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Volumn 3, Issue 2, 1996, Pages 75-85

The "edge strand" hypothesis: Prediction and test of a mutational "hot-spot" on the transthyretin molecule associated with FAP amyloidogenesis

Author keywords

Amyloid; Fap; Hot spot; Transthyretin; Variants; Strand

Indexed keywords


EID: 1842589542     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506129609014359     Document Type: Article
Times cited : (38)

References (38)
  • 1
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa P, Figueira A and Bravo F (1978). Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci USA 75, 4499-4503
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4499-4503
    • Costa, P.1    Figueira, A.2    Bravo, F.3
  • 2
    • 0016238506 scopus 로고
    • The amino acid sequence of human plasma prealbumin
    • Kanda Y, Goodman D, Canfield R and Morgan F (1974). The amino acid sequence of human plasma prealbumin. J Biol Chem 249, 6796-6805
    • (1974) J Biol Chem , vol.249 , pp. 6796-6805
    • Kanda, Y.1    Goodman, D.2    Canfield, R.3    Morgan, F.4
  • 3
    • 0017824077 scopus 로고
    • Structure of prealbumin secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8A
    • Blake CCF, Geisow MJ, Oatley SJ, Rerat B and Rerat C (1978). Structure of prealbumin secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8A. J Mol Biol 121, 339-356
    • (1978) J Mol Biol , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 4
    • 0015831649 scopus 로고
    • Binding of thyroxine and thyroxine analogs to human serum prealbumin
    • Edelhoch H, Pages RA and Robbins J (1973). Binding of thyroxine and thyroxine analogs to human serum prealbumin. Biochem 12, 2773-2779
    • (1973) Biochem , vol.12 , pp. 2773-2779
    • Edelhoch, H.1    Pages, R.A.2    Robbins, J.3
  • 5
    • 0002699669 scopus 로고
    • Multiple modes of binding of thyroid hormones and other iodothyronines to human plasma transthyretin
    • John Wiley and Sons Ltd
    • De La Paz P, Burridge JM, Oatley SJ and Blake CCF (1992). Multiple modes of binding of thyroid hormones and other iodothyronines to human plasma transthyretin. In The Design of Drugs to Macromolecular Targets, pp 119-172. (John Wiley and Sons Ltd)
    • (1992) The Design of Drugs to Macromolecular Targets , pp. 119-172
    • De La Paz, P.1    Burridge, J.M.2    Oatley, S.J.3    Blake, C.C.F.4
  • 6
    • 0014690587 scopus 로고
    • The interaction of thyroxine with human plasma prealbumin and with the prealbumin-retinol-binding protein complex
    • Raz A and Goodman DS (1969). The interaction of thyroxine with human plasma prealbumin and with the prealbumin-retinol-binding protein complex. J Biol Chem 244, 3230-3237
    • (1969) J Biol Chem , vol.244 , pp. 3230-3237
    • Raz, A.1    Goodman, D.S.2
  • 7
    • 0029062667 scopus 로고
    • Structure of a complex of 2 plasma-proteins-transthyretin and retinol binding protein
    • Monaco HL, Rizzi M and Coda A (1995). Structure of a complex of 2 plasma-proteins-transthyretin and retinol binding protein. Science 268, 1039-1041
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 8
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva MJM (1995). Transthyretin mutations in health and disease. Human Mutation 5, 191-196
    • (1995) Human Mutation , vol.5 , pp. 191-196
    • Saraiva, M.J.M.1
  • 9
    • 0015441111 scopus 로고
    • Protein volume in solution
    • Zamyatnin AA (1972). Protein volume in solution. In Prog Biophys Mol Biol 24, 107-123
    • (1972) Prog Biophys Mol Biol , vol.24 , pp. 107-123
    • Zamyatnin, A.A.1
  • 11
  • 12
    • 85033750580 scopus 로고
    • Seattle: Statistical Sciences, Inc
    • Statistical Sciences, Inc. (1992). S.PlusProgrammer Manual, Version 3.0, (Seattle: Statistical Sciences, Inc)
    • (1992) S.PlusProgrammer Manual, Version 3.0
  • 14
    • 0022333120 scopus 로고
    • Interactive computer graphics-Frodo
    • Jones TA (1985). Interactive computer graphics-Frodo. Methods in Enz 115, 157-171
    • (1985) Methods in Enz , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 15
    • 2642699794 scopus 로고
    • Rapid and efficient site specific mutagenesis without phenotypic selection
    • Kunkel TA (1985). Rapid and efficient site specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82, 488-492
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 16
    • 0024625363 scopus 로고
    • Efficient site-directed in vitro mutagenesis using phagemid vectors
    • McClary JA, Witney F and Geisselsoder J (1989). Efficient site-directed in vitro mutagenesis using phagemid vectors. Biotechniques 7, 282-289
    • (1989) Biotechniques , vol.7 , pp. 282-289
    • McClary, J.A.1    Witney, F.2    Geisselsoder, J.3
  • 17
  • 21
    • 0024363054 scopus 로고
    • Two simple methods for quantifying low-affinity-dye substrate binding
    • Klunk WE, Pettergrew JW and Abraham DJ (1989). Two simple methods for quantifying low-affinity-dye substrate binding. J Histochem & Cytochem 37, 1293-1297
    • (1989) J Histochem & Cytochem , vol.37 , pp. 1293-1297
    • Klunk, W.E.1    Pettergrew, J.W.2    Abraham, D.J.3
  • 22
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk WE, Pettergrew JW and Abraham DJ (1989). Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem & Cytochem 37, 1273-1281
    • (1989) J Histochem & Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettergrew, J.W.2    Abraham, D.J.3
  • 23
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H (1993). Thioflavine T interaction with synthetic alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Science 2, 404-410
    • (1993) Protein Science , vol.2 , pp. 404-410
    • LeVine, H.1
  • 24
    • 0001733723 scopus 로고
    • Thioflavine T interaction with amyloid β-sheet structures
    • LeVine H (1995). Thioflavine T interaction with amyloid β-sheet structures. Amyloid: Int J Exp Clin Invest 2, 1-6
    • (1995) Amyloid: Int J Exp Clin Invest , vol.2 , pp. 1-6
    • LeVine, H.1
  • 27
    • 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 and Buxbaum JN (1992). Transthyretin Pro55, a variant associated with early onset aggressive, diffuse amyloidosis with cardiac and neurologic involvement. Hum Genet 89, 353-356
    • (1992) Hum Genet , vol.89 , pp. 353-356
    • Jacobson, D.R.1    McFarlin, D.E.2    Kane, I.3    Buxbaum, J.N.4
  • 28
    • 0027363264 scopus 로고
    • Transthyretin mutation Leu55-Pro significantly alters tetramer stability and increases amyloidogenicity
    • McCutchen SL, Colon W and Kelly JW (1993). Transthyretin mutation Leu55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32, 12119-12127
    • (1993) Biochemistry , vol.32 , pp. 12119-12127
    • McCutchen, S.L.1    Colon, W.2    Kelly, J.W.3
  • 30
    • 0017754889 scopus 로고
    • Protein-DNA and protein hormone interaction in prealbumin
    • Blake CCF and Oatley (1977). Protein-DNA and protein hormone interaction in prealbumin. Nature 268, 115-120
    • (1977) Nature , vol.268 , pp. 115-120
    • Blake, C.C.F.1    Oatley2
  • 31
    • 0023696119 scopus 로고
    • Evidence that the amyloid fibrils protein in senile systemic amyloidosis is derived from normal transthyretin
    • Cornwell III GG, Sletten K, Johansson B and Westermark P (1988). Evidence that the amyloid fibrils protein in senile systemic amyloidosis is derived from normal transthyretin. Biochem Biophys Res Commun 154, 648-653
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 648-653
    • Cornwell III, G.G.1    Sletten, K.2    Johansson, B.3    Westermark, P.4
  • 32
    • 0021909227 scopus 로고
    • Prealbumin in Swedish patients with senile systemic amyloidosis and familial amyloidotic poly neuropathy
    • Felding P, Fex G, Westermark P, Olosson BO, Piykänen P and Benson L (1985). Prealbumin in Swedish patients with senile systemic amyloidosis and familial amyloidotic poly neuropathy. Scand J Immunol 21, 133-140
    • (1985) Scand J Immunol , vol.21 , pp. 133-140
    • Felding, P.1    Fex, G.2    Westermark, P.3    Olosson, B.O.4    Piykänen, P.5    Benson, L.6
  • 34
    • 0141715644 scopus 로고
    • Frequency analysis and structural correlation of FAP mutations in transthyretin
    • New York: Parthenon Publishing Group Inc.
    • Serpell LC and Blake CCF (1994). Frequency analysis and structural correlation of FAP mutations in transthyretin. In Amyloid and Amyloidosis, pp 447-450 (New York: Parthenon Publishing Group Inc.)
    • (1994) Amyloid and Amyloidosis , pp. 447-450
    • Serpell, L.C.1    Blake, C.C.F.2
  • 35
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthryretin and β-protein amyloid fibril formation
    • Kelly JW and Lansbury PT (1994). A chemical approach to elucidate the mechanism of transthryretin and β-protein amyloid fibril formation. Amyloid:Int J Exp Clin Invest 1, 186-205
    • (1994) Amyloid:Int J Exp Clin Invest , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury, P.T.2
  • 36
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W and Kelly JW (1992). Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31, 8654-8660
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 37
    • 0016428708 scopus 로고
    • Negative cooperativity in the binding of thyroxine to human serum prealbumin
    • Ferguson RN, Edelhoch H, Saroff HA and Robbins J (1975). Negative cooperativity in the binding of thyroxine to human serum prealbumin. Biochem 14, 282-289
    • (1975) Biochem , vol.14 , pp. 282-289
    • Ferguson, R.N.1    Edelhoch, H.2    Saroff, H.A.3    Robbins, J.4
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24, 946-950
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.