메뉴 건너뛰기




Volumn 81, Issue 8, 2012, Pages 1136-1140

Change in the enzymatic dual function of the peroxiredoxin protein by gamma irradiation

Author keywords

Chaperone; Dual function engineering; Dual functions; Gamma irradiation; Peroxiredoxin

Indexed keywords

CHAPERONE; CHAPERONE ACTIVITY; COVALENTLY CROSS-LINKED; DOSE-DEPENDENT MANNER; DOUBLE PEAK; DUAL FUNCTION; GAMMA IRRADIATION; OLIGOMERIC STRUCTURE; PEROXIDASE ACTIVITIES; PEROXIREDOXIN; SHOULDER PEAKS; STRUCTURAL CHANGE;

EID: 84862808524     PISSN: 0969806X     EISSN: 18790895     Source Type: Journal    
DOI: 10.1016/j.radphyschem.2012.01.019     Document Type: Article
Times cited : (8)

References (26)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA 1994, 91:7017-7021.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 5
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals, II. Modification of amino acids
    • Davies J.A., Delsignore M.E., Lin S.W. Protein damage and degradation by oxygen radicals, II. Modification of amino acids. J. Biol. Chem. 1987, 262:9902-9907.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9902-9907
    • Davies, J.A.1    Delsignore, M.E.2    Lin, S.W.3
  • 7
    • 0034855811 scopus 로고    scopus 로고
    • Chaperone-like activity of alpha-crystallin and other small heat shock proteins
    • Ganea E. Chaperone-like activity of alpha-crystallin and other small heat shock proteins. Curr. Prot. Pept. Sci. 2001, 2:205-225.
    • (2001) Curr. Prot. Pept. Sci. , vol.2 , pp. 205-225
    • Ganea, E.1
  • 8
    • 0035895908 scopus 로고    scopus 로고
    • Phosphorylation-induced change of the oligomerization state of alpha B-crystallin
    • Ito H., Kamei K., Iwamoto I., Inaguma Y., Nohara D., Kato K. Phosphorylation-induced change of the oligomerization state of alpha B-crystallin. J. Biol. Chem. 2001, 276:5346-5352.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5346-5352
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Nohara, D.5    Kato, K.6
  • 9
    • 33646872859 scopus 로고    scopus 로고
    • Structural and functional regulation of eukaryotic 2-Cys peroxiredoxins including the plant ones in cellular defense signaling mechanisms against oxidative stress
    • Jang H.H., Chi Y.H., Park S.K., Lee S.S., Lee J.R., Park J.H., Moon J.C., Lee Y.M., Kim S.Y., Lee K.H., Lee S.Y. Structural and functional regulation of eukaryotic 2-Cys peroxiredoxins including the plant ones in cellular defense signaling mechanisms against oxidative stress. Physiol. Plant. 2006, 126:549-559.
    • (2006) Physiol. Plant. , vol.126 , pp. 549-559
    • Jang, H.H.1    Chi, Y.H.2    Park, S.K.3    Lee, S.S.4    Lee, J.R.5    Park, J.H.6    Moon, J.C.7    Lee, Y.M.8    Kim, S.Y.9    Lee, K.H.10    Lee, S.Y.11
  • 12
    • 0034399152 scopus 로고    scopus 로고
    • A new member of human Tsa/AhpC as thioredoxin-dependent thiol peroxidase
    • Jeong W.J., Cha M.K., Kim I.H. A new member of human Tsa/AhpC as thioredoxin-dependent thiol peroxidase. BMB Rep. 2000, 33:234-241.
    • (2000) BMB Rep. , vol.33 , pp. 234-241
    • Jeong, W.J.1    Cha, M.K.2    Kim, I.H.3
  • 14
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • Korkegian A., Black M.E., Baker D., Stoddard B.L. Computational thermostabilization of an enzyme. Science 2005, 308:857-860.
    • (2005) Science , vol.308 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 15
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G.J., Roseman A.M., Saibil H.R., Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 1997, 16:659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 17
    • 0020564547 scopus 로고
    • Phenol coupling initiated by one-electron oxidation of tyrosine units in peptides and histone
    • Prütz W.A., Butler J., Land E.J. Phenol coupling initiated by one-electron oxidation of tyrosine units in peptides and histone. Int. J. Radiat. Biol. 1983, 44:183-196.
    • (1983) Int. J. Radiat. Biol. , vol.44 , pp. 183-196
    • Prütz, W.A.1    Butler, J.2    Land, E.J.3
  • 18
    • 33750631597 scopus 로고    scopus 로고
    • Chaperone-like activity and hydrophobicity of α-crystallin
    • Reddy B.G.B., Kumar A.P., Kumar S.M. Chaperone-like activity and hydrophobicity of α-crystallin. IUBMB Life 2006, 58:632-641.
    • (2006) IUBMB Life , vol.58 , pp. 632-641
    • Reddy, B.G.B.1    Kumar, A.P.2    Kumar, S.M.3
  • 19
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee S., Chae H., Kim K. Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 2005, 38:1543-1552.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.1    Chae, H.2    Kim, K.3
  • 20
    • 34247159537 scopus 로고    scopus 로고
    • Lipases from extremophiles and potential for industrial applications
    • Salameh M., Wiegel J. Lipases from extremophiles and potential for industrial applications. Adv. Appl. Microbiol. 2007, 61:253-283.
    • (2007) Adv. Appl. Microbiol. , vol.61 , pp. 253-283
    • Salameh, M.1    Wiegel, J.2
  • 21
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid with alpha-crystallin
    • Sharma K.K., Kaur H., Kumar G.S., Kester K. Interaction of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid with alpha-crystallin. J. Biol. Chem. 1998, 273:8965-8970.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8965-8970
    • Sharma, K.K.1    Kaur, H.2    Kumar, G.S.3    Kester, K.4
  • 22
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK
    • Shi L., Palleros D.R., Fink A.L. Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 1994, 33:7536-7546.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 23
    • 34547271956 scopus 로고    scopus 로고
    • The impact of industrial biotechnology
    • Soetaert W., Vandamme E. The impact of industrial biotechnology. Biotechnol. J 2006, 1:756-769.
    • (2006) Biotechnol. J , vol.1 , pp. 756-769
    • Soetaert, W.1    Vandamme, E.2
  • 24
    • 34548210533 scopus 로고    scopus 로고
    • Irradiation of human insulin in aqueous solution, first step towards radiosterilization
    • Terryn H., Maquille A., Houée-Levin C., Tilquin B. Irradiation of human insulin in aqueous solution, first step towards radiosterilization. Int. J. Pharm. 2007, 343:4-11.
    • (2007) Int. J. Pharm. , vol.343 , pp. 4-11
    • Terryn, H.1    Maquille, A.2    Houée-Levin, C.3    Tilquin, B.4
  • 25
    • 21844496983 scopus 로고
    • Food irradiation chemistry and applications
    • Thakur B.R., Singh R.K. Food irradiation chemistry and applications. Food Rev. Int. 1994, 10:437-473.
    • (1994) Food Rev. Int. , vol.10 , pp. 437-473
    • Thakur, B.R.1    Singh, R.K.2
  • 26
    • 1842857567 scopus 로고    scopus 로고
    • Stabilization and re-activation of trapped enzyme by immobilized heat shock protein and molecular chaperones
    • Yang Y., Zeng J., Gao C., Krull U. Stabilization and re-activation of trapped enzyme by immobilized heat shock protein and molecular chaperones. Biosens. Bioelectron. 2003, 18:311-317.
    • (2003) Biosens. Bioelectron. , vol.18 , pp. 311-317
    • Yang, Y.1    Zeng, J.2    Gao, C.3    Krull, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.