    • Binolfi, A.1    Rasia, R.M.2    Bertoncini, C.W.3    Ceolin, M.4    Zweckstetter, M.5    Griesinger, C.6    Jovin, T.M.7    Fernandez, C.O.8
  • 100
    • 33748584602 scopus 로고    scopus 로고
    • Interaction between Abeta peptide and alpha synuclein: Molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease
    • Mandal, P. K., Pettegrew, J. W., Masliah, E., Hamilton, R. L. and Mandal, R. (2006) Interaction between Abeta peptide and alpha synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease.Neurochem Res. 31,1153-1162
    • (2006) Neurochem Res , vol.31 , pp. 1153-1162
    • Mandal, P.K.1    Pettegrew, J.W.2    Masliah, E.3    Hamilton, R.L.4    Mandal, R.5
  • 101
    • 85035045151 scopus 로고    scopus 로고
    • Interaction between Abeta Peptide and alpha Synuclein: Molecular Mechanisms in Overlapping Pathology of Alzheimer's and Parkinson's in Dementia with Lewy Body Disease
    • Mandal, P. K. and Pettegrew, J. W. (2007) “Interaction between Abeta Peptide and alpha Synuclein: Molecular Mechanisms in Overlapping Pathology of Alzheimer's and Parkinson's in Dementia with Lewy Body Disease”.Neurochem Res 33,220
    • (2007) Neurochem Res , vol.33 , pp. 220
    • Mandal, P.K.1    Pettegrew, J.W.2
  • 102
    • 34250796802 scopus 로고    scopus 로고
    • The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states
    • Fredenburg, R. A., Rospigliosi, C., Meray, R. K., Kessler, J. C., Lashuel, H. A., Eliezer, D. and Lansbury, P. T., Jr. (2007) The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states.Biochemistry.46, 7107-7118
    • (2007) Biochemistry , vol.46 , pp. 7107-7118
    • Fredenburg, R.A.1    Rospigliosi, C.2    Meray, R.K.3    Kessler, J.C.4    Lashuel, H.A.5    Eliezer, D.6    Lansbury, P.T.7
  • 103
    • 34548189188 scopus 로고    scopus 로고
    • Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation
    • Bertoncini, C. W., Rasia, R. M., Lamberto, G. R., Binolfi, A., Zweckstetter, M., Griesinger, C. and Fernandez, C. O. (2007) Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation.J Mol Biol. 372,708-722
    • (2007) J Mol Biol , vol.372 , pp. 708-722
    • Bertoncini, C.W.1    Rasia, R.M.2    Lamberto, G.R.3    Binolfi, A.4    Zweckstetter, M.5    Griesinger, C.6    Fernandez, C.O.7
  • 104
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T. S., Bax, A., Cole, N. B. and Nussbaum, R. L. (2005) Structure and dynamics of micelle-bound human alpha-synuclein.J Biol Chem. 280,9595-9603
    • (2005) J Biol Chem , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 105
    • 0026710554 scopus 로고
    • Protein structures in SDS micelle-protein complexes
    • Parker, W. and Song, P. S. (1992) Protein structures in SDS micelle-protein complexes.Biophys J. 61,1435-1439
    • (1992) Biophys J , vol.61 , pp. 1435-1439
    • Parker, W.1    Song, P.S.2
  • 106
    • 0038341134 scopus 로고    scopus 로고
    • A broken alpha -helix in folded alpha -Synuclein
    • Chandra, S., Chen, X., Rizo, J., Jahn, R. and Sudhof, T. C. (2003) A broken alpha -helix in folded alpha -Synuclein.J Biol Chem. 278,15313-15318
    • (2003) J Biol Chem , vol.278 , pp. 15313-15318
    • Chandra, S.1    Chen, X.2    Rizo, J.3    Jahn, R.4    Sudhof, T.C.5
  • 107
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling
    • Jao, C. C., Der-Sarkissian, A., Chen, J. and Langen, R. (2004) Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling.Proc Natl Acad Sci U S A. 101,8331-8336
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 108
    • 0033038220 scopus 로고    scopus 로고
    • Conformational flexibility in calcitonin: The dynamic properties of human and salmon calcitonin in solution
    • Amodeo, P., Motta, A., Strazzullo, G. and Castiglione Morelli, M. A. (1999) Conformational flexibility in calcitonin: the dynamic properties of human and salmon calcitonin in solution.J Biomol NMR. 13,161-174
    • (1999) J Biomol NMR , vol.13 , pp. 161-174
    • Amodeo, P.1    Motta, A.2    Strazzullo, G.3    Castiglione Morelli, M.A.4
  • 109
    • 33747790300 scopus 로고    scopus 로고
    • Folding of the repeat domain of tau upon binding to lipid surfaces
    • Barre, P. and Eliezer, D. (2006) Folding of the repeat domain of tau upon binding to lipid surfaces.J Mol Biol. 362,312-326
    • (2006) J Mol Biol , vol.362 , pp. 312-326
    • Barre, P.1    Eliezer, D.2
  • 110
    • 34547920308 scopus 로고    scopus 로고
    • Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes
    • Jarvet, J., Danielsson, J., Damberg, P., Oleszczuk, M. and Graslund, A. (2007) Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes.J Biomol NMR. 39,63-72
    • (2007) J Biomol NMR , vol.39 , pp. 63-72
    • Jarvet, J.1    Danielsson, J.2    Damberg, P.3    Oleszczuk, M.4    Graslund, A.5
  • 111
    • 0033555275 scopus 로고    scopus 로고
    • Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease
    • Shao, H., Jao, S., Ma, K. and Zagorski, M. G. (1999) Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease.J Mol Biol. 285,755-773
    • (1999) J Mol Biol , vol.285 , pp. 755-773
    • Shao, H.1    Jao, S.2    Ma, K.3    Zagorski, M.G.4
  • 112
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • Coles, M., Bicknell, W., Watson, A. A., Fairlie, D. P. and Craik, D. J. (1998) Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?Biochemistry. 37,11064-11077
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 113
    • 1242269212 scopus 로고    scopus 로고
    • Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with Abeta(1-40) peptide in a membrane mimic environment
    • Mandal, P. K. and Pettegrew, J. W. (2004) Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with Abeta(1-40) peptide in a membrane mimic environment.Neurochem Res. 29,447-453
    • (2004) Neurochem Res , vol.29 , pp. 447-453
    • Mandal, P.K.1    Pettegrew, J.W.2
  • 114
  • 115
    • 47749136312 scopus 로고    scopus 로고
    • Roles of beta-turns in protein folding: From peptide models to protein engineering
    • Marcelino, A. M. and Gierasch, L. M. (2008) Roles of beta-turns in protein folding: From peptide models to protein engineering.Biopolymers. 89,380-391
    • (2008) Biopolymers , vol.89 , pp. 380-391
    • Marcelino, A.M.1    Gierasch, L.M.2
  • 116
    • 30044450420 scopus 로고    scopus 로고
    • Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants
    • Ulmer, T. S. and Bax, A. (2005) Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.J Biol Chem. 280,43179-43187
    • (2005) J Biol Chem , vol.280 , pp. 43179-43187
    • Ulmer, T.S.1    Bax, A.2
  • 117
    • 28544452382 scopus 로고    scopus 로고
    • Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils.J MolBiol
    • Chen, Z., Krause, G. and Reif, B. (2005) Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils.J MolBiol.354,760-776
    • (2005) 354 , pp. 760-776
    • Chen, Z.1    Krause, G.2    Reif, B.3
  • 118
    • 0028966761 scopus 로고
    • Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR
    • Zhang, Y. Z., Paterson, Y. and Roder, H. (1995) Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.Protein Sci. 4,804-814
    • (1995) Protein Sci , vol.4 , pp. 804-814
    • Zhang, Y.Z.1    Paterson, Y.2    Roder, H.3
  • 119
    • 25844493112 scopus 로고    scopus 로고
    • Capturing intermediate structures of Alzheimer's betaamyloid, Abeta(1-40), by solid-state NMR spectroscopy
    • Chimon, S. and Ishii, Y. (2005) Capturing intermediate structures of Alzheimer's betaamyloid, Abeta(1-40), by solid-state NMR spectroscopy.J Am Chem Soc. 127,13472-13473
    • (2005) J am Chem Soc , vol.127 , pp. 13472-13473
    • Chimon, S.1    Ishii, Y.2
  • 121
    • 15544388942 scopus 로고    scopus 로고
    • Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy
    • Whittemore, N. A., Mishra, R., Kheterpal, I., Williams, A. D., Wetzel, R. and Serpersu, E. H. (2005) Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy.Biochemistry. 44,4434-4441
    • (2005) Biochemistry , vol.44 , pp. 4434-4441
    • Whittemore, N.A.1    Mishra, R.2    Kheterpal, I.3    Williams, A.D.4    Wetzel, R.5    Serpersu, E.H.6
  • 122
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions
    • Olofsson, A., Lindhagen-Persson, M., Sauer-Eriksson, A. E. and Ohman, A. (2007) Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions.Biochem J. 404, 63-70
    • (2007) Biochem J , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Ohman, A.4
  • 123
    • 33644851439 scopus 로고    scopus 로고
    • The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy
    • Olofsson, A., Sauer-Eriksson, A. E. and Ohman, A. (2006) The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy.J Biol Chem. 281,477-483
    • (2006) J Biol Chem , vol.281 , pp. 477-483
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Ohman, A.3
  • 124
  • 125
    • 1842786897 scopus 로고    scopus 로고
    • Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange
    • Yamaguchi, K., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H. and Goto, Y. (2004) Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange.J Mol Biol.338, 559-571
    • (2004) J Mol Biol , vol.338 , pp. 559-571
    • Yamaguchi, K.1    Katou, H.2    Hoshino, M.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 126
    • 1242316998 scopus 로고    scopus 로고
    • Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy
    • Olofsson, A., Ippel, J. H., Wijmenga, S. S., Lundgren, E. and Ohman, A. (2004) Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.J Biol Chem. 279,5699-5707
    • (2004) J Biol Chem , vol.279 , pp. 5699-5707
    • Olofsson, A.1    Ippel, J.H.2    Wijmenga, S.S.3    Lundgren, E.4    Ohman, A.5
  • 127
    • 33749838193 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry--a window into amyloid structure
    • Kheterpal, I. and Wetzel, R. (2006) Hydrogen/deuterium exchange mass spectrometry--a window into amyloid structure.Acc Chem Res. 39,584-593
    • (2006) Acc Chem Res , vol.39 , pp. 584-593
    • Kheterpal, I.1    Wetzel, R.2
  • 128
    • 11144221004 scopus 로고    scopus 로고
    • Amyloid accomplices and enforcers
    • Alexandrescu, A. T. (2005) Amyloid accomplices and enforcers.Protein Sci. 14,1-12
    • (2005) Protein Sci , vol.14 , pp. 1-12
    • Alexandrescu, A.T.1
  • 129
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L. and Englander, S. W. (1995) Protein folding intermediates: native-state hydrogen exchange.Science. 269,192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 130
    • 33749509894 scopus 로고    scopus 로고
    • Characterization of amyloid structures at the molecular level by solid state nuclear magnetic resonance spectroscopy
    • Tycko, R. (2006) Characterization of amyloid structures at the molecular level by solid state nuclear magnetic resonance spectroscopy.Methods Enzymol. 413,103-122
    • (2006) Methods Enzymol , vol.413 , pp. 103-122
    • Tycko, R.1
  • 131
    • 33845334180 scopus 로고    scopus 로고
    • 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR
    • Iwata, K., Fujiwara, T., Matsuki, Y., Akutsu, H., Takahashi, S., Naiki, H. and Goto, Y. (2006) 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR.Proc Natl Acad Sci U SA.103,18119-18124
    • (2006) Proc Natl Acad Sci U SA , vol.103 , pp. 18119-18124
    • Iwata, K.1    Fujiwara, T.2    Matsuki, Y.3    Akutsu, H.4    Takahashi, S.5    Naiki, H.6    Goto, Y.7
  • 133
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR
    • Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D. and Baldus, M. (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.Proc Natl Acad Sci U S A. 102,15871-15876
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Ronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 134
    • 33646878753 scopus 로고    scopus 로고
    • Preparation of alpha-synuclein fibrils for solid-state NMR: Expression, purification, and incubation of wild-type and mutant forms
    • Kloepper, K. D., Woods, W. S., Winter, K. A., George, J. M. and Rienstra, C. M. (2006) Preparation of alpha-synuclein fibrils for solid-state NMR: expression, purification, and incubation of wild-type and mutant forms.Protein Expr Purif 48,112-117
    • (2006) Protein Expr Purif , vol.48 , pp. 112-117
    • Kloepper, K.D.1    Woods, W.S.2    Winter, K.A.3    George, J.M.4    Rienstra, C.M.5
  • 135
    • 35448948612 scopus 로고    scopus 로고
    • Temperature-dependent sensitivity enhancement of solid-state NMR spectra of alpha-synuclein fibrils
    • Kloepper, K. D., Zhou, D. H., Li, Y., Winter, K. A., George, J. M. and Rienstra, C. M. (2007) Temperature-dependent sensitivity enhancement of solid-state NMR spectra of alpha-synuclein fibrils.JBiomol NMR. 39,197-211
    • (2007) Jbiomol NMR , vol.39 , pp. 197-211
    • Kloepper, K.D.1    Zhou, D.H.2    Li, Y.3    Winter, K.A.4    George, J.M.5    Rienstra, C.M.6
  • 136
    • 36949026380 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils
    • Kloepper, K. D., Hartman, K. L., Ladror, D. T. and Rienstra, C. M. (2007) Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils.JPhys Chem B. 111,13353-13356
    • (2007) Jphys Chem B , vol.111 , pp. 13353-13356
    • Kloepper, K.D.1    Hartman, K.L.2    Ladror, D.T.3    Rienstra, C.M.4
  • 137
    • 0029181728 scopus 로고
    • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S. and Sykes, B. D. (1995) 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects.J Biomol NMR. 5,67-81
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 138
    • 32344451179 scopus 로고    scopus 로고
    • The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: A step by step conformational analysis suggests the location of beta conformation seeding
    • Tomaselli, S., Esposito, V., Vangone, P., van Nuland, N. A., Bonvin, A. M., Guerrini, R., Tancredi, T., Temussi, P. A. and Picone, D. (2006) The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding.Chembiochem.7, 257-2673.
    • (2006) Chembiochem , vol.7 , pp. 257-2673
    • Tomaselli, S.1    Esposito, V.2    Vangone, P.3    Van Nuland, N.A.4    Bonvin, A.M.5    Guerrini, R.6    Tancredi, T.7    Temussi, P.A.8    Picone, D.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.