메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

Proteomic analysis of highly prevalent amyloid a amyloidosis endemic to endangered Island foxes

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; APOLIPOPROTEIN A4; APOLIPOPROTEIN E; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C4; FIBRINOGEN; SERUM AMYLOID A;

EID: 84956608536     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0113765     Document Type: Article
Times cited : (16)

References (73)
  • 1
    • 0017237001 scopus 로고
    • Amyloid fibril protein AA: Purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay
    • Sipe JD, Ignaczak TF, Pollock PS, Glenner GG. (1976) Amyloid fibril protein AA: purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay. J Immunol. 116: 1151-1156.
    • (1976) J Immunol. , vol.116 , pp. 1151-1156
    • Sipe, J.D.1    Ignaczak, T.F.2    Pollock, P.S.3    Glenner, G.G.4
  • 3
    • 0022995862 scopus 로고
    • Structure of the murine serum amyloid A gene family. Gene conversion
    • Lowell CA, Potter DA, Stearman RS, Morrow JF. (1986) Structure of the murine serum amyloid A gene family. Gene conversion. J Biol Chem. 261: 8442-8452.
    • (1986) J Biol Chem. , vol.261 , pp. 8442-8452
    • Lowell, C.A.1    Potter, D.A.2    Stearman, R.S.3    Morrow, J.F.4
  • 4
    • 0025368248 scopus 로고
    • AA-amyloidosis. Tissue componentspecific association of various protein AA subspecies and evidence of a fourth SAA gene product
    • Westermark GT, Sletten K, Grubb A, Westermark P. (1990) AA-amyloidosis. Tissue componentspecific association of various protein AA subspecies and evidence of a fourth SAA gene product. Am J Pathol. 137: 377-383.
    • (1990) Am J Pathol. , vol.137 , pp. 377-383
    • Westermark, G.T.1    Sletten, K.2    Grubb, A.3    Westermark, P.4
  • 5
    • 27644549634 scopus 로고    scopus 로고
    • Essential role of STAT3 in cytokine-driven NF-kappaB-mediated serum amyloid A gene expression
    • Hagihara K, Nishikawa T, Sugamata Y, Song J, Isobe T, et al. (2005) Essential role of STAT3 in cytokine-driven NF-kappaB-mediated serum amyloid A gene expression. Genes Cells. 10: 1051-1063.
    • (2005) Genes Cells , vol.10 , pp. 1051-1063
    • Hagihara, K.1    Nishikawa, T.2    Sugamata, Y.3    Song, J.4    Isobe, T.5
  • 7
    • 0017145750 scopus 로고
    • Murine model for human secondary amyloidosis: Genetic variability of the acute-phase serum protein SAA response to endotoxins and casein
    • McAdam KP, Sipe JD. (1976) Murine model for human secondary amyloidosis: genetic variability of the acute-phase serum protein SAA response to endotoxins and casein. J Exp Med. 144: 1121-1127.
    • (1976) J Exp Med. , vol.144 , pp. 1121-1127
    • McAdam, K.P.1    Sipe, J.D.2
  • 8
    • 0035822274 scopus 로고    scopus 로고
    • Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein
    • Gillmore JD, Lovat LB, Persey MR, Pepys MB, Hawkins PN. (2001) Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein. Lancet. 358: 24-29.
    • (2001) Lancet. , vol.358 , pp. 24-29
    • Gillmore, J.D.1    Lovat, L.B.2    Persey, M.R.3    Pepys, M.B.4    Hawkins, P.N.5
  • 9
    • 0033569982 scopus 로고    scopus 로고
    • Serum amyloid A, the major vertebrate acute-phase reactant
    • Uhlar CM, Whitehead AS. (1999) Serum amyloid A, the major vertebrate acute-phase reactant. European Journal of Biochemistry. 265: 501-523.
    • (1999) European Journal of Biochemistry , vol.265 , pp. 501-523
    • Uhlar, C.M.1    Whitehead, A.S.2
  • 10
    • 84898028057 scopus 로고    scopus 로고
    • Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis
    • Lu J, Yu Y, Zhu I, Cheng Y, Sun PD. (2014) Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis. Proc Natl Acad Sci U S A. 111: 5189-5194.
    • (2014) Proc Natl Acad Sci U S A. , vol.111 , pp. 5189-5194
    • Lu, J.1    Yu, Y.2    Zhu, I.3    Cheng, Y.4    Sun, P.D.5
  • 11
    • 0029777342 scopus 로고    scopus 로고
    • Expression of recombinant human serum amyloid A in mammalian cells and demonstration of the region necessary for high-density lipoprotein binding and amyloid fibril formation by site-directed mutagenesis
    • Patel H, Bramall J, Waters H, De Beer MC, Woo P. (1996) Expression of recombinant human serum amyloid A in mammalian cells and demonstration of the region necessary for high-density lipoprotein binding and amyloid fibril formation by site-directed mutagenesis. Biochem J. 318 (Pt 3): 1041-1049.
    • (1996) Biochem J. , vol.318 , Issue.3 , pp. 1041-1049
    • Patel, H.1    Bramall, J.2    Waters, H.3    De Beer, M.C.4    Woo, P.5
  • 12
    • 70349661239 scopus 로고    scopus 로고
    • Heparan sulfate promotes the aggregation of HDLassociated serum amyloid A: Evidence for a proamyloidogenic histidine molecular switch
    • Elimova E, Kisilevsky R, Ancsin JB. (2009) Heparan sulfate promotes the aggregation of HDLassociated serum amyloid A: evidence for a proamyloidogenic histidine molecular switch. FASEB Journal. 23: 3436-3448.
    • (2009) FASEB Journal. , vol.23 , pp. 3436-3448
    • Elimova, E.1    Kisilevsky, R.2    Ancsin, J.B.3
  • 13
    • 9444263075 scopus 로고    scopus 로고
    • Amyloidogenesis recapitulated in cell culture: A peptide inhibitor provides direct evidence for the role of heparan sulfate and suggests a new treatment strategy
    • Elimova E, Kisilevsky R, Szarek WA, Ancsin JB. (2004) Amyloidogenesis recapitulated in cell culture: a peptide inhibitor provides direct evidence for the role of heparan sulfate and suggests a new treatment strategy. FASEB Journal. 18: 1749-1751.
    • (2004) FASEB Journal. , vol.18 , pp. 1749-1751
    • Elimova, E.1    Kisilevsky, R.2    Szarek, W.A.3    Ancsin, J.B.4
  • 14
    • 0026555175 scopus 로고
    • The N-terminal segment of protein AA determines its fibrillogenic property
    • Westermark GT, Engstrom U, Westermark P. (1992) The N-terminal segment of protein AA determines its fibrillogenic property. Biochem Biophys Res Commun. 182: 27-33.
    • (1992) Biochem Biophys Res Commun. , vol.182 , pp. 27-33
    • Westermark, G.T.1    Engstrom, U.2    Westermark, P.3
  • 15
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequencedependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L. (2004) Prediction of sequencedependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol. 22: 1302-1306.
    • (2004) Nat Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 17
    • 0021909988 scopus 로고
    • Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo
    • Husebekk A, Skogen B, Husby G, Marhaug G. (1985) Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scand J Immunol. 21: 283-287.
    • (1985) Scand J Immunol. , vol.21 , pp. 283-287
    • Husebekk, A.1    Skogen, B.2    Husby, G.3    Marhaug, G.4
  • 18
    • 19544366084 scopus 로고    scopus 로고
    • Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: Cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation
    • Rocken C, Menard R, Buhling F, Vockler S, Raynes J, et al. (2005) Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation. Ann Rheum Dis. 64: 808-815.
    • (2005) Ann Rheum Dis. , vol.64 , pp. 808-815
    • Rocken, C.1    Menard, R.2    Buhling, F.3    Vockler, S.4    Raynes, J.5
  • 19
    • 0028833148 scopus 로고
    • Characterization of amyloid A protein in human secondary amyloidosis: The predominant deposition of serum amyloid A1
    • Liepnieks JJ, Kluve-Beckerman B, Benson MD. (1995) Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum amyloid A1. Biochim Biophys Acta. 1270: 81-86.
    • (1995) Biochim Biophys Acta. , vol.1270 , pp. 81-86
    • Liepnieks, J.J.1    Kluve-Beckerman, B.2    Benson, M.D.3
  • 20
    • 0037388591 scopus 로고    scopus 로고
    • The contribution of genotypes at the MEFV and SAA1 loci to amyloidosis and disease severity in patients with familial Mediterranean fever
    • Gershoni-Baruch R, Brik R, Zacks N, Shinawi M, Lidar M, et al. (2003) The contribution of genotypes at the MEFV and SAA1 loci to amyloidosis and disease severity in patients with familial Mediterranean fever. Arthritis Rheum. 48: 1149-1155.
    • (2003) Arthritis Rheum. , vol.48 , pp. 1149-1155
    • Gershoni-Baruch, R.1    Brik, R.2    Zacks, N.3    Shinawi, M.4    Lidar, M.5
  • 21
    • 21244461521 scopus 로고    scopus 로고
    • Relative transcriptional activities of SAA1 promoters polymorphic at position 213(T/C): Potential association between increased transcription and amyloidosis
    • Moriguchi M, Kaneko H, Terai C, Koseki Y, Kajiyama H, et al. (2005) Relative transcriptional activities of SAA1 promoters polymorphic at position 213(T/C): potential association between increased transcription and amyloidosis. Amyloid. 12: 26-32.
    • (2005) Amyloid. , vol.12 , pp. 26-32
    • Moriguchi, M.1    Kaneko, H.2    Terai, C.3    Koseki, Y.4    Kajiyama, H.5
  • 22
    • 0032855777 scopus 로고    scopus 로고
    • Influence of genotypes at SAA1 and SAA2 loci on the development and the length of latent period of secondary AA-amyloidosis in patients with rheumatoid arthritis
    • Moriguchi M, Terai C, Koseki Y, Uesato M, Nakajima A, et al. (1999) Influence of genotypes at SAA1 and SAA2 loci on the development and the length of latent period of secondary AA-amyloidosis in patients with rheumatoid arthritis. Human Genetics. 105: 360-366.
    • (1999) Human Genetics. , vol.105 , pp. 360-366
    • Moriguchi, M.1    Terai, C.2    Koseki, Y.3    Uesato, M.4    Nakajima, A.5
  • 24
    • 0031261382 scopus 로고    scopus 로고
    • Systemic AA amyloidosis in captive cheetahs (Acinonyx jubatus)
    • Papendick RE, Munson L, O'Brien TD, Johnson KH. (1997) Systemic AA amyloidosis in captive cheetahs (Acinonyx jubatus). Vet Path. 34: 549-556.
    • (1997) Vet Path. , vol.34 , pp. 549-556
    • Papendick, R.E.1    Munson, L.2    O'Brien, T.D.3    Johnson, K.H.4
  • 25
    • 44449097903 scopus 로고    scopus 로고
    • Characterization of the cheetah serum amyloid A1 gene: Critical role and functional polymorphism of a cis-acting element
    • Zhang B, Une Y, Ge F, Fu X, Qian J, et al. (2008) Characterization of the cheetah serum amyloid A1 gene: Critical role and functional polymorphism of a cis-acting element. J Heredity. 99: 355-363.
    • (2008) J Heredity. , vol.99 , pp. 355-363
    • Zhang, B.1    Une, Y.2    Ge, F.3    Fu, X.4    Qian, J.5
  • 26
    • 0025321553 scopus 로고
    • Genetic fingerprinting reflects population differentiation in the California Channel Island fox
    • Gilbert DA, Lehman N, O'Brien SJ, Wayne RK . (1990) Genetic fingerprinting reflects population differentiation in the California Channel Island fox. Nature. 344: 764-767.
    • (1990) Nature. , vol.344 , pp. 764-767
    • Gilbert, D.A.1    Lehman, N.2    O'Brien, S.J.3    Wayne, R.K.4
  • 27
    • 84885573368 scopus 로고    scopus 로고
    • Shotgun-proteomics-based clinical testing for diagnosis and classification of amyloidosis
    • Theis JD, Dasari S, Vrana JA, Kurtin PJ, Dogan A. (2013) Shotgun-proteomics-based clinical testing for diagnosis and classification of amyloidosis. J Mass Spec. 48: 1067-1077.
    • (2013) J Mass Spec. , vol.48 , pp. 1067-1077
    • Theis, J.D.1    Dasari, S.2    Vrana, J.A.3    Kurtin, P.J.4    Dogan, A.5
  • 28
    • 73949091104 scopus 로고    scopus 로고
    • Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens
    • Vrana JA, Gamez JD, Madden BJ, Theis JD, Bergen HR, 3rd, et al. (2009) Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens. Blood. 114: 4957-4959.
    • (2009) Blood. , vol.114 , pp. 4957-4959
    • Vrana, J.A.1    Gamez, J.D.2    Madden, B.J.3    Theis, J.D.4    Bergen, H.R.5
  • 29
    • 14844324838 scopus 로고    scopus 로고
    • Listing the San Miquel Island Fox, Santa Rosa Island Fox, Santa Cruz Island Fox, and Santa Catalina Island Fox as Endangered. Department of the Interior Fish and Wildlife Service, Federal Register: Rules and Regulations CFR Part
    • Williams S. (2004) Endangered and Threatened Wildlife and Plants; Listing the San Miquel Island Fox, Santa Rosa Island Fox, Santa Cruz Island Fox, and Santa Catalina Island Fox as Endangered. Department of the Interior Fish and Wildlife Service, Federal Register: Rules and Regulations: Vol 69, 50 CFR Part 17, pp. 10335-10353.
    • (2004) Endangered and Threatened Wildlife and Plants , vol.69 , Issue.50 , pp. 10335-10353
    • Williams, S.1
  • 30
    • 84950288787 scopus 로고    scopus 로고
    • California Department of Fish and Wildlife, the Natural Resources Agency, California Natural Diveristy Database:Mammals
    • (2014) State and federally listed endangered and threatened animals of California. California Department of Fish and Wildlife, The Natural Resources Agency, California Natural Diveristy Database:Mammals. pp. 12.
    • (2014) State and Federally Listed Endangered and Threatened Animals of California , pp. 12
  • 31
    • 0021777826 scopus 로고
    • AA-amyloidosis in dogs: Partial amino acid sequence of protein AA and immunohistochemical cross-reactivity with human and cow AA-amyloid
    • Westermark P, Johnson KH, Sletten K, Hayden DW. (1985) AA-amyloidosis in dogs: partial amino acid sequence of protein AA and immunohistochemical cross-reactivity with human and cow AA-amyloid. Comp Biochem Physiol B. 82: 211-215.
    • (1985) Comp Biochem Physiol B. , vol.82 , pp. 211-215
    • Westermark, P.1    Johnson, K.H.2    Sletten, K.3    Hayden, D.W.4
  • 32
    • 0002812025 scopus 로고
    • AA amyloidosis in Chinese Shar-pei dogs: Immunohistochemical and amino acid sequence analyses
    • Johnson KH, Sletten K, Hayden DW, O'Brien TD, Rossow KD, et al. (1995) AA amyloidosis in Chinese Shar-pei dogs: Immunohistochemical and amino acid sequence analyses. Amyloid. 2: 92-99.
    • (1995) Amyloid. , vol.2 , pp. 92-99
    • Johnson, K.H.1    Sletten, K.2    Hayden, D.W.3    O'Brien, T.D.4    Rossow, K.D.5
  • 33
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov IV, Seymour SL, Patel AA, Loboda A, Tang WH, et al. (2007) The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol & Cell Proteom. 6: 1638-1655.
    • (2007) Mol & Cell Proteom. , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5
  • 34
    • 34247642450 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of distinct mammalian Mediator complexes using normalized spectral abundance factors
    • Paoletti AC, Parmely TJ, Tomomori-Sato C, Sato S, Zhu D, et al. (2006) Quantitative proteomic analysis of distinct mammalian Mediator complexes using normalized spectral abundance factors. Proc Natl Acad Sci U S A. 103: 18928-18933.
    • (2006) Proc Natl Acad Sci U S A. , vol.103 , pp. 18928-18933
    • Paoletti, A.C.1    Parmely, T.J.2    Tomomori-Sato, C.3    Sato, S.4    Zhu, D.5
  • 35
    • 85000053610 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y. (1995) Controlling the false discovery rate: A practical and powerful approach to multiple testing. J Royal Stat Soc Series B. 57: 289-300.
    • (1995) J Royal Stat Soc Series B. , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 36
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher VG, Tibshirani R, Chu G. (2001) Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci U S A. 98: 5116-5121.
    • (2001) Proc Natl Acad Sci U S A. , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 37
    • 77649265357 scopus 로고    scopus 로고
    • Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
    • Maurer-Stroh S, Debulpaep M, Kuemmerer N, Lopez de la Paz M, Martins IC, et al. (2010) Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nat Methods. 7: 237-242.
    • (2010) Nat Methods. , vol.7 , pp. 237-242
    • Maurer-Stroh, S.1    Debulpaep, M.2    Kuemmerer, N.3    Lopez De La Paz, M.4    Martins, I.C.5
  • 39
    • 1542681892 scopus 로고    scopus 로고
    • Secondary amyloidosis in patients with rheumatoid arthritis: Diagnostic and prognostic value of gastroduodenal biopsy
    • Kobayashi H, Tada S, Fuchigami T, Okuda Y, Takasugi K, et al. (1996) Secondary amyloidosis in patients with rheumatoid arthritis: diagnostic and prognostic value of gastroduodenal biopsy. Br J Rheumatol. 35: 44-49.
    • (1996) Br J Rheumatol. , vol.35 , pp. 44-49
    • Kobayashi, H.1    Tada, S.2    Fuchigami, T.3    Okuda, Y.4    Takasugi, K.5
  • 40
    • 0028084977 scopus 로고
    • Cause of death in 81 autopsied patients with rheumatoid arthritis
    • Suzuki A, Ohosone Y, Obana M, Mita S, Matsuoka Y, et al. (1994) Cause of death in 81 autopsied patients with rheumatoid arthritis. J Rheumatol. 21: 33-36.
    • (1994) J Rheumatol. , vol.21 , pp. 33-36
    • Suzuki, A.1    Ohosone, Y.2    Obana, M.3    Mita, S.4    Matsuoka, Y.5
  • 42
    • 0001611370 scopus 로고
    • Electron microscopic observations on a fibrous component in amyloid of diverse origins
    • Cohen AS, Calkins E. (1959) Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature. 183: 1202-1203.
    • (1959) Nature. , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 43
    • 0033548474 scopus 로고    scopus 로고
    • The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis
    • Ancsin JB, Kisilevsky R. (1999) The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis. J. Biol Chem. 274: 7172-7181.
    • (1999) J. Biol Chem. , vol.274 , pp. 7172-7181
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 44
    • 84863323376 scopus 로고    scopus 로고
    • Laser microdissection and mass spectrometry-based proteomics aids the diagnosis and typing of renal amyloidosis
    • Sethi S, Vrana JA, Theis JD, Leung N, Sethi A, et al. (2012) Laser microdissection and mass spectrometry-based proteomics aids the diagnosis and typing of renal amyloidosis. Kidney Int. 82: 226-234.
    • (2012) Kidney Int. , vol.82 , pp. 226-234
    • Sethi, S.1    Vrana, J.A.2    Theis, J.D.3    Leung, N.4    Sethi, A.5
  • 45
    • 84897501032 scopus 로고    scopus 로고
    • Leukocyte cell-derived chemotaxin 2 (LECT2)-associated amyloidosis is a frequent cause of hepatic amyloidosis in the United States
    • Mereuta OM, Theis JD, Vrana JA, Law ME, Grogg KL, et al. (2014) Leukocyte cell-derived chemotaxin 2 (LECT2)-associated amyloidosis is a frequent cause of hepatic amyloidosis in the United States. Blood. 123: 1479-1482.
    • (2014) Blood. , vol.123 , pp. 1479-1482
    • Mereuta, O.M.1    Theis, J.D.2    Vrana, J.A.3    Law, M.E.4    Grogg, K.L.5
  • 46
    • 56349162661 scopus 로고    scopus 로고
    • Structure and function of inter-alpha-trypsin inhibitor heavy chains
    • Zhuo L, Kimata K. (2008) Structure and function of inter-alpha-trypsin inhibitor heavy chains. Connect Tissue Res. 49: 311-320.
    • (2008) Connect Tissue Res. , vol.49 , pp. 311-320
    • Zhuo, L.1    Kimata, K.2
  • 48
    • 0141480688 scopus 로고    scopus 로고
    • Morbidity and mortality of red foxes (Vulpes vulpes) and gray foxes (Urocyon cinereoargenteus) admitted to the Wildlife Center of Virginia, 1993-2001
    • Kelly TR, Sleeman JM. (2003) Morbidity and mortality of red foxes (Vulpes vulpes) and gray foxes (Urocyon cinereoargenteus) admitted to the Wildlife Center of Virginia, 1993-2001. J Wildl Dis. 39: 467-469.
    • (2003) J Wildl Dis. , vol.39 , pp. 467-469
    • Kelly, T.R.1    Sleeman, J.M.2
  • 49
    • 0035932942 scopus 로고    scopus 로고
    • Prevalence of antibodies to Neospora caninum and Toxoplasma gondii in gray foxes (Urocyon cinereoargenteus) from South Carolina
    • Lindsay DS, Weston JL, Little SE. (2001) Prevalence of antibodies to Neospora caninum and Toxoplasma gondii in gray foxes (Urocyon cinereoargenteus) from South Carolina. Vet Parasitol. 97: 159-164.
    • (2001) Vet Parasitol. , vol.97 , pp. 159-164
    • Lindsay, D.S.1    Weston, J.L.2    Little, S.E.3
  • 50
    • 0026467993 scopus 로고
    • Diseases diagnosed in gray foxes (Urocyon cinereoargenteus) from the southeastern United States
    • Davidson WR, Nettles VF, Hayes LE, Howerth EW, Couvillion CE. (1992) Diseases diagnosed in gray foxes (Urocyon cinereoargenteus) from the southeastern United States. J Wildl Dis. 28: 28-33.
    • (1992) J Wildl Dis. , vol.28 , pp. 28-33
    • Davidson, W.R.1    Nettles, V.F.2    Hayes, L.E.3    Howerth, E.W.4    Couvillion, C.E.5
  • 51
    • 0019418279 scopus 로고
    • Prevalence of selected pathogenic microbial agents in the red fox (Vulpes fulva) and gray fox (Urocyon cinereoargenteus) of southwestern Wisconsin
    • Amundson TE, Yuill TM. (1981) Prevalence of selected pathogenic microbial agents in the red fox (Vulpes fulva) and gray fox (Urocyon cinereoargenteus) of southwestern Wisconsin. J Wildl Dis. 17: 17-22.
    • (1981) J Wildl Dis. , vol.17 , pp. 17-22
    • Amundson, T.E.1    Yuill, T.M.2
  • 52
    • 0041822083 scopus 로고    scopus 로고
    • Prion disease: Horizontal prion transmission in mule deer
    • Miller MW, Williams ES. (2003) Prion disease: horizontal prion transmission in mule deer. Nature. 425: 35-36.
    • (2003) Nature. , vol.425 , pp. 35-36
    • Miller, M.W.1    Williams, E.S.2
  • 54
    • 84878325217 scopus 로고    scopus 로고
    • Experimental induction and oral transmission of avian AA amyloidosis in vaccinated white hens
    • Murakami T, Muhammad N, Inoshima Y, Yanai T, Goryo M, et al. (2013) Experimental induction and oral transmission of avian AA amyloidosis in vaccinated white hens. Amyloid. 20: 80-85.
    • (2013) Amyloid. , vol.20 , pp. 80-85
    • Murakami, T.1    Muhammad, N.2    Inoshima, Y.3    Yanai, T.4    Goryo, M.5
  • 55
    • 44449092737 scopus 로고    scopus 로고
    • Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease
    • Zhang B, Une Y, Fu X, Yan J, Ge F, et al. (2008) Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease. Proc Natl Acad Sci U S A. 105: 7263-7268.
    • (2008) Proc Natl Acad Sci U S A. , vol.105 , pp. 7263-7268
    • Zhang, B.1    Une, Y.2    Fu, X.3    Yan, J.4    Ge, F.5
  • 56
    • 44449102871 scopus 로고    scopus 로고
    • Are cheetahs on the run from prion-like amyloidosis?
    • Caughey B, Baron GS. (2008) Are cheetahs on the run from prion-like amyloidosis? Proc Natl Acad Sci U S A. 105: 7113-7114.
    • (2008) Proc Natl Acad Sci U S A. , vol.105 , pp. 7113-7114
    • Caughey, B.1    Baron, G.S.2
  • 57
    • 0027255997 scopus 로고
    • Scintigraphic quantification and serial monitoring of human visceral amyloid deposits provide evidence for turnover and regression
    • Hawkins PN, Richardson S, MacSweeney JE, King AD, Vigushin DM, et al. (1993) Scintigraphic quantification and serial monitoring of human visceral amyloid deposits provide evidence for turnover and regression. Q J Med. 86: 365-374.
    • (1993) Q J Med. , vol.86 , pp. 365-374
    • Hawkins, P.N.1    Richardson, S.2    MacSweeney, J.E.3    King, A.D.4    Vigushin, D.M.5
  • 58
    • 0025025397 scopus 로고
    • Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component
    • Hawkins PN, Lavender JP, Pepys MB. (1990) Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component. N Engl J Med. 323: 508-513.
    • (1990) N Engl J Med. , vol.323 , pp. 508-513
    • Hawkins, P.N.1    Lavender, J.P.2    Pepys, M.B.3
  • 60
    • 0032820892 scopus 로고    scopus 로고
    • Familial amyloidosis in cats:Siamese and Abyssinian AA proteins differ in primary sequence and pattern of deposition
    • Niewold TA, van der Linde-Sipman JS, Murphy C, Tooten PC, Gruys E. (1999) Familial amyloidosis in cats:Siamese and Abyssinian AA proteins differ in primary sequence and pattern of deposition. Amyloid. 6: 205-209.
    • (1999) Amyloid. , vol.6 , pp. 205-209
    • Niewold, T.A.1    Van Der Linde-Sipman, J.S.2    Murphy, C.3    Tooten, P.C.4    Gruys, E.5
  • 61
    • 0026218072 scopus 로고
    • Equine cutaneous amyloidosis derived from an immunoglobulin lambda-light chain. Immunohistochemical, immunochemical and chemical results
    • Linke RP, Geisel O, Mann K. (1991) Equine cutaneous amyloidosis derived from an immunoglobulin lambda-light chain. Immunohistochemical, immunochemical and chemical results. Biol Chem Hoppe Seyler. 372: 835-843.
    • (1991) Biol Chem Hoppe Seyler. , vol.372 , pp. 835-843
    • Linke, R.P.1    Geisel, O.2    Mann, K.3
  • 64
    • 84856427728 scopus 로고    scopus 로고
    • Head and neck amyloidosis:Clinicopathological features and immunohistochemical analysis of 14 cases
    • Gouvea AF, Ribeiro AC, Leon JE, Carlos R, de Almeida OP, et al. (2012) Head and neck amyloidosis:clinicopathological features and immunohistochemical analysis of 14 cases. J Oral Pathol Med. 41: 178-185.
    • (2012) J Oral Pathol Med. , vol.41 , pp. 178-185
    • Gouvea, A.F.1    Ribeiro, A.C.2    Leon, J.E.3    Carlos, R.4    De Almeida, O.P.5
  • 65
    • 33645084269 scopus 로고    scopus 로고
    • Head and neck amyloidosis: A clinicopathologic study of 15 cases
    • Penner CR, Muller S. (2006) Head and neck amyloidosis: a clinicopathologic study of 15 cases. Oral Oncol. 42: 421-429.
    • (2006) Oral Oncol. , vol.42 , pp. 421-429
    • Penner, C.R.1    Muller, S.2
  • 66
    • 0030684085 scopus 로고    scopus 로고
    • A beta amyloidogenesis: Unique, or variation on a systemic theme?
    • Kisilevsky R, Fraser PE. (1997) A beta amyloidogenesis: unique, or variation on a systemic theme? Crit Rev Biochem Mol Biol. 32: 361-404.
    • (1997) Crit Rev Biochem Mol Biol. , vol.32 , pp. 361-404
    • Kisilevsky, R.1    Fraser, P.E.2
  • 67
    • 18144377807 scopus 로고    scopus 로고
    • In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis
    • Li JP, Galvis ML, Gong F, Zhang X, Zcharia E, et al. (2005) In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis. Proc Natl Acad Sci U S A. 102: 6473-6477.
    • (2005) Proc Natl Acad Sci U S A. , vol.102 , pp. 6473-6477
    • Li, J.P.1    Galvis, M.L.2    Gong, F.3    Zhang, X.4    Zcharia, E.5
  • 68
    • 84864105671 scopus 로고    scopus 로고
    • Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation
    • Noborn F, Ancsin JB, Ubhayasekera W, Kisilevsky R, Li JP. (2012) Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation. J Bio Chem. 287: 25669-25677.
    • (2012) J Bio Chem. , vol.287 , pp. 25669-25677
    • Noborn, F.1    Ancsin, J.B.2    Ubhayasekera, W.3    Kisilevsky, R.4    Li, J.P.5
  • 69
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T, Frangione B. (1992) Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett. 135: 235-238.
    • (1992) Neurosci Lett. , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 70
    • 0029119868 scopus 로고
    • Apolipoprotein E increases the fibrillogenic potential of synthetic peptides derived from Alzheimer's, gelsolin and AA amyloids
    • Soto C, Castano EM, Prelli F, Kumar RA, Baumann M. (1995) Apolipoprotein E increases the fibrillogenic potential of synthetic peptides derived from Alzheimer's, gelsolin and AA amyloids. FEBS Lett. 371: 110-114.
    • (1995) FEBS Lett. , vol.371 , pp. 110-114
    • Soto, C.1    Castano, E.M.2    Prelli, F.3    Kumar, R.A.4    Baumann, M.5
  • 71
    • 0031899218 scopus 로고    scopus 로고
    • Reduction in amyloid A amyloid formation in apolipoprotein-E-deficient mice
    • Kindy MS, Rader DJ. (1998) Reduction in amyloid A amyloid formation in apolipoprotein-E-deficient mice. Am J Pathol. 152: 1387-1395.
    • (1998) Am J Pathol. , vol.152 , pp. 1387-1395
    • Kindy, M.S.1    Rader, D.J.2
  • 72
    • 0030756579 scopus 로고    scopus 로고
    • Amyloid A protein amyloidosis induced in apolipoprotein-E-deficient mice
    • Hoshii Y, Kawano H, Cui D, Takeda T, Gondo T, et al. (1997) Amyloid A protein amyloidosis induced in apolipoprotein-E-deficient mice. Am J Pathol. 151: 911-917.
    • (1997) Am J Pathol. , vol.151 , pp. 911-917
    • Hoshii, Y.1    Kawano, H.2    Cui, D.3    Takeda, T.4    Gondo, T.5
  • 73
    • 84904678185 scopus 로고    scopus 로고
    • Apolipoprotein E in Alzheimer's Disease: An Update
    • Yu JT, Tan L, Hardy J. (2014) Apolipoprotein E in Alzheimer's Disease: An Update. Annu Rev Neurosci. 37: 79-100.
    • (2014) Annu Rev Neurosci. , vol.37 , pp. 79-100
    • Yu, J.T.1    Tan, L.2    Hardy, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.