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Volumn 18, Issue 6, 2008, Pages 756-764

Function and structure of inherently disordered proteins

Author keywords

[No Author keywords available]

Indexed keywords

NEUROLIGIN; SYNUCLEIN;

EID: 57049095821     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.10.002     Document Type: Review
Times cited : (848)

References (71)
  • 1
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity - linking function and disorder
    • Dunker A.K., and Obradovic Z. The protein trinity - linking function and disorder. Nat Biotechnol 19 (2001) 805-806
    • (2001) Nat Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 3
    • 44949262123 scopus 로고    scopus 로고
    • Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins
    • ••], this paper used theoretical predictions and experiments to test the prediction that highly polar, uncharged sequences collapse despite their lack of hydrophobic residues. This collapse occurs for a variety of polar uncharged sequences and even for the backbone alone. Thus, it is likely to be a general result that arises because water is such a poor solvent for both the backbone and certain polar polypeptide chains.
    • ••], this paper used theoretical predictions and experiments to test the prediction that highly polar, uncharged sequences collapse despite their lack of hydrophobic residues. This collapse occurs for a variety of polar uncharged sequences and even for the backbone alone. Thus, it is likely to be a general result that arises because water is such a poor solvent for both the backbone and certain polar polypeptide chains.
    • (2008) J Am Chem Soc , vol.130 , pp. 7380-7392
    • Tran, H.T.1    Mao, A.2    Pappu, R.V.3
  • 4
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?
    • Uversky V.N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?. Cell Mol Life Sci 60 (2003) 1852-1871
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 6
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins 41 (2000) 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 8
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • Ishida T., and Kinoshita K. Prediction of disordered regions in proteins based on the meta approach. Bioinformatics 24 (2008) 1344-1348
    • (2008) Bioinformatics , vol.24 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 9
    • 49649123303 scopus 로고    scopus 로고
    • Prediction of protein disorder
    • Dosztanyi Z., and Tompa P. Prediction of protein disorder. Methods Mol Biol 426 (2008) 103-115
    • (2008) Methods Mol Biol , vol.426 , pp. 103-115
    • Dosztanyi, Z.1    Tompa, P.2
  • 10
    • 36749081458 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP7
    • The CASP assessment papers are worth reading. Various researchers claim that one predictor or another (usually their own) is better than the others. The CASP exercises are evaluations based on blind predictions, and the evaluations are by third parties, so the comparisons are less biased. However, the CASP exercises involve only a small number of proteins, so claims to have developed 'the best predictor' should not be made on their basis either.
    • Bordoli L., Kiefer F., and Schwede T. Assessment of disorder predictions in CASP7. Proteins 69 Suppl 8 (2007) 129-136. The CASP assessment papers are worth reading. Various researchers claim that one predictor or another (usually their own) is better than the others. The CASP exercises are evaluations based on blind predictions, and the evaluations are by third parties, so the comparisons are less biased. However, the CASP exercises involve only a small number of proteins, so claims to have developed 'the best predictor' should not be made on their basis either.
    • (2007) Proteins , vol.69 , Issue.SUPPL. 8 , pp. 129-136
    • Bordoli, L.1    Kiefer, F.2    Schwede, T.3
  • 12
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337 (2004) 635-645
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 13
    • 39049185694 scopus 로고    scopus 로고
    • Packing regularities in biological structures relate to their dynamics
    • Jernigan R.L., and Kloczkowski A. Packing regularities in biological structures relate to their dynamics. Methods Mol Biol 350 (2007) 251-276
    • (2007) Methods Mol Biol , vol.350 , pp. 251-276
    • Jernigan, R.L.1    Kloczkowski, A.2
  • 14
    • 34047204789 scopus 로고    scopus 로고
    • Proportion of solvent-exposed amino acids in a protein and rate of protein evolution
    • Lin Y.S., Hsu W.L., Hwang J.K., and Li W.H. Proportion of solvent-exposed amino acids in a protein and rate of protein evolution. Mol Biol Evol 24 (2007) 1005-1011
    • (2007) Mol Biol Evol , vol.24 , pp. 1005-1011
    • Lin, Y.S.1    Hsu, W.L.2    Hwang, J.K.3    Li, W.H.4
  • 16
    • 35248852356 scopus 로고    scopus 로고
    • Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation
    • This paper reminds us that not all functions associated with disorder involve binding to a partner, and shows that features likely to be of functional importance, such as length and flexibility, can be conserved in the face of lack of amino acid sequence conservation.
    • Daughdrill G.W., Narayanaswami P., Gilmore S.H., Belczyk A., and Brown C.J. Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. J Mol Evol 65 (2007) 277-288. This paper reminds us that not all functions associated with disorder involve binding to a partner, and shows that features likely to be of functional importance, such as length and flexibility, can be conserved in the face of lack of amino acid sequence conservation.
    • (2007) J Mol Evol , vol.65 , pp. 277-288
    • Daughdrill, G.W.1    Narayanaswami, P.2    Gilmore, S.H.3    Belczyk, A.4    Brown, C.J.5
  • 17
    • 28644432411 scopus 로고    scopus 로고
    • Unwinding the helical linker of calcium-loaded calmodulin: a molecular dynamics study
    • Fiorin G., Biekofsky R.R., Pastore A., and Carloni P. Unwinding the helical linker of calcium-loaded calmodulin: a molecular dynamics study. Proteins 61 (2005) 829-839
    • (2005) Proteins , vol.61 , pp. 829-839
    • Fiorin, G.1    Biekofsky, R.R.2    Pastore, A.3    Carloni, P.4
  • 19
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6 (2005) 197-208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 21
    • 38549110665 scopus 로고    scopus 로고
    • Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data
    • This paper shows the power of Raman optical activity to distinguish between intrinsically unfolded sequences and sequences that fold into structures that are often difficult to differentiate from them, such as the polyproline-II fold.
    • Zhu F., Kapitan J., Tranter G.E., Pudney P.D., Isaacs N.W., Hecht L., and Barron L.D. Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data. Proteins 70 (2008) 823-833. This paper shows the power of Raman optical activity to distinguish between intrinsically unfolded sequences and sequences that fold into structures that are often difficult to differentiate from them, such as the polyproline-II fold.
    • (2008) Proteins , vol.70 , pp. 823-833
    • Zhu, F.1    Kapitan, J.2    Tranter, G.E.3    Pudney, P.D.4    Isaacs, N.W.5    Hecht, L.6    Barron, L.D.7
  • 22
    • 0242362184 scopus 로고    scopus 로고
    • The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded
    • Zeev-Ben-Mordehai T., Rydberg E.H., Solomon A., Toker L., Botti S., Auld V.J., Silman I., and Sussman J.L. The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. Proteins 53 (2003) 758-767
    • (2003) Proteins , vol.53 , pp. 758-767
    • Zeev-Ben-Mordehai, T.1    Rydberg, E.H.2    Solomon, A.3    Toker, L.4    Botti, S.5    Auld, V.J.6    Silman, I.7    Sussman, J.L.8
  • 25
    • 17644422781 scopus 로고    scopus 로고
    • Urea promotes polyproline II helix formation: implications for protein denatured states
    • Whittington S.J., Chellgren B.W., Hermann V.M., and Creamer T.P. Urea promotes polyproline II helix formation: implications for protein denatured states. Biochemistry 44 (2005) 6269-6275
    • (2005) Biochemistry , vol.44 , pp. 6269-6275
    • Whittington, S.J.1    Chellgren, B.W.2    Hermann, V.M.3    Creamer, T.P.4
  • 27
    • 41149125082 scopus 로고    scopus 로고
    • Structural disorder serves as a weak signal for intracellular protein degradation
    • These results were a big surprise; most expected unfolded proteins to be degraded faster than structured proteins. Intracellular protein lifetimes vary over at least 12 orders of magnitude. Evidently a number of factors, including protein disorder, contribute to intracellular protein lifetimes.
    • Tompa P., Prilusky J., Silman I., and Sussman J.L. Structural disorder serves as a weak signal for intracellular protein degradation. Proteins 71 (2008) 903-909. These results were a big surprise; most expected unfolded proteins to be degraded faster than structured proteins. Intracellular protein lifetimes vary over at least 12 orders of magnitude. Evidently a number of factors, including protein disorder, contribute to intracellular protein lifetimes.
    • (2008) Proteins , vol.71 , pp. 903-909
    • Tompa, P.1    Prilusky, J.2    Silman, I.3    Sussman, J.L.4
  • 28
    • 39749117978 scopus 로고    scopus 로고
    • Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome
    • This paper gives a good operational definition, in solution, of intrinsically unstructured proteins, and provides a basis for distinguishing them, in situ, from MGs and from folded proteins.
    • Tsvetkov P., Asher G., Paz A., Reuven N., Sussman J.L., Silman I., and Shaul Y. Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome. Proteins 70 (2008) 1357-1366. This paper gives a good operational definition, in solution, of intrinsically unstructured proteins, and provides a basis for distinguishing them, in situ, from MGs and from folded proteins.
    • (2008) Proteins , vol.70 , pp. 1357-1366
    • Tsvetkov, P.1    Asher, G.2    Paz, A.3    Reuven, N.4    Sussman, J.L.5    Silman, I.6    Shaul, Y.7
  • 29
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • Xie H., Vucetic S., Iakoucheva L.M., Oldfield C.J., Dunker A.K., Uversky V.N., and Obradovic Z. Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J Proteome Res 6 (2007) 1882-1898
    • (2007) J Proteome Res , vol.6 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Uversky, V.N.6    Obradovic, Z.7
  • 30
    • 34249282661 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions
    • Vucetic S., Xie H., Iakoucheva L.M., Oldfield C.J., Dunker A.K., Obradovic Z., and Uversky V.N. Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions. J Proteome Res 6 (2007) 1899-1916
    • (2007) J Proteome Res , vol.6 , pp. 1899-1916
    • Vucetic, S.1    Xie, H.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 31
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins
    • Xie H., Vucetic S., Iakoucheva L.M., Oldfield C.J., Dunker A.K., Obradovic Z., and Uversky V.N. Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J Proteome Res 6 (2007) 1917-1932
    • (2007) J Proteome Res , vol.6 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 32
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579 (2005) 3346-3354
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 34
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker A.K., Cortese M.S., Romero P., Iakoucheva L.M., and Uversky V.N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272 (2005) 5129-5148
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 35
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield C.J., Meng J., Yang J.Y., Yang M.Q., Uversky V.N., and Dunker A.K. Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics 9 Suppl 1 (2008) S1
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 36
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A., and Nakamura H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett 580 (2006) 2041-2045
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 38
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Dosztanyi Z., Chen J., Dunker A.K., Simon I., and Tompa P. Disorder and sequence repeats in hub proteins and their implications for network evolution. J Proteome Res 5 (2006) 2985-2995
    • (2006) J Proteome Res , vol.5 , pp. 2985-2995
    • Dosztanyi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 39
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • Ekman D., Light S., Bjorklund A.K., and Elofsson A. What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?. Genome Biol 7 (2006) R45
    • (2006) Genome Biol , vol.7
    • Ekman, D.1    Light, S.2    Bjorklund, A.K.3    Elofsson, A.4
  • 40
    • 30144437939 scopus 로고    scopus 로고
    • Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes
    • Singh G.P., Ganapathi M., Sandhu K.S., and Dash D. Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes. Proteins 62 (2006) 309-315
    • (2006) Proteins , vol.62 , pp. 309-315
    • Singh, G.P.1    Ganapathi, M.2    Sandhu, K.S.3    Dash, D.4
  • 43
    • 41149120313 scopus 로고    scopus 로고
    • SLiMFinder: a probabilistic method for identifying over-represented, convergently evolved, short linear motifs in proteins
    • Edwards R.J., Davey N.E., and Shields D.C. SLiMFinder: a probabilistic method for identifying over-represented, convergently evolved, short linear motifs in proteins. PLoS ONE 2 (2007) e967
    • (2007) PLoS ONE , vol.2
    • Edwards, R.J.1    Davey, N.E.2    Shields, D.C.3
  • 44
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • Oldfield C.J., Cheng Y., Cortese M.S., Romero P., Uversky V.N., and Dunker A.K. Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44 (2005) 12454-12470
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 45
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Disordered regions commonly contain localized regions that bind to specific partners. This paper shows that different bioinformatics methods for identifying binding sites often point to the same or overlapping localized regions despite the large differences in the methods used.
    • Fuxreiter M., Tompa P., and Simon I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23 (2007) 950-956. Disordered regions commonly contain localized regions that bind to specific partners. This paper shows that different bioinformatics methods for identifying binding sites often point to the same or overlapping localized regions despite the large differences in the methods used.
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 46
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • Cheng Y., Oldfield C.J., Meng J., Romero P., Uversky V.N., and Dunker A.K. Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry 46 (2007) 13468-13477
    • (2007) Biochemistry , vol.46 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 47
    • 52249101769 scopus 로고    scopus 로고
    • Short linear motifs recognized by SH2, SH3 and S/T kinase domains are conserved in disordered protein regions
    • Ren S., Uversky V.N., Chen Z., Dunker A.K., and Obradovic Z. Short linear motifs recognized by SH2, SH3 and S/T kinase domains are conserved in disordered protein regions. BMC Genomics 9 (2008) S26
    • (2008) BMC Genomics , vol.9
    • Ren, S.1    Uversky, V.N.2    Chen, Z.3    Dunker, A.K.4    Obradovic, Z.5
  • 49
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger A.C., and Fersht A.R. Structural biology of the tumor suppressor p53. Annu Rev Biochem 77 (2008) 557-582
    • (2008) Annu Rev Biochem , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 51
    • 84943232112 scopus 로고    scopus 로고
    • Signaling to the p53 tumor suppressor through pathways activated by genotoxic and nongenotoxic stress
    • Bradshaw R.A., and Dennis E.A. (Eds), Academic Press
    • Anderson C.W., and Appella E. Signaling to the p53 tumor suppressor through pathways activated by genotoxic and nongenotoxic stress. In: Bradshaw R.A., and Dennis E.A. (Eds). Handbook of Cell Signaling (2003), Academic Press 237-247
    • (2003) Handbook of Cell Signaling , pp. 237-247
    • Anderson, C.W.1    Appella, E.2
  • 52
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: introducing the D2 concept
    • Uversky V.N., Oldfield C.J., and Dunker A.K. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Bipohys Biomol Struct 37 (2008) 215-246
    • (2008) Annu Rev Bipohys Biomol Struct , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 53
    • 45449091418 scopus 로고    scopus 로고
    • Amyloidogenesis of natively unfolded proteins
    • Uversky V.N. Amyloidogenesis of natively unfolded proteins. Curr Alzheimer Res 5 (2008) 260-287
    • (2008) Curr Alzheimer Res , vol.5 , pp. 260-287
    • Uversky, V.N.1
  • 54
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • This is a critical review of the evidence that amyloid peptides cause disease by a mechanism involving pore formation.
    • Lashuel H.A., and Lansbury Jr. P.T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?. Quart Rev Biophys 39 (2006) 167-201. This is a critical review of the evidence that amyloid peptides cause disease by a mechanism involving pore formation.
    • (2006) Quart Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2
  • 55
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment
    • Terry R.D., Masliah E., Salmon D.P., Butters N., DeTeresa R., Hill R., Hansen L.A., and Katzman R. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann Neurol 30 (1991) 572-580
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 56
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes
    • Arispe N., Pollard H.B., and Rojas E. Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes. Proc Natl Acad Sci U S A 90 (1993) 10573-10577
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 57
    • 0033600590 scopus 로고    scopus 로고
    • 2+-sensitive channel in reconstituted lipid vesicles
    • 2+-sensitive channel in reconstituted lipid vesicles. Biochemistry 38 (1999) 11189-11196
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3
  • 58
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: a common structural link for protein-misfolding disease
    • In this study atomic force microscopy is used to show that several amyloid peptides form ion-channel-like structures in reconstituted membranes.
    • Quist A., Doudevski I., Lin H., Azimova R., Ng D., Frangione B., Kagan B., Ghiso J., and Lal R. Amyloid ion channels: a common structural link for protein-misfolding disease. Proc Natl Acad Sci U S A 102 (2005) 10427-10432. In this study atomic force microscopy is used to show that several amyloid peptides form ion-channel-like structures in reconstituted membranes.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lin, H.3    Azimova, R.4    Ng, D.5    Frangione, B.6    Kagan, B.7    Ghiso, J.8    Lal, R.9
  • 59
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins
    • Uversky V.N., Li J., Souillac P., Millett I.S., Doniach S., Jakes R., Goedert M., and Fink A.L. Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins. J Biol Chem 277 (2002) 11970-11978
    • (2002) J Biol Chem , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6    Goedert, M.7    Fink, A.L.8
  • 60
    • 0035109738 scopus 로고    scopus 로고
    • Synucleinopathies: clinical and pathological implications
    • Galvin J.E., Lee V.M., and Trojanowski J.Q. Synucleinopathies: clinical and pathological implications. Arch Neurol 58 (2001) 186-190
    • (2001) Arch Neurol , vol.58 , pp. 186-190
    • Galvin, J.E.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 61
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation
    • Uversky V.N. Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation. J Neurochem 103 (2007) 17-37
    • (2007) J Neurochem , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 62
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky V.N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J Biomol Struct Dyn 21 (2003) 211-234
    • (2003) J Biomol Struct Dyn , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 63
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell L.C., Berriman J., Jakes R., Goedert M., and Crowther R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc Natl Acad Sci U S A 97 (2000) 4897-4902
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 64
    • 34948829554 scopus 로고    scopus 로고
    • Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein
    • Kim H.Y., Heise H., Fernandez C.O., Baldus M., and Zweckstetter M. Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein. Chembiochem 8 (2007) 1671-1674
    • (2007) Chembiochem , vol.8 , pp. 1671-1674
    • Kim, H.Y.1    Heise, H.2    Fernandez, C.O.3    Baldus, M.4    Zweckstetter, M.5
  • 66
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem 273 (1998) 9443-9449
    • (1998) J Biol Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 67
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits alpha-synuclein fibril formation
    • Zhu M., and Fink A.L. Lipid binding inhibits alpha-synuclein fibril formation. J Biol Chem 278 (2003) 16873-16877
    • (2003) J Biol Chem , vol.278 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2
  • 68
    • 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. Structure and dynamics of micelle-bound human alpha-synuclein. J Biol Chem 280 (2005) 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
  • 69
    • 37249003742 scopus 로고    scopus 로고
    • Helical alpha-synuclein forms highly conductive ion channels
    • A combined biophysical and electrophysiological study showing that on phospholipid surfaces αSN adopts an α-helical conformation which produces ion channels.
    • Zakharov S.D., Hulleman J.D., Dutseva E.A., Antonenko Y.N., Rochet J.C., and Cramer W.A. Helical alpha-synuclein forms highly conductive ion channels. Biochemistry 46 (2007) 14369-14379. A combined biophysical and electrophysiological study showing that on phospholipid surfaces αSN adopts an α-helical conformation which produces ion channels.
    • (2007) Biochemistry , vol.46 , pp. 14369-14379
    • Zakharov, S.D.1    Hulleman, J.D.2    Dutseva, E.A.3    Antonenko, Y.N.4    Rochet, J.C.5    Cramer, W.A.6
  • 70
    • 33947210032 scopus 로고    scopus 로고
    • Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein
    • A theoretical and experimental study providing evidence that αSN associates to form ring-like α-helical oligomers on the surfaces of phospholipid membranes that produce ion channels, and that the association of αSN with βSN inhibits the process.
    • Tsigelny I.F., Bar-On P., Sharikov Y., Crews L., Hashimoto M., Miller M.A., Keller S.H., Platoshyn O., Yuan J.X., and Masliah E. Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein. FEBS J 274 (2007) 1862-1877. A theoretical and experimental study providing evidence that αSN associates to form ring-like α-helical oligomers on the surfaces of phospholipid membranes that produce ion channels, and that the association of αSN with βSN inhibits the process.
    • (2007) FEBS J , vol.274 , pp. 1862-1877
    • Tsigelny, I.F.1    Bar-On, P.2    Sharikov, Y.3    Crews, L.4    Hashimoto, M.5    Miller, M.A.6    Keller, S.H.7    Platoshyn, O.8    Yuan, J.X.9    Masliah, E.10
  • 71
    • 9944244038 scopus 로고    scopus 로고
    • An antiaggregation gene therapy strategy for Lewy body disease utilizing beta-synuclein lentivirus in a transgenic model
    • Hashimoto M., Rockenstein E., Mante M., Crews L., Bar-On P., Gage F.H., Marr R., and Masliah E. An antiaggregation gene therapy strategy for Lewy body disease utilizing beta-synuclein lentivirus in a transgenic model. Gene Ther 11 (2004) 1713-1723
    • (2004) Gene Ther , vol.11 , pp. 1713-1723
    • Hashimoto, M.1    Rockenstein, E.2    Mante, M.3    Crews, L.4    Bar-On, P.5    Gage, F.H.6    Marr, R.7    Masliah, E.8


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