메뉴 건너뛰기




Volumn 37, Issue 4, 2004, Pages 454-462

Multiple oxidative stress-response members of the Adapt78 family

Author keywords

DMEM; Dulbecco's minimal essential medium; FCS; fetal calf serum; HP; hydrogen peroxide; HyperP; hyperphosphorylated; HypoP; hypophosphorylated; lambda phosphatase; LP; Nitrosative stress; NonP; nonphosphorylated; Oxidative stress; PAO; peroxynitrite; phenylarsine; PN

Indexed keywords

ADAPT78 PROTEIN; CALCIUM; GENE PRODUCT; PHOSPHATASE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN; PROTEIN P29; PROTEIN P41; UNCLASSIFIED DRUG;

EID: 3142646774     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.05.014     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0031172775 scopus 로고    scopus 로고
    • Hamster adapt78 mRNA is a Down syndrome critical region homologue that is inducible by oxidative stress
    • Crawford D.R., Leahy K.P., Abramova N., Lan L., Wang Y., Davies K.J.A. Hamster adapt78 mRNA is a Down syndrome critical region homologue that is inducible by oxidative stress. Arch. Biochem. Biophys. 342:1997;6-12
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 6-12
    • Crawford, D.R.1    Leahy, K.P.2    Abramova, N.3    Lan, L.4    Wang, Y.5    Davies, K.J.A.6
  • 3
    • 0034661467 scopus 로고    scopus 로고
    • Adapt78 protects cells against stress damage and suppresses cell growth
    • Leahy K.P., Crawford D.R. adapt78 protects cells against stress damage and suppresses cell growth. Arch. Biochem. Biophys. 379:2000;221-228
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 221-228
    • Leahy, K.P.1    Crawford, D.R.2
  • 8
    • 0030032483 scopus 로고    scopus 로고
    • Hydrogen peroxide induces the expression of adapt15, a novel RNA associated with polysomes in hamster HA-1 cells
    • Crawford D.R., Schools G.P., Salmon S.L., Davies K.J.A. Hydrogen peroxide induces the expression of adapt15, a novel RNA associated with polysomes in hamster HA-1 cells. Arch. Biochem. Biophys. 325:1996;256-264
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 256-264
    • Crawford, D.R.1    Schools, G.P.2    Salmon, S.L.3    Davies, K.J.A.4
  • 11
    • 0343192437 scopus 로고    scopus 로고
    • Identification and characterization of a highly conserved calcineurin binding protein, CBP1/calcipressin, in Cryptococcus neoformans
    • Gorlach J., Fox D.S., Cutler N.S., Cox G.M., Perfect J.R., Heitman J. Identification and characterization of a highly conserved calcineurin binding protein, CBP1/calcipressin, in Cryptococcus neoformans. EMBO J. 19:2000;3618-3629
    • (2000) EMBO J. , vol.19 , pp. 3618-3629
    • Gorlach, J.1    Fox, D.S.2    Cutler, N.S.3    Cox, G.M.4    Perfect, J.R.5    Heitman, J.6
  • 12
    • 0034234963 scopus 로고    scopus 로고
    • A conserved family of calcineurin regulators
    • Kingsbury T.J., Cunningham K.W. A conserved family of calcineurin regulators. Genes Dev. 14:2000;1595-1604
    • (2000) Genes Dev. , vol.14 , pp. 1595-1604
    • Kingsbury, T.J.1    Cunningham, K.W.2
  • 13
    • 0034708825 scopus 로고    scopus 로고
    • A protein encoded within the Down syndrome critical region is enriched in striated muscles and inhibits calcineurin signaling
    • Rothermel B., Vega R.B., Yang J., Wu H., Bassel-Duby R., Williams R.S. A protein encoded within the Down syndrome critical region is enriched in striated muscles and inhibits calcineurin signaling. J. Biol. Chem. 275:2000;8719-8725
    • (2000) J. Biol. Chem. , vol.275 , pp. 8719-8725
    • Rothermel, B.1    Vega, R.B.2    Yang, J.3    Wu, H.4    Bassel-Duby, R.5    Williams, R.S.6
  • 14
  • 15
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak F., Mertz P. Calcineurin: form and function. Physiol. Rev. 80:2000;1483-1521
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 17
    • 0028971035 scopus 로고
    • Calcineurin functions in Ca(2+)-activated cell death in mammalian cells
    • Shibasaki F., McKeon F. Calcineurin functions in Ca(2+)-activated cell death in mammalian cells. J. Cell Biol. 131:1995;735-743
    • (1995) J. Cell Biol. , vol.131 , pp. 735-743
    • Shibasaki, F.1    McKeon, F.2
  • 18
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A., Luo C., Hogan P.G. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 15:1997;707-747
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 22
    • 0030945154 scopus 로고    scopus 로고
    • Cytoskeletal changes in the brains of mice lacking calcineurin a alpha
    • Kayyali U.S., Zhang W., Yee A.G., Seidman J.G., Potter H. Cytoskeletal changes in the brains of mice lacking calcineurin A alpha. J. Neurochem. 68:1997;1668-1678
    • (1997) J. Neurochem. , vol.68 , pp. 1668-1678
    • Kayyali, U.S.1    Zhang, W.2    Yee, A.G.3    Seidman, J.G.4    Potter, H.5
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0034008234 scopus 로고    scopus 로고
    • Modulation of the phosphatase activity of calcineurin by oxidants and antioxidants in vitro
    • Sommer D., Fakata K.L., Swanson S.A., Stemmer P.M. Modulation of the phosphatase activity of calcineurin by oxidants and antioxidants in vitro. Eur. J. Biochem. 267:2000;2312-2322
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2312-2322
    • Sommer, D.1    Fakata, K.L.2    Swanson, S.A.3    Stemmer, P.M.4
  • 29
    • 0037155226 scopus 로고    scopus 로고
    • Redox control of calcineurin by targeting the binuclear Fe(2+)-Zn(2+) center at the enzyme active site
    • Namgaladze D., Hofer H.W., Ullrich V. Redox control of calcineurin by targeting the binuclear Fe(2+)-Zn(2+) center at the enzyme active site. J. Biol. Chem. 277:2002;5962-5969
    • (2002) J. Biol. Chem. , vol.277 , pp. 5962-5969
    • Namgaladze, D.1    Hofer, H.W.2    Ullrich, V.3
  • 30
    • 0037418597 scopus 로고    scopus 로고
    • Superoxide as inhibitor of calcineurin and mediator of redox regulation
    • Ullrich V., Namgaladze D., Frein D. Superoxide as inhibitor of calcineurin and mediator of redox regulation. Toxicol. Lett. 139:2003;107-110
    • (2003) Toxicol. Lett. , vol.139 , pp. 107-110
    • Ullrich, V.1    Namgaladze, D.2    Frein, D.3
  • 31
    • 0041761256 scopus 로고    scopus 로고
    • Phosphorylation of calcipressin 1 increases its ability to inhibit calcineurin and decreases calcipressin half-life
    • Genesca L., Aubareda A., Fuentes J.J., Estivill X., de la L.S., Perez-Riba M. Phosphorylation of calcipressin 1 increases its ability to inhibit calcineurin and decreases calcipressin half-life. Biochem. J. 374:2003;567-575
    • (2003) Biochem. J. , vol.374 , pp. 567-575
    • Genesca, L.1    Aubareda, A.2    Fuentes, J.J.3    Estivill, X.4    De La L., S.5    Perez-Riba, M.6
  • 32
    • 0030049439 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase by H2O2. Role in cell survival following oxidant injury
    • Guyton K.Z., Liu Y., Gorospe M., Xu Q., Holbrook N.J. Activation of mitogen-activated protein kinase by H2O2. Role in cell survival following oxidant injury. J. Biol. Chem. 271:1996;4138-4142
    • (1996) J. Biol. Chem. , vol.271 , pp. 4138-4142
    • Guyton, K.Z.1    Liu, Y.2    Gorospe, M.3    Xu, Q.4    Holbrook, N.J.5
  • 33
    • 0033927997 scopus 로고    scopus 로고
    • Reactive oxygen species stimulate p44/42 mitogen-activated protein kinase and induce p27(Kip1): Role in angiotensin II-mediated hypertrophy of proximal tubular cells
    • Hannken T., Schroeder R., Zahner G., Stahl R.A., Wolf G. Reactive oxygen species stimulate p44/42 mitogen-activated protein kinase and induce p27(Kip1): role in angiotensin II-mediated hypertrophy of proximal tubular cells. J. Am. Soc. Nephrol. 11:2000;1387-1397
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 1387-1397
    • Hannken, T.1    Schroeder, R.2    Zahner, G.3    Stahl, R.A.4    Wolf, G.5
  • 34
    • 0031952589 scopus 로고    scopus 로고
    • Stimulation of p42 and p44 mitogen-activated protein kinases by reactive oxygen species and nitric oxide in hippocampus
    • Kanterewicz B.I., Knapp L.T., Klann E. Stimulation of p42 and p44 mitogen-activated protein kinases by reactive oxygen species and nitric oxide in hippocampus. J. Neurochem. 70:1998;1009-1016
    • (1998) J. Neurochem. , vol.70 , pp. 1009-1016
    • Kanterewicz, B.I.1    Knapp, L.T.2    Klann, E.3
  • 35
    • 0036270446 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated phosphorylation of ERK1/2, Akt/PKB and JNK in cortical neurones: Dependence on Ca(2+) and PI3-kinase
    • Crossthwaite A.J., Hasan S., Williams R.J. Hydrogen peroxide-mediated phosphorylation of ERK1/2, Akt/PKB and JNK in cortical neurones: dependence on Ca(2+) and PI3-kinase. J. Neurochem. 80:2002;24-35
    • (2002) J. Neurochem. , vol.80 , pp. 24-35
    • Crossthwaite, A.J.1    Hasan, S.2    Williams, R.J.3
  • 36
    • 0001737772 scopus 로고    scopus 로고
    • Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation
    • Cunnick J.M., Dorsey J.F., Mei L., Wu J. Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation. Biochem. Mol. Biol. Int. 45:1998;887-894
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 887-894
    • Cunnick, J.M.1    Dorsey, J.F.2    Mei, L.3    Wu, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.