메뉴 건너뛰기




Volumn 265, Issue 3, 2009, Pages 329-334

The emerging concept of functional amyloid

Author keywords

sheet aggregates; Amyloidosis; Functional amyloid; Prions; Protein conformation; Protein based inheritance

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CHAPLIN; CSGA PROTEIN; CSGB PROTEIN; CURLI PROTEIN; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; MELANIN; POLYAMINE; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 60349097590     PISSN: 09546820     EISSN: 13652796     Source Type: Journal    
DOI: 10.1111/j.1365-2796.2008.02068.x     Document Type: Review
Times cited : (100)

References (45)
  • 1
    • 1242317785 scopus 로고    scopus 로고
    • The systemic amyloidoses: Clearer understanding of the molecular mechanisms offers hope for more effective therapies
    • Merlini G, Westermark P. The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies. J Intern Med 2004 255 : 159 78.
    • (2004) J Intern Med , vol.255 , pp. 159-78
    • Merlini, G.1    Westermark, P.2
  • 2
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • Pepys MB. Amyloidosis. Annu Rev Med 2006 57 : 223 41.
    • (2006) Annu Rev Med , vol.57 , pp. 223-41
    • Pepys, M.B.1
  • 3
    • 0842281551 scopus 로고    scopus 로고
    • Principles on protein folding, misfolding and aggregation
    • Dobson CM. Principles on protein folding, misfolding and aggregation. Semin Cell Dev Biol 2004 15 : 3 16.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloiod and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloiod and human disease. Annu Rev Biochemistry 2006 75 : 333 66.
    • (2006) Annu Rev Biochemistry , vol.75 , pp. 333-66
    • Chiti, F.1    Dobson, C.M.2
  • 5
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B. Molecular chaperones and protein quality control. Cell 2006 125 : 443 51.
    • (2006) Cell , vol.125 , pp. 443-51
    • Bukau, B.1
  • 6
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBPP bound to the transactivation domain of CREB: A model foractivator:coactivator interactions
    • Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE. Solution structure of the KIX domain of CBPP bound to the transactivation domain of CREB: a model foractivator:coactivator interactions. Cell 1997 91 : 741 52.
    • (1997) Cell , vol.91 , pp. 741-52
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 7
    • 9944258521 scopus 로고    scopus 로고
    • New insights into FAK signaling and localization based on detyection of a FAT domain folding intermediate
    • Dixon RD, Chen Y, Ding F et al. New insights into FAK signaling and localization based on detyection of a FAT domain folding intermediate. Structure 2004 12 : 2161 71.
    • (2004) Structure , vol.12 , pp. 2161-71
    • Dixon, R.D.1    Chen, Y.2    Ding, F.3
  • 8
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FLGM, becomes structured when bound to its target, sigma 28
    • Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. The C-terminal half of the anti-sigma factor, FLGM, becomes structured when bound to its target, sigma 28. Nat Struct Biol 1997 4 : 285 91.
    • (1997) Nat Struct Biol , vol.4 , pp. 285-91
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 9
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005 6 : 435 50.
    • (2005) Nat Rev Genet , vol.6 , pp. 435-50
    • Shorter, J.1    Lindquist, S.2
  • 10
    • 48349091748 scopus 로고    scopus 로고
    • Self-replicating protein conformations and information transfer: The adaptive β-sheet model
    • Maury CPJ. Self-replicating protein conformations and information transfer: the adaptive β-sheet model. Biosci Hypotheses 2008 1 : 82 9.
    • (2008) Biosci Hypotheses , vol.1 , pp. 82-9
    • Maury, C.P.J.1
  • 11
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973 181 : 223 30.
    • (1973) Science , vol.181 , pp. 223-30
    • Anfinsen, C.B.1
  • 12
    • 46649088364 scopus 로고    scopus 로고
    • Metamorphic proteins
    • Murzin AG. Metamorphic proteins. Science 2008 320 : 1725 6.
    • (2008) Science , vol.320 , pp. 1725-6
    • Murzin, A.G.1
  • 13
    • 45849095234 scopus 로고    scopus 로고
    • How do proteins interact?
    • Boehr DD, Wright PE. How do proteins interact? Science 2008 320 : 1429 30.
    • (2008) Science , vol.320 , pp. 1429-30
    • Boehr, D.D.1    Wright, P.E.2
  • 19
    • 23944519950 scopus 로고    scopus 로고
    • The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats
    • Cherny I, Rockah L, Levy-Nissenbaum O, Gophna U, Ron EZ, Gazit E. The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats. J Mol Biol 2005 352 : 245 52.
    • (2005) J Mol Biol , vol.352 , pp. 245-52
    • Cherny, I.1    Rockah, L.2    Levy-Nissenbaum, O.3    Gophna, U.4    Ron, E.Z.5    Gazit, E.6
  • 21
    • 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
    • Claessen D, Rink R, de Jong WW et al. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev 2003 17 : 1714 26.
    • (2003) Genes Dev , vol.17 , pp. 1714-26
    • Claessen, D.1    Rink, R.2    De Jong, W.W.3
  • 22
    • 0033823006 scopus 로고    scopus 로고
    • Molecular genetics of heterokaryon incompatibility in filamentous Ascomycetes
    • Saupe SJ. Molecular genetics of heterokaryon incompatibility in filamentous Ascomycetes. Microbiol Mol Biol Rev 2000 64 : 489 502.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 489-502
    • Saupe, S.J.1
  • 23
    • 0038219626 scopus 로고    scopus 로고
    • Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
    • Balguerie A, Dos Reis S, Ritter C et al. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J 2003 22 : 2071 81.
    • (2003) EMBO J , vol.22 , pp. 2071-81
    • Balguerie, A.1    Dos Reis, S.2    Ritter, C.3
  • 24
    • 0037986392 scopus 로고    scopus 로고
    • Propertrin convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson JF, Theos AC, Harper DC, Tenza D, Raposo G, Marks MS. Propertrin convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J Cell Biol 2003 161 : 521 33.
    • (2003) J Cell Biol , vol.161 , pp. 521-33
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 26
    • 38349177843 scopus 로고    scopus 로고
    • Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes
    • Harper DC, Theos AC, Herman KE, Tenza D, Raposo G, Marks MS. Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes. J Biol Chem 2008 283 : 2307 22.
    • (2008) J Biol Chem , vol.283 , pp. 2307-22
    • Harper, D.C.1    Theos, A.C.2    Herman, K.E.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 27
    • 0037195269 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator is a multiligand cross-β structure receptor
    • Kranenburg O, Bouma B, Kroon-Betnburg LM et al. Tissue-type plasminogen activator is a multiligand cross-β structure receptor. Curr Biol 2002 12 : 1833 9.
    • (2002) Curr Biol , vol.12 , pp. 1833-9
    • Kranenburg, O.1    Bouma, B.2    Kroon-Betnburg, L.M.3
  • 29
    • 4444322354 scopus 로고    scopus 로고
    • Do antiangiogenic protein fragments have amyloid properties
    • Gebbink MF, Voest EE, Rejerkerk A. Do antiangiogenic protein fragments have amyloid properties. Blood 2004 104 : 1601 5.
    • (2004) Blood , vol.104 , pp. 1601-5
    • Gebbink, M.F.1    Voest, E.E.2    Rejerkerk, A.3
  • 30
    • 36849093472 scopus 로고    scopus 로고
    • Semen-derived amyloid fibrils drastically enhance HIV infection
    • Munch J, Rucker E, Ständker L et al. Semen-derived amyloid fibrils drastically enhance HIV infection. Cell 2007 131 : 1059 71.
    • (2007) Cell , vol.131 , pp. 1059-71
    • Munch, J.1    Rucker, E.2    Ständker, L.3
  • 31
    • 25444496212 scopus 로고    scopus 로고
    • Nucleic acid chaperones: A theory of an RNA-assisted protein folding
    • Biro JC. Nucleic acid chaperones: a theory of an RNA-assisted protein folding. Theor Biol Med Model 2005 2 : 35 45.
    • (2005) Theor Biol Med Model , vol.2 , pp. 35-45
    • Biro, J.C.1
  • 32
    • 50549103984 scopus 로고    scopus 로고
    • Protein solubility and folding enhancement by interaction with RNA
    • Choi SI, Han KS, Kim CW et al. Protein solubility and folding enhancement by interaction with RNA. PLoS ONE 2008 3 : e2677.
    • (2008) PLoS ONE , vol.3
    • Choi, S.I.1    Han, K.S.2    Kim, C.W.3
  • 33
    • 33750292395 scopus 로고    scopus 로고
    • Cross-talk between RNA and prions
    • Crist CG, Nakamura Y. Cross-talk between RNA and prions. J Biochem 2006 140 : 167 73.
    • (2006) J Biochem , vol.140 , pp. 167-73
    • Crist, C.G.1    Nakamura, Y.2
  • 35
    • 9444267651 scopus 로고    scopus 로고
    • The state of the prion
    • Weissmann C. The state of the prion. Nat Rev Microbiol 2004 2 : 861 71.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 861-71
    • Weissmann, C.1
  • 36
    • 17444366966 scopus 로고    scopus 로고
    • From microbes to prions: The final proof of the prion hypothesis
    • When-Quan Z, Cambetti P. From microbes to prions: the final proof of the prion hypothesis. Cell 2005 12 : 155 62.
    • (2005) Cell , vol.12 , pp. 155-62
    • When-Quan, Z.1    Cambetti, P.2
  • 37
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 2004 428 : 319 23.
    • (2004) Nature , vol.428 , pp. 319-23
    • King, C.Y.1    Diaz-Avalos, R.2
  • 38
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variation in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Conformational variation in an infectious protein determine prion strain differences. Nature 2004 248 : 323 8.
    • (2004) Nature , vol.248 , pp. 323-8
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 40
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structure and infectivity of the HET-s prion
    • Ritter C, Maddelein ML, Siemer AB et al. Correlation of structure and infectivity of the HET-s prion. Nature 2005 435 : 844 8.
    • (2005) Nature , vol.435 , pp. 844-8
    • Ritter, C.1    Maddelein, M.L.2    Siemer, A.B.3
  • 42
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K, Lindquist S, Kandel ER. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003 115 : 879 91.
    • (2003) Cell , vol.115 , pp. 879-91
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 43
    • 44449179474 scopus 로고    scopus 로고
    • Chaperone-dependent amyloid assembly protects cells from prion toxicity
    • Douglas PM, Treusch S, Ren HY et al. Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci USA 2008 105 : 7206 11.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7206-11
    • Douglas, P.M.1    Treusch, S.2    Ren, H.Y.3
  • 44
    • 0035005523 scopus 로고    scopus 로고
    • Survival of water stress in fish embryos:dehydration avoidance and egg envelope amyloid fibers
    • Podrabsky JE, Carpenter JF, Hand SC. Survival of water stress in fish embryos:dehydration avoidance and egg envelope amyloid fibers. Am J Physiol Regul Integr Comp Physiol 2001 280 : R123 31.
    • (2001) Am J Physiol Regul Integr Comp Physiol , vol.280
    • Podrabsky, J.E.1    Carpenter, J.F.2    Hand, S.C.3
  • 45
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect silk moth oocyte and embryo
    • Iconomidou VA, Vriend G, Hamodrakas SJ. Amyloids protect silk moth oocyte and embryo. FEBS Lett 2000 479 : 141 1445.
    • (2000) FEBS Lett , vol.479 , pp. 141-1445
    • Iconomidou, V.A.1    Vriend, G.2    Hamodrakas, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.