메뉴 건너뛰기




Volumn 47, Issue 3, 2012, Pages 282-296

Gelsolin amyloidosis: Genetics, biochemistry, pathology and possible strategies for therapeutic intervention

Author keywords

Aberrant proteolysis; Amyloidogenesis; Calcium binding; Familial amyloidosis of Finnish type; Furin; Gelsolin amyloid disease

Indexed keywords

FURIN; GELSOLIN; METALLOPROTEINASE;

EID: 84860128609     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2012.661401     Document Type: Review
Times cited : (86)

References (145)
  • 1
    • 33846029140 scopus 로고    scopus 로고
    • Amyloidosis-related nephrotic syndrome due to a G654A gelsolin mutation: The first report from the Middle East
    • DOI 10.1093/ndt/gfl548, Special Issue on Pediatric Overweight
    • Ardalan MR, Shoja MM, Kiuru-Enari S. 2007. Amyloidosis-related nephrotic syndrome due to a G654A gelsolin mutation: the first report from the Middle East. Nephrol Dial Transplant 22: 272-275. (Pubitemid 46050357)
    • (2007) Nephrology Dialysis Transplantation , vol.22 , Issue.1 , pp. 272-275
    • Ardalan, M.R.1    Shoja, M.M.2    Kiuru-Enari, S.3
  • 4
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch WE, Morimoto RI, Dillin A, Kelly JW. 2008. Adapting proteostasis for disease intervention. Science 319: 916-919. (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 5
    • 0031684499 scopus 로고    scopus 로고
    • Discovering transthyretin amyloid fibril inhibitors by limited screening
    • DOI 10.1016/S0968-0896(98)00130-8, PII S0968089698001308
    • Baures PW, Peterson SA, Kelly JW. 1998. Discovering transthyretin amyloid fibril inhibitors by limited screening. Bioorg Med Chem 6: 1389-1401. (Pubitemid 28398970)
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , Issue.8 , pp. 1389-1401
    • Baures, P.W.1    Peterson, S.A.2    Kelly, J.W.3
  • 6
    • 0032970177 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid
    • DOI 10.1016/S0968-0896(99)00066-8, PII S0968089699000668
    • Baures PW, Oza VB, Peterson SA, Kelly JW. 1999. Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid. Bioorg Med Chem 7: 1339-1347. (Pubitemid 29292374)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.7 , pp. 1339-1347
    • Baures, P.W.1    Oza, V.B.2    Peterson, S.A.3    Kelly, J.W.4
  • 8
    • 16344385440 scopus 로고    scopus 로고
    • Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a two-step mechanism, eliminating the requirement for nucleation
    • DOI 10.1021/bi0501030
    • Bieschke J, Zhang Q, Powers ET, Lerner RA, Kelly JW. 2005. Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a twostep mechanism, eliminating the requirement for nucleation. Biochemistry 44: 4977-4983. (Pubitemid 40471214)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 4977-4983
    • Bieschke, J.1    Zhang, Q.2    Powers, E.T.3    Lerner, R.A.4    Kelly, J.W.5
  • 12
    • 79851492876 scopus 로고    scopus 로고
    • Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion
    • Bourgault S, Solomon JP, Reixach N, Kelly JW. 2011. Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion. Biochemistry 50: 1001-1015.
    • (2011) Biochemistry , vol.50 , pp. 1001-1015
    • Bourgault, S.1    Solomon, J.P.2    Reixach, N.3    Kelly, J.W.4
  • 14
    • 57849150175 scopus 로고    scopus 로고
    • Extracellular gelsolin binds lipoteichoic acid and modulates cellular response to proinflammatory bacterial wall components
    • Bucki R, Byfield FJ, Kulakowska A, McCormick ME, Drozdowski W, Namiot Z, Hartung T, Janmey PA. 2008a. Extracellular gelsolin binds lipoteichoic acid and modulates cellular response to proinflammatory bacterial wall components. J Immunol 181: 4936-4944.
    • (2008) J Immunol , vol.181 , pp. 4936-4944
    • Bucki, R.1    Byfield, F.J.2    Kulakowska, A.3    McCormick, M.E.4    Drozdowski, W.5    Namiot, Z.6    Hartung, T.7    Janmey, P.A.8
  • 16
    • 65549117004 scopus 로고    scopus 로고
    • Plasma gelsolin: Function, prognostic value, and potential therapeutic use
    • Bucki R, Levental I, Kulakowska A, Janmey PA. 2008b. Plasma gelsolin: function, prognostic value, and potential therapeutic use. Curr Protein Pept Sci 9: 541-551.
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 541-551
    • Bucki, R.1    Levental, I.2    Kulakowska, A.3    Janmey, P.A.4
  • 17
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
    • DOI 10.1016/S0092-8674(00)80527-9
    • Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC. 1997. The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell 90: 661-670. (Pubitemid 27357958)
    • (1997) Cell , vol.90 , Issue.4 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6    Robinson, R.C.7
  • 18
    • 73349122594 scopus 로고    scopus 로고
    • Lattice corneal dystrophy, gelsolin type (Meretoja's syndrome)
    • Carrwik C, Stenevi U. 2009. Lattice corneal dystrophy, gelsolin type (Meretoja's syndrome). Acta Ophthalmol 87: 813-819.
    • (2009) Acta Ophthalmol , vol.87 , pp. 813-819
    • Carrwik, C.1    Stenevi, U.2
  • 20
    • 30344467836 scopus 로고    scopus 로고
    • Cardiac conduction alterations in a French family with amyloidosis of the Finnish type with the p.Asp187Tyr mutation in the GSN gene
    • DOI 10.1002/mus.20448
    • Chastan N, Baert-Desurmont S, Saugier-Veber P, Dérumeaux G, Cabot A, Frébourg T, Hannequin D. 2006. Cardiac conduction alterations in a French family with amyloidosis of the Finnish type with the p.Asp187Tyr mutation in the GSN gene. Muscle Nerve 33: 113-119. (Pubitemid 43062993)
    • (2006) Muscle and Nerve , vol.33 , Issue.1 , pp. 113-119
    • Chastan, N.1    Baert-Desurmont, S.2    Saugier-Veber, P.3    Derumeaux, G.4    Cabot, A.5    Frebourg, T.6    Hannequin, D.7
  • 21
    • 56049096721 scopus 로고    scopus 로고
    • Anti-amyloidogenic, anti-oxidant and anti-apoptotic role of gelsolin in Alzheimer's disease
    • Chauhan V, Ji L, Chauhan A. 2008. Anti-amyloidogenic, anti-oxidant and anti-apoptotic role of gelsolin in Alzheimer's disease. Biogerontology 9: 381-389.
    • (2008) Biogerontology , vol.9 , pp. 381-389
    • Chauhan, V.1    Ji, L.2    Chauhan, A.3
  • 24
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. 2003. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424: 805-808. (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 25
    • 0036923313 scopus 로고    scopus 로고
    • The calcium activation of gelsolin: Insights from the 3 A structure of the G4-G6/actin complex
    • DOI 10.1016/S0022-2836(02)01131-2
    • Choe H, Burtnick LD, Mejillano M, Yin HL, Robinson RC, Choe S. 2002. The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex. J Mol Biol 324: 691-702. (Pubitemid 36044107)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.4 , pp. 691-702
    • Choe, H.1    Burtnick, L.D.2    Mejillano, M.3    Yin, H.L.4    Robinson, R.C.5    Choe, S.6
  • 26
    • 0000650678 scopus 로고    scopus 로고
    • Nucleated antiparallel β-sheet that folds and undergoes self-assembly: A template promoted folding strategy toward controlled molecular architectures
    • Choo DW, Schneider JP, Graciani NR, Kelly JW. 1996. Nucleated antiparallel OE≤-sheet that folds and undergoes self-assembly: a template promoted folding strategy toward controlled molecular architectures. Macromolecules 29: 355-366. (Pubitemid 126548685)
    • (1996) Macromolecules , vol.29 , Issue.1 , pp. 355-366
    • Choo, D.W.1    Schneider, J.P.2    Graciani, N.R.3    Kelly, J.W.4
  • 29
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to proteinmisfolding diseases
    • Cohen FE, Kelly JW. 2003. Therapeutic approaches to proteinmisfolding diseases. Nature 426: 905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 33
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • Dobson CM. 2003. Protein folding and misfolding. Nature 426: 884-890. (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 34
    • 33644850570 scopus 로고    scopus 로고
    • Inclusion-body myositis: Clinical, diagnostic, and pathologic aspects
    • PII 0000611420060124100004
    • Engel WK, Askanas V. 2006. Inclusion-body myositis: clinical, diagnostic, and pathologic aspects. Neurology 66: S20-S29. (Pubitemid 43739980)
    • (2006) Neurology , vol.66 , Issue.2 SUPPL. 1
    • Engel, W.K.1    Askanas, V.2
  • 35
    • 77958459087 scopus 로고    scopus 로고
    • Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies
    • Falzone TL, Gunawardena S, McCleary D, Reis GF, Goldstein LS. 2010. Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies. Hum Mol Genet 19: 4399-4408.
    • (2010) Hum Mol Genet , vol.19 , pp. 4399-4408
    • Falzone, T.L.1    Gunawardena, S.2    McCleary, D.3    Reis, G.F.4    Goldstein, L.S.5
  • 36
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich M, Fletcher MA, Dobson CM. 2001. Amyloid fibrils from muscle myoglobin. Nature 410: 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 37
    • 84860114158 scopus 로고    scopus 로고
    • Corneal lattic dystrophy type II: Familial amyloid neuropathy type IV (gelsolin amyloidosis)
    • Felix EPV, Jung LS, Carvalho GS, Oliveira ASB. 2008. Corneal lattic dystrophy type II: Familial amyloid neuropathy type IV (gelsolin amyloidosis). Einstein 6: 505-506.
    • (2008) Einstein , vol.6 , pp. 505-506
    • Felix, E.P.V.1    Jung, L.S.2    Carvalho, G.S.3    Oliveira, A.S.B.4
  • 38
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L. 2004. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22: 1302-1306. (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 39
    • 84860199935 scopus 로고    scopus 로고
    • Amyloid, Prions, and Other Protein Aggregates San Diego: Academic Press, Inc.
    • Ferrone F. 1999. Analysis of protein aggregation kinetics. Amyloid, Prions, and Other Protein Aggregates San Diego: Academic Press Inc.
    • (1999) Analysis of Protein Aggregation Kinetics
    • Ferrone, F.1
  • 40
    • 56649100319 scopus 로고    scopus 로고
    • The structure of glycosaminoglycans and their interactions with proteins
    • Gandhi NS, Mancera RL. 2008. The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des 72: 455-482.
    • (2008) Chem Biol Drug des , vol.72 , pp. 455-482
    • Gandhi, N.S.1    Mancera, R.L.2
  • 41
    • 0242299247 scopus 로고    scopus 로고
    • Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization
    • DOI 10.1021/ja030294z
    • Green NS, Palaninathan SK, Sacchettini JC, Kelly JW. 2003. Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization. J Am Chem Soc 125: 13404-13414. (Pubitemid 37352125)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.44 , pp. 13404-13414
    • Green, N.S.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 44
    • 0038661338 scopus 로고    scopus 로고
    • D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: A prescription for central nervous system amyloidosis?
    • DOI 10.1021/bi027319b
    • Hammarström P, Sekijima Y, White JT, Wiseman RL, Lim A, Costello CE, Altland K, Garzuly F, Budka H, Kelly JW. 2003a. D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis? Biochemistry 42: 6656-6663. (Pubitemid 36666106)
    • (2003) Biochemistry , vol.42 , Issue.22 , pp. 6656-6663
    • Hammarstrom, P.1    Sekijima, Y.2    White, J.T.3    Wiseman, R.L.4    Lim, A.5    Costello, C.E.6    Altland, K.7    Garzuly, F.8    Budka, H.9    Kelly, J.W.10
  • 46
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • DOI 10.1126/science.1062245
    • Hammarström P, Schneider F, Kelly JW. 2001. Trans-suppression of misfolding in an amyloid disease. Science 293: 2459-2462. (Pubitemid 32917328)
    • (2001) Science , vol.293 , Issue.5539 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 47
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin arnyloid disease by changing protein misfolding energetics
    • DOI 10.1126/science.1079589
    • Hammarström P, Wiseman RL, Powers ET, Kelly JW. 2003b. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science. 299: 713-716. (Pubitemid 36159487)
    • (2003) Science , vol.299 , Issue.5607 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 48
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. 2011. Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 49
    • 58149385090 scopus 로고    scopus 로고
    • Enhanced sensitivity of striatal neurons to axonal transport defects induced by mutant huntingtin
    • Her LS, Goldstein LS. 2008. Enhanced sensitivity of striatal neurons to axonal transport defects induced by mutant huntingtin. J Neurosci 28: 13662-13672.
    • (2008) J Neurosci , vol.28 , pp. 13662-13672
    • Her, L.S.1    Goldstein, L.S.2
  • 50
    • 34548107246 scopus 로고    scopus 로고
    • Peripheral transgene expression of plasma gelsolin reduces amyloid in transgenic mouse models of Alzheimer's disease
    • DOI 10.1038/sj.mt.6300253, PII 6300253
    • Hirko AC, Meyer EM, King MA, Hughes JA. 2007. Peripheral transgene expression of plasma gelsolin reduces amyloid in transgenic mouse models of Alzheimer's disease. Mol Ther 15: 1623-1629. (Pubitemid 47289005)
    • (2007) Molecular Therapy , vol.15 , Issue.9 , pp. 1623-1629
    • Hirko, A.C.1    Meyer, E.M.2    King, M.A.3    Hughes, J.A.4
  • 52
    • 0347481472 scopus 로고    scopus 로고
    • Pathological and functional amyloid formation orchestrated by the secretory pathway
    • DOI 10.1016/j.sbi.2003.10.010
    • Huff ME, Balch WE, Kelly JW. 2003a. Pathological and functional amyloid formation orchestrated by the secretory pathway. Curr Opin Struct Biol 13: 674-682. (Pubitemid 37522142)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.6 , pp. 674-682
    • Huff, M.E.1    Balch, W.E.2    Kelly, J.W.3
  • 53
    • 0142195727 scopus 로고    scopus 로고
    • 2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of Finnish type
    • DOI 10.1016/j.jmb.2003.09.029
    • Huff ME, Page LJ, Balch WE, Kelly JW. 2003b. Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of Finnish type. J Mol Biol 334: 119-127. (Pubitemid 37330104)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.1 , pp. 119-127
    • Huff, M.E.1    Page, L.J.2    Balch, W.E.3    Kelly, J.W.4
  • 54
    • 46049085810 scopus 로고    scopus 로고
    • Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: The relationship between stability and amyloidosis
    • DOI 10.1021/bi800636q
    • Hurshman Babbes AR, Powers ET, Kelly JW. 2008. Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis. Biochemistry 47: 6969-6984. (Pubitemid 351898951)
    • (2008) Biochemistry , vol.47 , Issue.26 , pp. 6969-6984
    • Hurshman Babbes, A.R.1    Powers, E.T.2    Kelly, J.W.3
  • 55
    • 4644236043 scopus 로고    scopus 로고
    • Causal relation between α-synuclein gene duplication and familial Parkinson's disease
    • DOI 10.1016/S0140-6736(04)17104-3, PII S0140673604171043
    • Ibáñez P, Bonnet AM, Débarges B, Lohmann E, Tison F, Pollak P, Agid Y, Dürr A, Brice A. 2004. Causal relation between α-synuclein gene duplication and familial Parkinson's disease. Lancet 364: 1169-1171. (Pubitemid 39296605)
    • (2004) Lancet , vol.364 , Issue.9440 , pp. 1169-1171
    • Ibanez, P.1    Bonnet, A.-M.2    Debarges, B.3    Lohmann, E.4    Tison, F.5    Pollak, P.6    Agid, Y.7    Durr, A.8    Brice, P.A.9
  • 57
    • 79959944588 scopus 로고    scopus 로고
    • γ-secretase inhibitors and modulators for the treatment of Alzheimer's disease: Disappointments and hopes
    • Imbimbo BP, Giardina GA. 2011. γ-secretase inhibitors and modulators for the treatment of Alzheimer's disease: disappointments and hopes. Curr Top Med Chem 11: 1555-1570.
    • (2011) Curr Top Med Chem , vol.11 , pp. 1555-1570
    • Imbimbo, B.P.1    Giardina, G.A.2
  • 58
    • 39749137459 scopus 로고    scopus 로고
    • Cytoplasmic gelsolin in pheochromocytoma-12 cells forms a complex with amyloid beta-protein
    • DOI 10.1097/WNR.0b013e3282f5f79a, PII 0000175620080305000014
    • Ji L, Chauhan A, Chauhan V. 2008. Cytoplasmic gelsolin in pheochromocytoma-12 cells forms a complex with amyloid betaprotein. Neuroreport 19: 463-466. (Pubitemid 351301606)
    • (2008) NeuroReport , vol.19 , Issue.4 , pp. 463-466
    • Ji, L.1    Chauhan, A.2    Chauhan, V.3
  • 59
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • DOI 10.1073/pnas.261419998
    • Jiang X, Buxbaum JN, Kelly JW. 2001. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci USA 98: 14943-14948. (Pubitemid 34013949)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.26 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 61
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, Kelly JW. 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
  • 62
    • 0029817405 scopus 로고    scopus 로고
    • In vitro expression analysis shows that the secretory form of gelsolin is the sole source of amyloid in gelsolin-related amyloidosis
    • DOI 10.1093/hmg/5.9.1237
    • Kangas H, Paunio T, Kalkkinen N, Jalanko A, Peltonen L. 1996. In vitro expression analysis shows that the secretory form of gelsolin is the sole source of amyloid in gelsolin-related amyloidosis. Hum Mol Genet 5: 1237-1243. (Pubitemid 26335840)
    • (1996) Human Molecular Genetics , vol.5 , Issue.9 , pp. 1237-1243
    • Kangas, H.1    Paunio, T.2    Kalkkinen, N.3    Jalanko, A.4    Peltonen, L.5
  • 63
    • 0035997522 scopus 로고    scopus 로고
    • Role of proprotein convertases in the pathogenic processing of the amyloidosis-associated form of secretory gelsolin
    • Kangas H, Seidah NG, Paunio T. 2002. Role of proprotein convertases in the pathogenic processing of the amyloidosis-associated form of secretory gelsolin. Amyloid 9: 83-87. (Pubitemid 34787801)
    • (2002) Amyloid , vol.9 , Issue.2 , pp. 83-87
    • Kangas, H.1    Seidah, N.G.2    Paunio, T.3
  • 65
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • DOI 10.1016/S0959-440X(96)80089-3
    • Kelly JW. 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6: 11-17. (Pubitemid 26073939)
    • (1996) Current Opinion in Structural Biology , vol.6 , Issue.1 , pp. 11-17
    • Kelly, J.W.1
  • 66
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • DOI 10.1016/S0959-440X(98)80016-X
    • Kelly JW. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8: 101-106. (Pubitemid 28107921)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.1 , pp. 101-106
    • Kelly, J.W.1
  • 67
    • 0037134851 scopus 로고    scopus 로고
    • Ca-dependent binding of actin to gelsolin
    • DOI 10.1016/S0014-5793(02)02657-1, PII S0014579302026571
    • Khaitlina S, Hinssen H. 2002. Ca-dependent binding of actin to gelsolin. FEBS Lett 521: 14-18. (Pubitemid 34628449)
    • (2002) FEBS Letters , vol.521 , Issue.1-3 , pp. 14-18
    • Khaitlina, S.1    Hinssen, H.2
  • 68
    • 14844296958 scopus 로고    scopus 로고
    • Cutis laxa in hereditary gelsolin amyloidosis
    • DOI 10.1111/j.1365-2133.2004.06276.x
    • Kiuru-Enari S, Keski-Oja J, Haltia M. 2005. Cutis laxa in hereditary gelsolin amyloidosis. Br J Dermatol 152: 250-257. (Pubitemid 40343594)
    • (2005) British Journal of Dermatology , vol.152 , Issue.2 , pp. 250-257
    • Kiuru-Enari, S.1    Keski-Oja, J.2    Haltia, M.3
  • 70
    • 0032012657 scopus 로고    scopus 로고
    • Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide
    • Kiuru S. 1998. Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide. Amyloid 5: 55-66. (Pubitemid 128691218)
    • (1998) Amyloid , vol.5 , Issue.1 , pp. 55-66
    • Kiuru, S.1
  • 71
    • 0027980608 scopus 로고
    • Autonomic nervous system and cardiac involvement in familial amyloidosis, Finnish type (FAF)
    • DOI 10.1016/0022-510X(94)90092-2
    • Kiuru S, Matikainen E, Kupari M, Haltia M, Palo J. 1994. Autonomic nervous system and cardiac involvement in familial amyloidosis, Finnish type (FAF). J Neurol Sci 126: 40-48. (Pubitemid 24305257)
    • (1994) Journal of the Neurological Sciences , vol.126 , Issue.1 , pp. 40-48
    • Kiuru, S.1    Matikainen, E.2    Kupari, M.3    Haltia, M.4    Palo, J.5
  • 72
    • 0028053692 scopus 로고
    • Ocular amyloid deposition in familial amyloidosis, Finnish: An analysis of native and variant gelsolin in Meretoja's syndrome
    • Kivelä T, Tarkkanen A, Frangione B, Ghiso J, Haltia M. 1994. Ocular amyloid deposition in familial amyloidosis, Finnish: an analysis of native and variant gelsolin in Meretoja's syndrome. Invest Ophthalmol Vis Sci 35: 3759-3769. (Pubitemid 24337989)
    • (1994) Investigative Ophthalmology and Visual Science , vol.35 , Issue.10 , pp. 3759-3769
    • Kivela, T.1    Tarkkanen, A.2    Frangione, B.3    Ghiso, J.4    Haltia, M.5
  • 75
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL. 1986. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323: 455-458. (Pubitemid 16026275)
    • (1986) Nature , vol.323 , Issue.6087 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3
  • 77
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr. 2002. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418: 291. (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 78
    • 84860389674 scopus 로고    scopus 로고
    • Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    • Lee J, Culyba EK, Powers ET, Kelly JW. 2011. Amyloid-β forms fibrils by nucleated conformational conversion of oligomers. Nat Chem Biol 7: 602-609.
    • (2011) Nat Chem Biol , vol.7 , pp. 602-609
    • Lee, J.1    Culyba, E.K.2    Powers, E.T.3    Kelly, J.W.4
  • 79
    • 33947164459 scopus 로고    scopus 로고
    • Plasma gelsolin is a marker and therapeutic agent in animal sepsis
    • DOI 10.1097/01.CCM.0000253815.26311.24, PII 0000324620070300000024
    • Lee PS, Waxman AB, Cotich KL, Chung SW, Perrella MA, Stossel TP. 2007. Plasma gelsolin is a marker and therapeutic agent in animal sepsis. Crit Care Med 35: 849-855. (Pubitemid 46407801)
    • (2007) Critical Care Medicine , vol.35 , Issue.3 , pp. 849-855
    • Lee, P.-S.1    Waxman, A.B.2    Cotich, K.L.3    Chung, S.W.4    Perrella, M.A.5    Stossel, T.P.6
  • 80
    • 0037622075 scopus 로고    scopus 로고
    • Molecular dynamics study of a gelsolin-derived peptide binding to a lipid bilayer containing phosphatidylinositol 4,5-bisphosphate
    • DOI 10.1002/bip.10375
    • Liepina I, Czaplewski C, Janmey P, Liwo A. 2003. Molecular dynamics study of a gelsolin-derived peptide binding to a lipid bilayer containing phosphatidylinositol 4,5-bisphosphate. Biopolymers 71: 49-70. (Pubitemid 36548117)
    • (2003) Biopolymers - Peptide Science Section , vol.71 , Issue.1 , pp. 49-70
    • Liepina, I.1    Czaplewski, C.2    Janmey, P.3    Liwo, A.4
  • 82
    • 0034625120 scopus 로고    scopus 로고
    • Calcium regulation of gelsolin and adseverin: A natural test of the helix latch hypothesis
    • DOI 10.1021/bi992871v
    • Lueck A, Yin HL, Kwiatkowski DJ, Allen PG. 2000. Calcium regulation of gelsolin and adseverin: a natural test of the helix latch hypothesis. Biochemistry 39: 5274-5279. (Pubitemid 30257065)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5274-5279
    • Lueck, A.1    Yin, H.L.2    Kwiatkowski, D.J.3    Allen, P.G.4
  • 83
    • 77951290391 scopus 로고    scopus 로고
    • Hereditary amyloidosis of the Finnish type in a German family: Clinical and electrophysiological presentation
    • Lüttmann RJ, Teismann I, Husstedt IW, Ringelstein EB, Kuhlenbäumer G. 2010. Hereditary amyloidosis of the Finnish type in a German family: clinical and electrophysiological presentation. Muscle Nerve 41: 679-684.
    • (2010) Muscle Nerve , vol.41 , pp. 679-684
    • Lüttmann, R.J.1    Teismann, I.2    Husstedt, I.W.3    Ringelstein, E.B.4    Kuhlenbäumer, G.5
  • 85
    • 79958031499 scopus 로고    scopus 로고
    • 1-Palmitoyl-2-(9'-oxononanoyl)-sn-glycero-3-phosphocholine, an oxidized phospholipid, accelerates Finnish type familial gelsolin amyloidosis in vitro
    • Mahalka AK, Maury CP, Kinnunen PK. 2011. 1-Palmitoyl-2-(9'-oxononanoyl)- sn-glycero-3-phosphocholine, an oxidized phospholipid, accelerates Finnish type familial gelsolin amyloidosis in vitro. Biochemistry 50: 4877-4889.
    • (2011) Biochemistry , vol.50 , pp. 4877-4889
    • Mahalka, A.K.1    Maury, C.P.2    Kinnunen, P.K.3
  • 86
    • 77952835929 scopus 로고    scopus 로고
    • Familial amyloid polyneuropathy (Finnish type) presenting multiple cranial nerve deficits with carpal tunnel syndrome and orthostatic hypotension
    • Makioka K, Ikeda M, Ikeda Y, Nakasone A, Osawa T, Sasaki A, Otani T, Arai M, Okamoto K. 2010. Familial amyloid polyneuropathy (Finnish type) presenting multiple cranial nerve deficits with carpal tunnel syndrome and orthostatic hypotension. Neurol Res 32: 472-475.
    • (2010) Neurol Res , vol.32 , pp. 472-475
    • Makioka, K.1    Ikeda, M.2    Ikeda, Y.3    Nakasone, A.4    Osawa, T.5    Sasaki, A.6    Otani, T.7    Arai, M.8    Okamoto, K.9
  • 87
    • 0025779730 scopus 로고
    • Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin
    • Maury CP. 1991. Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin. J Clin Invest 87: 1195-1199.
    • (1991) J Clin Invest , vol.87 , pp. 1195-1199
    • Maury, C.P.1
  • 88
    • 0027317623 scopus 로고
    • Homozygous familial amyloidosis, Finnish type: Demonstration of glomerular gelsolin-derived amyloid and non-amyloid tubular gelsolin
    • Maury CP. 1993. Homozygous familial amyloidosis, Finnish type: demonstration of glomerular gelsolin-derived amyloid and nonamyloid tubular gelsolin. Clin Nephrol 40: 53-56. (Pubitemid 23221734)
    • (1993) Clinical Nephrology , vol.40 , Issue.1 , pp. 53-56
    • Maury, C.P.J.1
  • 89
    • 0028263333 scopus 로고
    • Amyloid fibril formation in gelsolin-derived amyloidosis: Definition of the amyloidogenic region and evidence of accelerated amyloid formation of mutant Asn-187 and Tyr-187 gelsolin peptides
    • Maury CP, Nurmiaho-Lassila EL, Rossi H. 1994. Amyloid fibril formation in gelsolin-derived amyloidosis. Definition of the amyloidogenic region and evidence of accelerated amyloid formation of mutant Asn-187 and Tyr-187 gelsolin peptides. Lab Invest 70: 558-564. (Pubitemid 24185027)
    • (1994) Laboratory Investigation , vol.70 , Issue.4 , pp. 558-564
    • Maury, C.P.J.1    Nurmiaho-Lassila, E.-L.2    Rossi, H.3
  • 90
    • 0014640130 scopus 로고
    • Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms. A previously unrecognized heritable syndrome
    • Meretoja J. 1969. Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms. A previously unrecognized heritable syndrome. Ann Clin Res 1: 314-324.
    • (1969) Ann Clin Res , vol.1 , pp. 314-324
    • Meretoja, J.1
  • 91
    • 0015806355 scopus 로고
    • Genetic aspects of familial amyloidosis with corneal lattice dystrophy and cranial neuropathy
    • Meretoja J. 1973. Genetic aspects of familial amyloidosis with corneal lattice dystrophy and cranial neuropathy. Clin Genet 4: 173-185.
    • (1973) Clin Genet , vol.4 , pp. 173-185
    • Meretoja, J.1
  • 92
    • 2942599707 scopus 로고    scopus 로고
    • Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants
    • DOI 10.1038/labinvest.3700059
    • Miller SR, Sekijima Y, Kelly JW. 2004. Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants. Lab Invest 84: 545-552. (Pubitemid 38858463)
    • (2004) Laboratory Investigation , vol.84 , Issue.5 , pp. 545-552
    • Miller, S.R.1    Sekijima, Y.2    Kelly, J.W.3
  • 96
    • 77952501011 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis
    • Ong DS, Mu TW, Palmer AE, Kelly JW. 2010. Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis. Nat Chem Biol 6: 424-432.
    • (2010) Nat Chem Biol , vol.6 , pp. 424-432
    • Ong, D.S.1    Mu, T.W.2    Palmer, A.E.3    Kelly, J.W.4
  • 101
    • 33644548658 scopus 로고    scopus 로고
    • Characterization of plasma gelsolin as a substrate for matrix metalloproteinases
    • Park SM, Hwang IK, Kim SY, Lee SJ, Park KS, Lee ST. 2006. Characterization of plasma gelsolin as a substrate for matrix metalloproteinases. Proteomics 6: 1192-1199.
    • (2006) Proteomics , vol.6 , pp. 1192-1199
    • Park, S.M.1    Hwang, I.K.2    Kim, S.Y.3    Lee, S.J.4    Park, K.S.5    Lee, S.T.6
  • 102
    • 0028567731 scopus 로고
    • Toward understanding the pathogenic mechanisms in gelsolinrelated amyloidosis: In vitro expression reveals an abnormal gelsolin fragment
    • Paunio T, Kangas H, Kalkkinen N, Haltia M, Palo J, Peltonen L. 1994. Toward understanding the pathogenic mechanisms in gelsolinrelated amyloidosis: in vitro expression reveals an abnormal gelsolin fragment. Hum Mol Genet 3: 2223-2229.
    • (1994) Hum Mol Genet , vol.3 , pp. 2223-2229
    • Paunio, T.1    Kangas, H.2    Kalkkinen, N.3    Haltia, M.4    Palo, J.5    Peltonen, L.6
  • 103
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • DOI 10.1146/annurev.med.57.121304.131243
    • Pepys MB. 2006. Amyloidosis. Annu Rev Med 57: 223-241. (Pubitemid 43261989)
    • (2006) Annual Review of Medicine , vol.57 , pp. 223-241
    • Pepys, M.B.1
  • 106
    • 79958716179 scopus 로고    scopus 로고
    • Gelsolin amyloidosis as a cause of early aging and progressive bilateral facial paralysis
    • Pihlamaa T, Rautio J, Kiuru-Enari S, Suominen S. 2011. Gelsolin amyloidosis as a cause of early aging and progressive bilateral facial paralysis. Plast Reconstr Surg 127: 2342-2351.
    • (2011) Plast Reconstr Surg , vol.127 , pp. 2342-2351
    • Pihlamaa, T.1    Rautio, J.2    Kiuru-Enari, S.3    Suominen, S.4
  • 107
  • 108
    • 38349011533 scopus 로고    scopus 로고
    • Mechanisms of protein fibril formation: Nucleated polymerization with competing off-pathway aggregation
    • Powers ET, Powers DL. 2008. Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation. Biophys J 94: 379-391.
    • (2008) Biophys J , vol.94 , pp. 379-391
    • Powers, E.T.1    Powers, D.L.2
  • 110
    • 0033133911 scopus 로고    scopus 로고
    • The amyloidogenicity of gelsolin is controlled by proteolysis and pH
    • DOI 10.1016/S1074-5521(99)80075-1
    • Ratnaswamy G, Koepf E, Bekele H, Yin H, Kelly JW. 1999. The amyloidogenicity of gelsolin is controlled by proteolysis and pH. Chem Biol 6: 293-304. (Pubitemid 29363180)
    • (1999) Chemistry and Biology , vol.6 , Issue.5 , pp. 293-304
    • Ratnaswamy, G.1    Koepf, E.2    Bekele, H.3    Yin, H.4    Kelly, J.W.5
  • 111
    • 0033988752 scopus 로고    scopus 로고
    • Gelsolin inhibits the fibrillization of amyloid beta-protein, and also defibrillizes its preformed fibrils
    • DOI 10.1016/S0006-8993(99)02315-X, PII S000689939902315X
    • Ray I, Chauhan A, Wegiel J, Chauhan VP. 2000. Gelsolin inhibits the fibrillization of amyloid β-protein, and also defibrillizes its preformed fibrils. Brain Res 853: 344-351. (Pubitemid 30035235)
    • (2000) Brain Research , vol.853 , Issue.2 , pp. 344-351
    • Ray, I.1    Chauhan, A.2    Wegiel, J.3    Chauhan, V.P.S.4
  • 112
  • 114
    • 33846844868 scopus 로고    scopus 로고
    • Calcium-induced conformational changes in the amino-terminal half of gelsolin
    • DOI 10.1016/j.febslet.2007.01.031, PII S0014579307000609
    • Roustan C, Ferjani I, Maciver SK, Fattoum A, Rebière B, Benyamin Y. 2007. Calcium-induced conformational changes in the aminoterminal half of gelsolin. FEBS Lett 581: 681-686. (Pubitemid 46216292)
    • (2007) FEBS Letters , vol.581 , Issue.4 , pp. 681-686
    • Roustan, C.1    Ferjani, I.2    Maciver, S.K.3    Fattoum, A.4    Rebiere, B.5    Benyamin, Y.6
  • 115
    • 20544466133 scopus 로고    scopus 로고
    • Evidence of the existence of micelles in the fibrillogenesis of β-amyloid peptide
    • DOI 10.1021/jp050716m
    • Sabaté R, Estelrich J. 2005. Evidence of the existence of micelles in the fibrillogenesis of beta-amyloid peptide. J Phys Chem B 109: 11027-11032. (Pubitemid 40844540)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.21 , pp. 11027-11032
    • Sabate, R.1    Estelrich, J.2
  • 118
    • 79952529991 scopus 로고    scopus 로고
    • What the halted phase III γ-secretase inhibitor trial may (or may not) be telling us
    • Schor NF. 2011. What the halted phase III γ-secretase inhibitor trial may (or may not) be telling us. Ann Neurol 69: 237-239.
    • (2011) Ann Neurol , vol.69 , pp. 237-239
    • Schor, N.F.1
  • 120
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • DOI 10.1038/nature02264
    • Selkoe DJ. 2003. Folding proteins in fatal ways. Nature 426: 900-904. (Pubitemid 38056883)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 121
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • DOI 10.1126/science.289.5483.1317
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, Arnsdorf MF, Lindquist SL. 2000. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-1321. (Pubitemid 30656041)
    • (2000) Science , vol.289 , Issue.5483 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6    Arnsdorf, M.F.7    Lindquist, S.L.8
  • 123
    • 67049087912 scopus 로고    scopus 로고
    • Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration
    • Shewmaker F, Kryndushkin D, Chen B, Tycko R, Wickner RB. 2009. Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration. Biochemistry 48: 5074-5082.
    • (2009) Biochemistry , vol.48 , pp. 5074-5082
    • Shewmaker, F.1    Kryndushkin, D.2    Chen, B.3    Tycko, R.4    Wickner, R.B.5
  • 125
    • 0023128689 scopus 로고
    • Sulfated glycosaminoglycans: A common constituent of all amyloids?
    • Snow AD, Willmer J, Kisilevsky R. 1987. Sulfated glycosaminoglycans: a common constituent of all amyloids Lab Invest 56: 120-123. (Pubitemid 17011178)
    • (1987) Laboratory Investigation , vol.56 , Issue.1 , pp. 120-123
    • Snow, A.D.1    Willmer, J.2    Kisilevsky, R.3
  • 126
    • 79953179308 scopus 로고    scopus 로고
    • Heparin binds 8 kDa gelsolin cross-β-sheet oligomers and accelerates amyloidogenesis by hastening fibril extension
    • Solomon JP, Bourgault S, Powers ET, Kelly JW. 2011. Heparin binds 8 kDa gelsolin cross-β-sheet oligomers and accelerates amyloidogenesis by hastening fibril extension. Biochemistry 50: 2486-2498.
    • (2011) Biochemistry , vol.50 , pp. 2486-2498
    • Solomon, J.P.1    Bourgault, S.2    Powers, E.T.3    Kelly, J.W.4
  • 127
    • 73149083275 scopus 로고    scopus 로고
    • The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic
    • Solomon JP, Yonemoto IT, Murray AN, Price JL, Powers ET, Balch WE, Kelly JW. 2009. The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic. Biochemistry 48: 11370-11380.
    • (2009) Biochemistry , vol.48 , pp. 11370-11380
    • Solomon, J.P.1    Yonemoto, I.T.2    Murray, A.N.3    Price, J.L.4    Powers, E.T.5    Balch, W.E.6    Kelly, J.W.7
  • 128
    • 0034057570 scopus 로고    scopus 로고
    • Late onset lattice corneal dystrophy with systemic familial amyloidosis, amyloidosis V, in an English family
    • DOI 10.1136/bjo.84.4.390
    • Stewart HS, Parveen R, Ridgway AE, Bonshek R, Black GC. 2000. Late onset lattice corneal dystrophy with systemic familial amyloidosis, amyloidosis V, in an English family. Br J Ophthalmol 84: 390-394. (Pubitemid 30255488)
    • (2000) British Journal of Ophthalmology , vol.84 , Issue.4 , pp. 390-394
    • Stewart, H.S.1    Parveen, R.2    Ridgway, A.E.3    Bonshek, R.4    Black, G.C.M.5
  • 129
    • 33746355958 scopus 로고    scopus 로고
    • Axonal transport and Alzheimer's disease
    • DOI 10.1146/annurev.biochem.75.103004.142637
    • Stokin GB, Goldstein LS. 2006. Axonal transport and Alzheimer's disease. Annu Rev Biochem 75: 607-627. (Pubitemid 44118045)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 607-627
    • Stokin, G.B.1    Goldstein, L.S.B.2
  • 130
    • 33144470924 scopus 로고    scopus 로고
    • Heparin accelerates gelsolin amyloidogenesis
    • DOI 10.1021/bi0519295
    • Suk JY, Zhang F, Balch WE, Linhardt RJ, Kelly JW. 2006. Heparin accelerates gelsolin amyloidogenesis. Biochemistry 45: 2234-2242. (Pubitemid 43271322)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2234-2242
    • Suk, J.Y.1    Zhang, F.2    Balch, W.E.3    Linhardt, R.J.4    Kelly, J.W.5
  • 132
    • 33947627069 scopus 로고    scopus 로고
    • Severe ataxia with neuropathy in hereditary gelsolin amyloidosis: A case report
    • DOI 10.1080/13506120601116393, PII 775701311
    • Tanskanen M, Paetau A, Salonen O, Salmi T, Lamminen A, Lindsberg P, Somer H, Kiuru-Enari S. 2007. Severe ataxia with neuropathy in hereditary gelsolin amyloidosis: a case report. Amyloid 14: 89-95. (Pubitemid 46491167)
    • (2007) Amyloid , vol.14 , Issue.1 , pp. 89-95
    • Tanskanen, M.1    Paetau, A.2    Salonen, O.3    Salmi, T.4    Lamminen, A.5    Lindsberg, P.6    Somer, H.7    Kiuru-Enari, S.8
  • 133
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • DOI 10.1016/j.cell.2005.02.008
    • Tanzi RE, Bertram L. 2005. Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120: 545-555. (Pubitemid 40269768)
    • (2005) Cell , vol.120 , Issue.4 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 134
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • DOI 10.1021/bi027378p
    • Tycko R. 2003. Insights into the amyloid folding problem from solidstate NMR. Biochemistry 42: 3151-3159. (Pubitemid 36348623)
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3151-3159
    • Tycko, R.1
  • 135
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ. 2002. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539. (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 136
    • 34248190279 scopus 로고    scopus 로고
    • A β oligomers-A decade of discovery
    • Walsh DM, Selkoe DJ. 2007. A β oligomers-a decade of discovery. J Neurochem 101: 1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 139
    • 0029785996 scopus 로고    scopus 로고
    • The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure
    • DOI 10.1021/bi960920n
    • Wen D, Corina K, Chow EP, Miller S, Janmey PA, Pepinsky RB. 1996. The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure. Biochemistry 35: 9700-9709. (Pubitemid 26302982)
    • (1996) Biochemistry , vol.35 , Issue.30 , pp. 9700-9709
    • Wen, D.1    Corina, K.2    Pingchang Chow, E.3    Miller, S.4    Janmey, P.A.5    Blake Pepinsky, R.6
  • 140
    • 36049032748 scopus 로고    scopus 로고
    • An adaptable standard for protein export from the endoplasmic reticulum
    • DOI 10.1016/j.cell.2007.10.025, PII S0092867407013438
    • Wiseman RL, Powers ET, Buxbaum JN, Kelly JW, Balch WE. 2007. An adaptable standard for protein export from the endoplasmic reticulum. Cell 131: 809-821. (Pubitemid 350087203)
    • (2007) Cell , vol.131 , Issue.4 , pp. 809-821
    • Wiseman, R.L.1    Powers, E.T.2    Buxbaum, J.N.3    Kelly, J.W.4    Balch, W.E.5
  • 141
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke W, Sharpe AH, Hartwig JH, Azuma T, Stossel TP, Kwiatkowski DJ. 1995. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell 81: 41-51.
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 143
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • DOI 10.1038/281583a0
    • Yin HL, Stossel TP. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281: 583-586. (Pubitemid 10242871)
    • (1979) Nature , vol.281 , Issue.5732 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2
  • 144
    • 33846265304 scopus 로고    scopus 로고
    • Isofagomine- and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for gaucher disease intervention
    • DOI 10.1021/jm060677i
    • Yu Z, Sawkar AR, Whalen LJ, Wong CH, Kelly JW. 2007. Isofagomine-and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention. J Med Chem 50: 94-100. (Pubitemid 46105502)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.1 , pp. 94-100
    • Yu, Z.1    Sawkar, A.R.2    Whalen, L.J.3    Wong, C.-H.4    Kelly, J.W.5
  • 145
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou A, Webb G, Zhu X, Steiner DF. 1999. Proteolytic processing in the secretory pathway. J Biol Chem 274: 20745-20748.
    • (1999) J Biol Chem , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.