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Volumn 582, Issue 19, 2008, Pages 2893-2898

Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli

Author keywords

Amyloid; Cell toxicity; Escherichia coli; Evolution; Protein aggregation; Transthyretin; Transthyretin related protein family

Indexed keywords

PREALBUMIN; SIGNAL PEPTIDE; THYROXINE;

EID: 48749127539     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.07.025     Document Type: Article
Times cited : (6)

References (27)
  • 3
    • 0036910445 scopus 로고    scopus 로고
    • The evolution of transthyretin synthesis in vertebrate liver, in primitive eukaryotes and in bacteria
    • Richardson S.J. The evolution of transthyretin synthesis in vertebrate liver, in primitive eukaryotes and in bacteria. Clin. Chem. Lab. Med. 40 (2002) 1191-1199
    • (2002) Clin. Chem. Lab. Med. , vol.40 , pp. 1191-1199
    • Richardson, S.J.1
  • 4
    • 0030977515 scopus 로고    scopus 로고
    • Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3′ splice site of intron 1)
    • Aldred A.R., Prapunpoj P., and Schreiber G. Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3′ splice site of intron 1). Eur. J. Biochem. 246 (1997) 401-409
    • (1997) Eur. J. Biochem. , vol.246 , pp. 401-409
    • Aldred, A.R.1    Prapunpoj, P.2    Schreiber, G.3
  • 6
    • 0007824822 scopus 로고    scopus 로고
    • Evolution of thyroid hormone binding by transthyretins in birds and mammals
    • Chang L., Munro S.L.A., Richardson S.J., and Schreiber G. Evolution of thyroid hormone binding by transthyretins in birds and mammals. Eur. J. Biochem. 259 (1999) 534-542
    • (1999) Eur. J. Biochem. , vol.259 , pp. 534-542
    • Chang, L.1    Munro, S.L.A.2    Richardson, S.J.3    Schreiber, G.4
  • 7
    • 0031468610 scopus 로고    scopus 로고
    • Analysis of protein domain families in Caenorhabditis elegans
    • Sonnhammer E.L., and Durbin R. Analysis of protein domain families in Caenorhabditis elegans. Genomics 46 (1997) 200-216
    • (1997) Genomics , vol.46 , pp. 200-216
    • Sonnhammer, E.L.1    Durbin, R.2
  • 8
    • 0034684193 scopus 로고    scopus 로고
    • The transthyretin-retinol-binding protein complex
    • Monaco H.L. The transthyretin-retinol-binding protein complex. Biochim. Biophys. Acta 1482 (2000) 65-72
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 65-72
    • Monaco, H.L.1
  • 9
    • 0033639180 scopus 로고    scopus 로고
    • Evolution of structure, ontogeny of gene expression, and function of Xenopus laevis transthyretin
    • Prapunpoj P., Yamauchi K., Nishiyama N., Richardson S.J., and Schreiber G. Evolution of structure, ontogeny of gene expression, and function of Xenopus laevis transthyretin. Am. J. Physiol. 279 (2000) 2026-2041
    • (2000) Am. J. Physiol. , vol.279 , pp. 2026-2041
    • Prapunpoj, P.1    Yamauchi, K.2    Nishiyama, N.3    Richardson, S.J.4    Schreiber, G.5
  • 10
    • 0036801304 scopus 로고    scopus 로고
    • The evolutionary and integrative roles of transthyretin in thyroid hormone homeostasis
    • Schreiber G. The evolutionary and integrative roles of transthyretin in thyroid hormone homeostasis. J. Endocrinol. 175 (2002) 61-73
    • (2002) J. Endocrinol. , vol.175 , pp. 61-73
    • Schreiber, G.1
  • 11
    • 33748475698 scopus 로고    scopus 로고
    • Structural and functional evolution of transthyretin and transthyretin-like proteins
    • Hennebry S.C., Wright H.M., Likic V.A., and Richardson S.J. Structural and functional evolution of transthyretin and transthyretin-like proteins. Proteins 64 (2006) 1024-1045
    • (2006) Proteins , vol.64 , pp. 1024-1045
    • Hennebry, S.C.1    Wright, H.M.2    Likic, V.A.3    Richardson, S.J.4
  • 12
    • 4544236639 scopus 로고    scopus 로고
    • The Arabidopsis transthyretin-like protein is a potential substrate of brassinosteroid-insensitive 1
    • Nam K.H., and Li J. The Arabidopsis transthyretin-like protein is a potential substrate of brassinosteroid-insensitive 1. Plant Cell 16 (2004) 2406-2417
    • (2004) Plant Cell , vol.16 , pp. 2406-2417
    • Nam, K.H.1    Li, J.2
  • 13
    • 0035031537 scopus 로고    scopus 로고
    • Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator
    • Schultz A.C., Nygaard P., and Saxild H.H. Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J. Bacteriol. 183 (2001) 3293-3302
    • (2001) J. Bacteriol. , vol.183 , pp. 3293-3302
    • Schultz, A.C.1    Nygaard, P.2    Saxild, H.H.3
  • 14
    • 33745618437 scopus 로고    scopus 로고
    • Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family
    • Jung D.K., Lee Y., Park S.G., Park B.C., Kim G.H., and Rhee S. Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family. Proc. Natl. Acad. Sci. USA 103 (2006) 9790-9795
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9790-9795
    • Jung, D.K.1    Lee, Y.2    Park, S.G.3    Park, B.C.4    Kim, G.H.5    Rhee, S.6
  • 15
    • 24044525647 scopus 로고    scopus 로고
    • Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction
    • Lee Y., Lee D.H., Kho C.W., Lee A.Y., Jang M., Cho S., Lee C.H., Lee J.S., Myung P.K., Park B.C., and Park S.G. Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett. 579 (2005) 4769-4774
    • (2005) FEBS Lett. , vol.579 , pp. 4769-4774
    • Lee, Y.1    Lee, D.H.2    Kho, C.W.3    Lee, A.Y.4    Jang, M.5    Cho, S.6    Lee, C.H.7    Lee, J.S.8    Myung, P.K.9    Park, B.C.10    Park, S.G.11
  • 16
    • 33745231703 scopus 로고    scopus 로고
    • The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase
    • Hennebry S.C., Law R.H., Richardson S.J., Buckle A.M., and Whisstock J.C. The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase. J. Mol. Biol. 359 (2006) 1389-1399
    • (2006) J. Mol. Biol. , vol.359 , pp. 1389-1399
    • Hennebry, S.C.1    Law, R.H.2    Richardson, S.J.3    Buckle, A.M.4    Whisstock, J.C.5
  • 18
    • 33847635267 scopus 로고    scopus 로고
    • Mouse transthyretin-related protein is a hydrolase which degrades 5-hydroxyisourate, the end product of the uricase reaction
    • Lee Y., Park B.C., Lee do H., Bae K.H., Cho S., Lee C.H., Lee J.S., Myung P.K., and Park S.G. Mouse transthyretin-related protein is a hydrolase which degrades 5-hydroxyisourate, the end product of the uricase reaction. Mol. Cell 22 (2006) 141-145
    • (2006) Mol. Cell , vol.22 , pp. 141-145
    • Lee, Y.1    Park, B.C.2    Lee do, H.3    Bae, K.H.4    Cho, S.5    Lee, C.H.6    Lee, J.S.7    Myung, P.K.8    Park, S.G.9
  • 19
    • 16744366300 scopus 로고    scopus 로고
    • 'In vitro' amyloid fibril formation from transthyretin: the influence of ions and the amyloidogenicity of TTR variants
    • Bonifacio M.J., Sakaki Y., and Saraiva M.J. 'In vitro' amyloid fibril formation from transthyretin: the influence of ions and the amyloidogenicity of TTR variants. Biochim. Biophys. Acta 1316 (1996) 35-42
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 35-42
    • Bonifacio, M.J.1    Sakaki, Y.2    Saraiva, M.J.3
  • 20
    • 0036295080 scopus 로고    scopus 로고
    • Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils
    • Cardoso I., Goldsbury C.S., Muller S.A., Olivieri V., Wirtz S., Damas A.M., Aebi U., and Saraiva M.J. Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. J. Mol. Biol. 317 (2002) 683-695
    • (2002) J. Mol. Biol. , vol.317 , pp. 683-695
    • Cardoso, I.1    Goldsbury, C.S.2    Muller, S.A.3    Olivieri, V.4    Wirtz, S.5    Damas, A.M.6    Aebi, U.7    Saraiva, M.J.8
  • 21
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates
    • Sousa M.M., Cardoso I., Fernandes R., Guimaraes A., and Saraiva M.J. Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am. J. Pathol. 159 (2001) 1993-2000
    • (2001) Am. J. Pathol. , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 22
    • 33748788511 scopus 로고    scopus 로고
    • The transthyretin-related protein: structural investigation of a novel protein family
    • Lundberg E., Backstrom S., Sauer U.H., and Sauer-Eriksson A.E. The transthyretin-related protein: structural investigation of a novel protein family. J. Struct. Biol. 155 (2006) 445-457
    • (2006) J. Struct. Biol. , vol.155 , pp. 445-457
    • Lundberg, E.1    Backstrom, S.2    Sauer, U.H.3    Sauer-Eriksson, A.E.4
  • 24
    • 34250305540 scopus 로고    scopus 로고
    • Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria
    • Oh J., Kim J.G., Jeon E., Yoo C.H., Moon J.S., Rhee S., and Hwang I. Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria. J. Biol. Chem. 282 (2007) 13601-13609
    • (2007) J. Biol. Chem. , vol.282 , pp. 13601-13609
    • Oh, J.1    Kim, J.G.2    Jeon, E.3    Yoo, C.H.4    Moon, J.S.5    Rhee, S.6    Hwang, I.7
  • 25
    • 0037022681 scopus 로고    scopus 로고
    • Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines
    • Hetz C., Bono M.R., Barros L.F., and Lagos R. Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines. Proc. Natl. Acad. Sci. USA 99 (2002) 2696-2701
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2696-2701
    • Hetz, C.1    Bono, M.R.2    Barros, L.F.3    Lagos, R.4
  • 26
    • 22844451606 scopus 로고    scopus 로고
    • Amyloid formation modulates the biological activity of a bacterial protein
    • Bieler S., Estrada L., Lagos R., Baeza M., Castilla J., and Soto C. Amyloid formation modulates the biological activity of a bacterial protein. J. Biol. Chem. 280 (2005) 26880-26885
    • (2005) J. Biol. Chem. , vol.280 , pp. 26880-26885
    • Bieler, S.1    Estrada, L.2    Lagos, R.3    Baeza, M.4    Castilla, J.5    Soto, C.6
  • 27
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., and Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. USA 90 (1993) 5011-5015
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6


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