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Volumn 210, Issue 5, 2007, Pages 555-564

Human TRP14 gene homologue from amphioxus Branchiostoma belcheri: Identification, evolution, expression and functional characterization

Author keywords

Amphioxus; Branchiostoma; Evolution; Expression; Thioredoxin related protein

Indexed keywords

AMINO ACID; CELL PROTEIN; CYSTEINE; INSULIN; OXIDOREDUCTASE; PROLINE; PROTEIN TRP14; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34247524096     PISSN: 00218782     EISSN: 14697580     Source Type: Journal    
DOI: 10.1111/j.1469-7580.2007.00722.x     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, et al. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 25, 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 2
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér ESJ, Holmgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267, 6102-6109.
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0346139366 scopus 로고
    • Ovalbumin gene: Evidence for a leader sequence in mRNA and DNA sequences at the exon-intron boundaries
    • Breathnach R, Benoist C, O'Hare K, Cannon F, Chambon P (1978) Ovalbumin gene: Evidence for a leader sequence in mRNA and DNA sequences at the exon-intron boundaries. Proc Natl Acad Sci USA 75, 4853-4857.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4853-4857
    • Breathnach, R.1    Benoist, C.2    O'Hare, K.3    Cannon, F.4    Chambon, P.5
  • 6
    • 0033990096 scopus 로고    scopus 로고
    • DNASTAR's Lasergene sequence analysis software
    • Burland TG (2000) DNASTAR's Lasergene sequence analysis software. Meth Mol Biol 132, 71-91.
    • (2000) Meth Mol Biol , vol.132 , pp. 71-91
    • Burland, T.G.1
  • 8
    • 1542514717 scopus 로고    scopus 로고
    • Thioredoxin system in premature and newborn biology
    • Das KC (2004) Thioredoxin system in premature and newborn biology. Antioxid Redox Signal 6, 405-412.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 405-412
    • Das, K.C.1
  • 9
    • 2342456306 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a glutathione S-transferase from largemouth bass (Micropterus salmoides) liver that is involved in the detoxification of 4-hydroxynonenal
    • Doi AM, Pham RT, Hughes EM, Barber DS, Gallagher EP (2004) Molecular cloning and characterization of a glutathione S-transferase from largemouth bass (Micropterus salmoides) liver that is involved in the detoxification of 4-hydroxynonenal. Biochem Pharmacol 67, 2129-2139.
    • (2004) Biochem Pharmacol , vol.67 , pp. 2129-2139
    • Doi, A.M.1    Pham, R.T.2    Hughes, E.M.3    Barber, D.S.4    Gallagher, E.P.5
  • 10
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund H, Gleason FK, Holmgren A (1991) Structural and functional relations among thioredoxins of different species. Protein 11, 13-28.
    • (1991) Protein , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 12
    • 0036290861 scopus 로고    scopus 로고
    • Thioredoxin superfamily and thioredoxin inducing agents
    • Hirota K, Nakamura H, Masutani H, Yodoi J (2002) Thioredoxin superfamily and thioredoxin inducing agents. Ann NY Acad Sci 957, 189-199.
    • (2002) Ann NY Acad Sci , vol.957 , pp. 189-199
    • Hirota, K.1    Nakamura, H.2    Masutani, H.3    Yodoi, J.4
  • 13
    • 6044221292 scopus 로고    scopus 로고
    • The chordate amphioxus: An emerging model organism for developmental biology
    • Holland LZ, Laudet V, Schubert M (2004) The chordate amphioxus: An emerging model organism for developmental biology. Cell Mol Life Sci 61, 2290-2308.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 2290-2308
    • Holland, L.Z.1    Laudet, V.2    Schubert, M.3
  • 14
    • 0015500758 scopus 로고
    • Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin
    • Holmgren A (1972) Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin. J Biol Chem 247, 1992-1998.
    • (1972) J Biol Chem , vol.247 , pp. 1992-1998
    • Holmgren, A.1
  • 15
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254, 9627-9632.
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 16
    • 0028774178 scopus 로고
    • High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin
    • Jeng MF, Campbell AP, Begley T, et al. (1994) High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2, 853-868.
    • (1994) Structure , vol.2 , pp. 853-868
    • Jeng, M.F.1    Campbell, A.P.2    Begley, T.3
  • 17
    • 0942298136 scopus 로고    scopus 로고
    • Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function
    • Jeong WJ, Yoon HW, Lee SR, Rhee SG (2004a) Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function. J Biol Chem 279, 3142-3150.
    • (2004) J Biol Chem , vol.279 , pp. 3142-3150
    • Jeong, W.J.1    Yoon, H.W.2    Lee, S.R.3    Rhee, S.G.4
  • 18
    • 0942287237 scopus 로고    scopus 로고
    • Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways
    • Jeong WJ, Chang TS, Boja ES, Fales HM, Rhee SG (2004b) Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways. J Biol Chem 279, 3151-3159.
    • (2004) J Biol Chem , vol.279 , pp. 3151-3159
    • Jeong, W.J.1    Chang, T.S.2    Boja, E.S.3    Fales, H.M.4    Rhee, S.G.5
  • 19
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M (1987) An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res 15, 8125-8148.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent TC, Moore EC, Reichard P (1964) Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J Biol Chem 239, 3436-3444.
    • (1964) J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 22
    • 32444441481 scopus 로고    scopus 로고
    • Presence and localization of antithrombin and its regulation after acute lipopolysaccharide exposure in amphioxus, with implications for the origin of vertebrate liver
    • Liang Y, Zhang S, Lun L, Han L (2006) Presence and localization of antithrombin and its regulation after acute lipopolysaccharide exposure in amphioxus, with implications for the origin of vertebrate liver. Cell Tissue Res 323, 537-541.
    • (2006) Cell Tissue Res , vol.323 , pp. 537-541
    • Liang, Y.1    Zhang, S.2    Lun, L.3    Han, L.4
  • 23
    • 0041370109 scopus 로고    scopus 로고
    • Molecular cloning and phylogenetic analysis of AmphiUbf80, a new member of Ubiquitin family from the amphioxus Branchiostoma belcheri tsingtauense
    • Liu Z, Zhang S, Yuan J, Sawant MS, Wei J, Xu A (2002) Molecular cloning and phylogenetic analysis of AmphiUbf80, a new member of Ubiquitin family from the amphioxus Branchiostoma belcheri tsingtauense. Curr Sci 83, 50-53.
    • (2002) Curr Sci , vol.83 , pp. 50-53
    • Liu, Z.1    Zhang, S.2    Yuan, J.3    Sawant, M.S.4    Wei, J.5    Xu, A.6
  • 24
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin JL (1995) Thioredoxin - a fold for all reasons. Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 25
    • 0036869712 scopus 로고    scopus 로고
    • Redox regulation by thioredoxin and its related molecules
    • Matsuo Y, Hirota K, Nakamura H, Yodoi J (2002) Redox regulation by thioredoxin and its related molecules. Drug News Perspect 15, 575-580.
    • (2002) Drug News Perspect , vol.15 , pp. 575-580
    • Matsuo, Y.1    Hirota, K.2    Nakamura, H.3    Yodoi, J.4
  • 26
    • 17644395645 scopus 로고    scopus 로고
    • Thioredoxin and its related molecules: Update 2005
    • Nakamura H (2005) Thioredoxin and its related molecules: Update 2005. Antioxidants Redox Signaling 7, 823-828.
    • (2005) Antioxidants Redox Signaling , vol.7 , pp. 823-828
    • Nakamura, H.1
  • 27
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thiuoredoxin in cell growth and cancer
    • Powis G, Mustacich D, Coon A (2000) The role of the redox protein thiuoredoxin in cell growth and cancer. Free Rad Biol Med 29, 312-322.
    • (2000) Free Rad Biol Med , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 28
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis G, Montfort WR (2001) Properties and biological activities of thioredoxins. Annu Rev Pharmacol Toxicol 41, 261-295.
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 29
    • 0035664149 scopus 로고    scopus 로고
    • Bioinformatic tools for DNA/protein sequence analysis, functional assignment of genes and protein classification
    • Rehm BH (2001) Bioinformatic tools for DNA/protein sequence analysis, functional assignment of genes and protein classification. Appl Microbiol Biotechnol 57, 579-592.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 579-592
    • Rehm, B.H.1
  • 30
    • 0001000501 scopus 로고    scopus 로고
    • The lancelet: Also known as 'amphioxus', this curious creature has returned to the limelight as a player in the phylogenetic history of the vertebrates
    • Stokes MD, Holland ND (1998) The lancelet: Also known as 'amphioxus', this curious creature has returned to the limelight as a player in the phylogenetic history of the vertebrates. Am Sci 86, 552-560.
    • (1998) Am Sci , vol.86 , pp. 552-560
    • Stokes, M.D.1    Holland, N.D.2
  • 31
    • 33845659892 scopus 로고    scopus 로고
    • An evolutionarily conserved 16 kDa thioredoxin-related protein is an antioxidant which regulates the NF-κB signaling pathway
    • Wang XW, Liou YC, Ho B, Ding JL (2007) An evolutionarily conserved 16 kDa thioredoxin-related protein is an antioxidant which regulates the NF-κB signaling pathway. Free Radical Biol Med 42, 247-259.
    • (2007) Free Radical Biol Med , vol.42 , pp. 247-259
    • Wang, X.W.1    Liou, Y.C.2    Ho, B.3    Ding, J.L.4
  • 32
    • 0034681347 scopus 로고    scopus 로고
    • The thioredoxin system of Helicobacter pylori
    • Windle HJ, Fox A, Ni ED, Kelleher D (2000) The thioredoxin system of Helicobacter pylori. J Biol Chem 275, 5081-5089.
    • (2000) J Biol Chem , vol.275 , pp. 5081-5089
    • Windle, H.J.1    Fox, A.2    Ni, E.D.3    Kelleher, D.4
  • 33
    • 9144234217 scopus 로고    scopus 로고
    • Structural basis of cellular redox regulation by human TRP14
    • Woo JR, Kim SJ, Jeong W, et al. (2004) Structural basis of cellular redox regulation by human TRP14. J Biol Chem 279, 48120-48125.
    • (2004) J Biol Chem , vol.279 , pp. 48120-48125
    • Woo, J.R.1    Kim, S.J.2    Jeong, W.3
  • 34
    • 33747349292 scopus 로고    scopus 로고
    • Verification, characterization and tissue-specific expression of UreG, a urease accessory protein gene, from the amphioxus Branchiostoma belcheri
    • Xue JY, Zhang SC, Liu NG, Liu ZH (2006) Verification, characterization and tissue-specific expression of UreG, a urease accessory protein gene, from the amphioxus Branchiostoma belcheri. Acta Biochim Biophys Sin 38, 549-555.
    • (2006) Acta Biochim Biophys Sin , vol.38 , pp. 549-555
    • Xue, J.Y.1    Zhang, S.C.2    Liu, N.G.3    Liu, Z.H.4


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