메뉴 건너뛰기




Volumn 2, Issue 80, 2009, Pages

Functional amyloids signal their arrival

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PEPTIDE HORMONE;

EID: 70349575077     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.280pe43     Document Type: Short Survey
Times cited : (52)

References (37)
  • 1
    • 43549085062 scopus 로고    scopus 로고
    • We find them here, we find them there: Functional bacterial amyloid
    • D. Otzen, P. H. Nielsen, We find them here, we find them there: Functional bacterial amyloid. Cell. Mol. Life Sci. 65, 910-927 (2008).
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 910-927
    • Otzen, D.1    Nielsen, P.H.2
  • 2
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • J. D. Sipe, A. S. Cohen, Review: History of the amyloid fibril. J. Struct. Biol. 130, 88-98 (2000).
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 3
    • 0037038813 scopus 로고    scopus 로고
    • Amyloidosis and Alzheimer's disease
    • J. Ghiso, B. Frangione, Amyloidosis and Alzheimer's disease. Adv. Drug Deliv. Rev. 54, 1539-1551 (2002).
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 1539-1551
    • Ghiso, J.1    Frangione, B.2
  • 5
    • 48149108245 scopus 로고    scopus 로고
    • Protein aggregation in the brain: The molecular basis for Alzheimer's and Parkinson's diseases
    • G. B. Irvine, O. M. El-Agnaf, G. M. Shankar, D. M. Walsh, Protein aggregation in the brain: The molecular basis for Alzheimer's and Parkinson's diseases. Mol. Med. 14, 451-464 (2008).
    • (2008) Mol. Med. , vol.14 , pp. 451-464
    • Irvine, G.B.1    El-Agnaf, O.M.2    Shankar, G.M.3    Walsh, D.M.4
  • 8
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • H. L. True, S. L. Lindquist, A yeast prion provides a mechanism for genetic variation and phenotypic diversity.Nature 407, 477-483 (2000).
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 12
    • 0031977366 scopus 로고    scopus 로고
    • Isolation of an Escherichia coli K-12 mutant strain able to form biofilms on inert surfaces: Involvement of a new ompR allele that increases curli expression
    • O. Vidal, R. Longin, C. Prigent-Combaret, C. Dorel, M. Hooreman, P. Lejeune, Isolation of an Escherichia coli K-12 mutant strain able to form biofilms on inert surfaces: Involvement of a new ompR allele that increases curli expression. J. Bacteriol. 180, 2442-2449 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 2442-2449
    • Vidal, O.1    Longin, R.2    Prigent-Combaret, C.3    Dorel, C.4    Hooreman, M.5    Lejeune, P.6
  • 13
    • 0034006823 scopus 로고    scopus 로고
    • Expression of and cytokine activation by Escherichia coli curli fibers in human sepsis
    • Z. Bian, A. Brauner, Y. Li, S. Normark, Expression of and cytokine activation by Escherichia coli curli fibers in human sepsis. J. Infect. Dis. 181, 602-612 (2000).
    • (2000) J. Infect. Dis. , vol.181 , pp. 602-612
    • Bian, Z.1    Brauner, A.2    Li, Y.3    Normark, S.4
  • 15
    • 52049111387 scopus 로고    scopus 로고
    • The molecular basis of functional bacterial amyloid polymerization and nucleation
    • X. Wang, N. D. Hammer, M. R. Chapman, The molecular basis of functional bacterial amyloid polymerization and nucleation. J. Biol. Chem. 283, 21530-21539 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21530-21539
    • Wang, X.1    Hammer, N.D.2    Chapman, M.R.3
  • 16
    • 0141838884 scopus 로고    scopus 로고
    • Aerial morphogenesis: Enter the chaplins
    • N. J. Talbot, Aerial morphogenesis: Enter the chaplins. Curr. Biol. 13, R696-R698 (2003).
    • (2003) Curr. Biol. , vol.13
    • Talbot, N.J.1
  • 17
    • 0038681008 scopus 로고    scopus 로고
    • The chaplins: A family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor
    • M. A. Elliot, N. Karoonuthaisiri, J. Huang, M. J. Bibb, S. N. Cohen, C. M. Kao, M. J. Buttner, The chaplins: A family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor. Genes Dev. 17, 1727-1740 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1727-1740
    • Elliot, M.A.1    Karoonuthaisiri, N.2    Huang, J.3    Bibb, M.J.4    Cohen, S.N.5    Kao, C.M.6    Buttner, M.J.7
  • 19
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • S. Alberti, R. Halfmann, O. King, A. Kapila, S. Lindquist, A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137, 146-158 (2009).
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 21
    • 0033062601 scopus 로고    scopus 로고
    • Protein hormone storage in secretory granules: Mechanisms for concentration and sorting
    • P. S. Dannies, Protein hormone storage in secretory granules: Mechanisms for concentration and sorting. Endocr. Rev. 20, 3-21 (1999).
    • (1999) Endocr. Rev. , vol.20 , pp. 3-21
    • Dannies, P.S.1
  • 22
    • 3042704069 scopus 로고    scopus 로고
    • Is there structural specificity in the reversible protein aggregates that are stored in secretory granules?
    • C. Keeler, M. E. Hodsdon, P. S. Dannies, Is there structural specificity in the reversible protein aggregates that are stored in secretory granules? J. Mol. Neurosci. 22, 43-49 (2004).
    • (2004) J. Mol. Neurosci. , vol.22 , pp. 43-49
    • Keeler, C.1    Hodsdon, M.E.2    Dannies, P.S.3
  • 25
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • D. J. Selkoe, Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases.Nat. Cell Biol. 6, 1054-1061 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 27
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • C. Korth, B. C. May, F. E. Cohen, S. B. Prusiner, Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. U.S.A. 98, 9836-9841 (2001).
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.C.2    Cohen, F.E.3    Prusiner, S.B.4
  • 28
    • 0020684553 scopus 로고
    • Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells
    • H. P. Moore, B. Gumbiner, R. B. Kelly, Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells. Nature 302, 434-436 (1983).
    • (1983) Nature , vol.302 , pp. 434-436
    • Moore, H.P.1    Gumbiner, B.2    Kelly, R.B.3
  • 30
    • 45249090641 scopus 로고    scopus 로고
    • Polymerizing the fibre between bacteria and host cells: The biogenesis of functional amyloid fibres
    • E. A. Epstein, M. R. Chapman, Polymerizing the fibre between bacteria and host cells: The biogenesis of functional amyloid fibres. Cell. Microbiol. 10, 1413-1420 (2008).
    • (2008) Cell. Microbiol. , vol.10 , pp. 1413-1420
    • Epstein, E.A.1    Chapman, M.R.2
  • 32
    • 0038004458 scopus 로고    scopus 로고
    • A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils
    • D. Claessen, R. Rink, W. de Jong, J. Siebring, P. de Vreugd, F. G. Boersma, L. Dijkhuizen, H. A. Wosten, A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev. 17, 1714-1726 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1714-1726
    • Claessen, D.1    Rink, R.2    De Jong, W.3    Siebring, J.4    De Vreugd, P.5    Boersma, F.G.6    Dijkhuizen, L.7    Wosten, H.A.8
  • 33
    • 34250305540 scopus 로고    scopus 로고
    • Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria
    • J. Oh, J. G. Kim, E. Jeon, C. H.Yoo, J. S. Moon, S. Rhee, I. Hwang, Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria. J. Biol. Chem. 282, 13601-13609 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 13601-13609
    • Oh, J.1    Kim, J.G.2    Jeon, E.3    Yoo, C.H.4    Moon, J.S.5    Rhee, S.6    Hwang, I.7
  • 35
    • 0343664397 scopus 로고    scopus 로고
    • Hydrophobins, the fungal coat unraveled
    • H. A. Wosten, M. L. de Vocht, Hydrophobins, the fungal coat unravelled. Biochim. Biophys. Acta 1469, 79-86 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 79-86
    • Wosten, H.A.1    De Vocht, M.L.2
  • 36
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • V. Coustou, C. Deleu, S. Saupe, J. Begueret, The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. U.S.A. 94, 9773-9778 (1997).
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 37
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • K. Si, S. Lindquist, E. R. Kandel, A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 115, 879-891 (2003).
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.