메뉴 건너뛰기




Volumn 13, Issue 2, 2006, Pages 57-66

R104H may suppress transthyretin amyloidogenesis by thermodynamic stabilization, but not by the kinetic mechanism characterizing T119 interallelic trans-suppression

Author keywords

Amyloidosis; Familial amyloid polyneuropathy; Misfolding; Retinol binding protein; Thyroxine; Trans suppression

Indexed keywords

AMYLOID; ARGININE; HISTIDINE; METHIONINE; MONOMER; PREALBUMIN; TETRAMER; THREONINE;

EID: 33747613353     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.1080/13506120600722449     Document Type: Article
Times cited : (22)

References (31)
  • 1
    • 0034799733 scopus 로고    scopus 로고
    • Transthyretin: A review from a structural perspective
    • Hamilton JA, Benson MD. Transthyretin: a review from a structural perspective. Cell Mol Life Sci 2001;58(10):1491-1521.
    • (2001) Cell Mol Life Sci , vol.58 , Issue.10 , pp. 1491-1521
    • Hamilton, J.A.1    Benson, M.D.2
  • 3
    • 0344074661 scopus 로고    scopus 로고
    • Genotypic-phenotypic variations in a series of 65 patients with familial amyloid polyneuropathy
    • Plante-Bordeneuve V, Lalu T, Misrahi M, Reilly MM, Adams D, Lacroix C, Said G. Genotypic-phenotypic variations in a series of 65 patients with familial amyloid polyneuropathy. Neurology 1998;51(3):708-714.
    • (1998) Neurology , vol.51 , Issue.3 , pp. 708-714
    • Plante-Bordeneuve, V.1    Lalu, T.2    Misrahi, M.3    Reilly, M.M.4    Adams, D.5    Lacroix, C.6    Said, G.7
  • 5
    • 0026612659 scopus 로고
    • Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement
    • Jacobson DR, McFarlin DE, Kane I, Buxbaum JN. Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement. Hum Genet 1992;89(3):353-356.
    • (1992) Hum Genet , vol.89 , Issue.3 , pp. 353-356
    • Jacobson, D.R.1    McFarlin, D.E.2    Kane, I.3    Buxbaum, J.N.4
  • 6
    • 0037046222 scopus 로고    scopus 로고
    • Familial transthyretin-type amyloid polyneuropathy in Japan: Clinical and genetic heterogeneity
    • Ikeda S, Nakazato M, Ando Y, Sobue G. Familial transthyretin-type amyloid polyneuropathy in Japan: clinical and genetic heterogeneity. Neurology 2002;58(7):1001-1007.
    • (2002) Neurology , vol.58 , Issue.7 , pp. 1001-1007
    • Ikeda, S.1    Nakazato, M.2    Ando, Y.3    Sobue, G.4
  • 7
    • 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?
    • Hammarstrom P, Sekijima Y,White JT, Wiseman RL, Lim A, Costello CE, Altland K, Garzuly F, Budka H, Kelly JW. D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis? Biochemistry 2003;42(22):6656-6663.
    • (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
  • 8
    • 0037344272 scopus 로고    scopus 로고
    • Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology
    • Sekijima Y, Hammarstrom P, Matsumura M, Shimizu Y, Iwata M, Tokuda T, Ikeda S, Kelly JW. Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology. Lab Invest 2003;83(3):409-417.
    • (2003) Lab Invest , vol.83 , Issue.3 , pp. 409-417
    • Sekijima, Y.1    Hammarstrom, P.2    Matsumura, M.3    Shimizu, Y.4    Iwata, M.5    Tokuda, T.6    Ikeda, S.7    Kelly, J.W.8
  • 9
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly JW. Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 1997;5(5):595-600.
    • (1997) Structure , vol.5 , Issue.5 , pp. 595-600
    • Kelly, J.W.1
  • 10
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly JW. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 1996;6(1):11-17.
    • (1996) Curr Opin Struct Biol , vol.6 , Issue.1 , pp. 11-17
    • Kelly, J.W.1
  • 11
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W, Kelly JW. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 1992;31(36):8654-8660.
    • (1992) Biochemistry , vol.31 , Issue.36 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 12
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai Z, Colon W, Kelly JW. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 1996;35(20):6470-6482.
    • (1996) Biochemistry , vol.35 , Issue.20 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 13
    • 0033813424 scopus 로고    scopus 로고
    • A glimpse of a possible amyloidogenic intermediate of transthyretin
    • Liu K, Cho HS, Lashuel HA, Kelly JW, Wemmer DE. A glimpse of a possible amyloidogenic intermediate of transthyretin. Nat Struct Biol 2000;7(9):754-757.
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 754-757
    • Liu, K.1    Cho, H.S.2    Lashuel, H.A.3    Kelly, J.W.4    Wemmer, D.E.5
  • 15
    • 0037058942 scopus 로고    scopus 로고
    • Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
    • Hammarstrom P, Jiang X, Hurshman AR, Powers ET, Kelly JW. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proc Natl Acad Sci USA 2002;99(Suppl 4):16427-16432.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.SUPPL. 4 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 16
    • 0001189971 scopus 로고
    • A strikingly benign evolution of FAP in an individual compound heterozygote for two TTR mutations: TTR Met30 and TTR Met119
    • Coelho T, Carvalho M, Saraiva MJ, et al. A strikingly benign evolution of FAP in an individual compound heterozygote for two TTR mutations: TTR Met30 and TTR Met119. J Rheumatol 1993;20:179.
    • (1993) J Rheumatol , vol.20 , pp. 179
    • Coelho, T.1    Carvalho, M.2    Saraiva, M.J.3
  • 17
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • Hammarstrom P, Schneider F, Kelly JW. Trans-suppression of misfolding in an amyloid disease. Science 2001;293(5539):2459-2462.
    • (2001) Science , vol.293 , Issue.5539 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 18
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • Hammarstrom P, Wiseman RL, Powers ET, Kelly JW. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 2003;299(5607):713-716.
    • (2003) Science , vol.299 , Issue.5607 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 20
    • 0028925450 scopus 로고
    • A novel variant of transthyretin, 59Thr-> Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family
    • Booth DR, Tan SY, Hawkins PN, Pepys MB, Frustaci A. A novel variant of transthyretin, 59Thr-> Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family. Circulation 1995;91(4):962-967.
    • (1995) Circulation , vol.91 , Issue.4 , pp. 962-967
    • Booth, D.R.1    Tan, S.Y.2    Hawkins, P.N.3    Pepys, M.B.4    Frustaci, A.5
  • 21
    • 0035997528 scopus 로고    scopus 로고
    • Identification of a novel transthyretin Thr59Lys/Arg104His. A case of compound heterozygosity in a Chinese patient diagnosed with familial transthyretin amyloidosis
    • Lim A, Prokaeva T, Connor LH, Falk RH, Skinner M, Costello CE. Identification of a novel transthyretin Thr59Lys/Arg104His. A case of compound heterozygosity in a Chinese patient diagnosed with familial transthyretin amyloidosis. Amyloid J Protein Folding Dis 2002;9(2):134-140.
    • (2002) Amyloid J Protein Folding Dis , vol.9 , Issue.2 , pp. 134-140
    • Lim, A.1    Prokaeva, T.2    Connor, L.H.3    Falk, R.H.4    Skinner, M.5    Costello, C.E.6
  • 23
    • 0034696835 scopus 로고    scopus 로고
    • Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M
    • Almeida MR, Alves IL, Terazaki H, Ando Y, Saraiva MJ. Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M. Biochem Biophys Res Commun 2000;270(3):1024-1028.
    • (2000) Biochem Biophys Res Commun , vol.270 , Issue.3 , pp. 1024-1028
    • Almeida, M.R.1    Alves, I.L.2    Terazaki, H.3    Ando, Y.4    Saraiva, M.J.5
  • 24
    • 0033550075 scopus 로고    scopus 로고
    • The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
    • Lashuel HA, Wurth C, Woo L, Kelly JW. The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry 1999;38(41):13560-13573.
    • (1999) Biochemistry , vol.38 , Issue.41 , pp. 13560-13573
    • Lashuel, H.A.1    Wurth, C.2    Woo, L.3    Kelly, J.W.4
  • 25
    • 0034919395 scopus 로고    scopus 로고
    • Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins
    • Schneider F, Hammarstrom P, Kelly JW. Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins. Protein Sci 2001;10(8):1606-1613.
    • (2001) Protein Sci , vol.10 , Issue.8 , pp. 1606-1613
    • Schneider, F.1    Hammarstrom, P.2    Kelly, J.W.3
  • 26
    • 0035818516 scopus 로고    scopus 로고
    • Support for the multigenic hypothesis of amyloidosis: The binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro
    • White JT, Kelly JW. Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro. Proc Natl Acad Sci USA 2001;98(23):13019-13024.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.23 , pp. 13019-13024
    • White, J.T.1    Kelly, J.W.2
  • 27
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • Jiang X, Buxbaum JN, Kelly JW. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci USA 2001;98(26):14943-14948.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.26 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 29
    • 0028168367 scopus 로고
    • The Ile-84->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein
    • Berni R, Malpeli G, Folli C, Murrell JR, Liepnieks JJ, Benson MD. The Ile-84->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein. J Biol Chem 1994;269(38):23395-23398.
    • (1994) J Biol Chem , vol.269 , Issue.38 , pp. 23395-23398
    • Berni, R.1    Malpeli, G.2    Folli, C.3    Murrell, J.R.4    Liepnieks, J.J.5    Benson, M.D.6
  • 30
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman A, White JT, Powers ET, Kelly JW. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 2004;43(23):7365-7381.
    • (2004) Biochemistry , vol.43 , Issue.23 , pp. 7365-7381
    • Hurshman, A.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 31
    • 0042848710 scopus 로고    scopus 로고
    • Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions
    • Zhang Q, Kelly JW. Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions. Biochemistry 2003;42(29):8756- 8761.
    • (2003) Biochemistry , vol.42 , Issue.29 , pp. 8756-8761
    • Zhang, Q.1    Kelly, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.