메뉴 건너뛰기




Volumn 438, Issue 7069, 2005, Pages 878-881

The importance of sequence diversity in the aggregation and evolution of proteins

Author keywords

[No Author keywords available]

Indexed keywords

DISEASES; IMMUNOLOGY; REACTION KINETICS;

EID: 28644437048     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04195     Document Type: Article
Times cited : (280)

References (30)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. Folding proteins in fatal ways. Nature 426, 900-904 (2003).
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 3
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic, G., Gough, J. & Teichmann, S. A. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J. Mol. Biol. 310, 311-325 (2001).
    • (2001) J. Mol. Biol. , vol.310 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.A.3
  • 4
    • 0034602176 scopus 로고    scopus 로고
    • Parkinson's disease-associated α-synuclein is more fibrillogenic than β- and γ-synuclein and cannot cross-seed its homologs
    • Biere, A. L. et al. Parkinson's disease-associated α-synuclein is more fibrillogenic than β- and γ-synuclein and cannot cross-seed its homologs. J. Biol. Chem. 275, 34574-34579 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34574-34579
    • Biere, A.L.1
  • 5
  • 6
    • 0032878322 scopus 로고    scopus 로고
    • Formation of short-lived protein aggregates directly from the coil in two-state folding
    • Silow, M., Tan, Y.-J., Fersht, A. R. & Oliveberg, M. Formation of short-lived protein aggregates directly from the coil in two-state folding. Biochemistry 38, 13006-13012 (1999).
    • (1999) Biochemistry , vol.38 , pp. 13006-13012
    • Silow, M.1    Tan, Y.-J.2    Fersht, A.R.3    Oliveberg, M.4
  • 7
    • 0025329555 scopus 로고
    • A regular pattern of two types of 100-residue motif in the sequence of titin
    • Labeit, S. et al. A regular pattern of two types of 100-residue motif in the sequence of titin. Nature 345, 273-276 (1990).
    • (1990) Nature , vol.345 , pp. 273-276
    • Labeit, S.1
  • 8
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band Ig domain region as an entropic spring
    • Linke, W. A., Stockmeier, M. R., Ivemeyer, M., Hosser, H. & Mundel, P. Characterizing titin's I-band Ig domain region as an entropic spring. J. Cell Sci. 111, 1567-1574 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 1567-1574
    • Linke, W.A.1    Stockmeier, M.R.2    Ivemeyer, M.3    Hosser, H.4    Mundel, P.5
  • 9
    • 0033020141 scopus 로고    scopus 로고
    • Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains
    • Raffen, R. et al. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci. 8, 509-517 (1999).
    • (1999) Protein Sci. , vol.8 , pp. 509-517
    • Raffen, R.1
  • 10
    • 0034254241 scopus 로고    scopus 로고
    • 2-microglobulin and amyloid formation in vitro
    • 2- microglobulin and amyloid formation in vitro. Biochemistry 39, 8735-8746 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8735-8746
    • McParland, V.J.1
  • 12
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • Chiti, F. et al. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA 96, 3590-3594 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3590-3594
    • Chiti, F.1
  • 13
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M. et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273, 729-739 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 729-739
    • Sunde, M.1
  • 15
    • 0036707999 scopus 로고    scopus 로고
    • Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
    • Steward, A., Toca-Herrera, J. L. & Clarke, J. Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy. Protein Sci. 11, 2179-2183 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2179-2183
    • Steward, A.1    Toca-Herrera, J.L.2    Clarke, J.3
  • 16
    • 0036304229 scopus 로고    scopus 로고
    • Titin: A multidomain protein that behaves as the sum of its parts
    • Scott, K. A., Steward, A., Fowler, S. B. & Clarke, J. Titin: a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315, 819-829 (2002).
    • (2002) J. Mol. Biol. , vol.315 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 17
    • 0041822089 scopus 로고    scopus 로고
    • Join the crowd
    • Ellis, R. J. & Minton, A. P. Join the crowd. Nature 425, 27-28 (2003).
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 18
    • 0035961291 scopus 로고    scopus 로고
    • Pathogenesis, diagnosis and treatment of systemic amyloidosis
    • Pepys, M. B. Pathogenesis, diagnosis and treatment of systemic amyloidosis. Phil. Trans. R. Soc. Lond. B 356, 203-211 (2001).
    • (2001) Phil. Trans. R. Soc. Lond. B , vol.356 , pp. 203-211
    • Pepys, M.B.1
  • 19
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan, R. S., Illing, M. E., Bence, N. F. & Kopito, R. Specificity in intracellular protein aggregation and inclusion body formation. Proc. Natl Acad. Sci. USA 98, 13060-13065 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.4
  • 20
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • Nelson, R. et al. Structure of the cross-β spine of amyloid-like fibrils. Nature 435, 773-778 (2005).
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1
  • 21
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec, C. P. et al. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc. Natl Acad. Sci. USA 101, 711-716 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1
  • 22
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan, R. & Lindquist, S. L. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772 (2005).
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 23
    • 0034730203 scopus 로고    scopus 로고
    • Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
    • Otzen, D. E., Kristensen, O. & Oliveberg, M. Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. Proc. Natl Acad. Sci. USA 97, 9907-9912 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9907-9912
    • Otzen, D.E.1    Kristensen, O.2    Oliveberg, M.3
  • 24
    • 0037053429 scopus 로고    scopus 로고
    • Sequence conservation in Ig-like domains: The role of highly conserved proline residues in the fibronectin type III superfamily
    • Steward, A., Adhya, S. & Clarke, J. Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. J. Mol. Biol. 318, 935-940 (2002).
    • (2002) J. Mol. Biol. , vol.318 , pp. 935-940
    • Steward, A.1    Adhya, S.2    Clarke, J.3
  • 25
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J. S. & Richardson, D. C. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl Acad. Sci. USA 99, 2754-2759 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 26
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer, W. J. & Hartl, F. U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388, 343-349 (1997).
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 28
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899 (2003).
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 29
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford, S. L. & Lindquist, S. Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342 (1998).
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 30
    • 0036087169 scopus 로고    scopus 로고
    • SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments
    • Gough, J. & Chothia, C. SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments. Nucleic Acids Res. 30, 268-272 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 268-272
    • Gough, J.1    Chothia, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.