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Volumn 42, Issue 5, 2010, Pages 355-360

Essential role of copper in the activity and regular periodicity of a recombinant, tumor-associated, cell surface, growth-related and time-keeping hydroquinone (NADH) oxidase with protein disulfide-thiol interchange activity (ENOX2)

Author keywords

Biological clock; Copper; Growth; Hydroquinone (NADH) oxidase; TNOX or ENOX2

Indexed keywords

BATHOCUPROINE; CELL SURFACE PROTEIN; CHELATING AGENT; COPPER; ENOX2 PROTEIN; HYDROQUINONE; IRON; NICKEL; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; ZINC;

EID: 78650000808     PISSN: 0145479X     EISSN: 15736881     Source Type: Journal    
DOI: 10.1007/s10863-010-9305-8     Document Type: Article
Times cited : (6)

References (24)
  • 2
    • 0028945240 scopus 로고
    • 1:CAS:528:DyaK2MXks1Ckt7Y%3D 10.1006/abio.1995.1194
    • AJ Brenner ED Harris 1995 Anal Biochem 226 80 84 1:CAS:528: DyaK2MXks1Ckt7Y%3D 10.1006/abio.1995.1194
    • (1995) Anal Biochem , vol.226 , pp. 80-84
    • Brenner, A.J.1    Harris, E.D.2
  • 4
    • 0037133540 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface
    • DOI 10.1021/bi012041t
    • P-J Chueh C Kim N Cho DM Morré DJ Morré 2002 Biochemistry 41 3732 3741 1:CAS:528:DC%2BD38XhtlOktrk%3D 10.1021/bi012041t (Pubitemid 34224687)
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3732-3741
    • Chueh, P.-J.1    Kim, C.2    Cho, N.3    Morre, D.M.4    Morre, D.J.5
  • 7
    • 78650009536 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD2sXivVOhtbs%3D 10.2203/dose-response.003.03.008
    • C Kim S Layman DM Morré DJ Morré 2005 Dose Response 3 391 413 1:CAS:528:DC%2BD2sXivVOhtbs%3D 10.2203/dose-response.003.03.008
    • (2005) Dose Response , vol.3 , pp. 391-413
    • Kim, C.1    Layman, S.2    Morré, D.M.3    Morré, D.J.4
  • 8
    • 0032943350 scopus 로고    scopus 로고
    • The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity
    • DOI 10.1016/S0005-2728(99)00049-3, PII S0005272899000493
    • T Kishi DM Morré DJ Morré 1999 Biochim Biophys Acta 1412 66 77 1:CAS:528:DyaK1MXjsF2qtLw%3D 10.1016/S0005-2728(99)00049-3 (Pubitemid 29238118)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1412 , Issue.1 , pp. 66-77
    • Kishi, T.1    Morre, D.M.2    Morre, D.J.3
  • 11
    • 0029608917 scopus 로고
    • NADH oxidase activity of HeLa plasma membranes inhibited by the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N'-(4-chlorophenyl)urea (LY181984) at an external site
    • DOI 10.1016/0005-2736(95)00199-9
    • DJ Morré 1995 Biochim Biophys Acta 1240 201 208 10.1016/0005-2736(95)00199-9 (Pubitemid 26005548)
    • (1995) Biochimica et Biophysica Acta - Biomembranes , vol.1240 , Issue.2 , pp. 201-208
    • Morre, D.J.1
  • 13
    • 0043198154 scopus 로고    scopus 로고
    • Cell surface NADH oxidases (ECTO-NOX proteins) with roles in cancer, cellular time-keeping, growth, aging and neurodegenerative diseases
    • DOI 10.1080/1071576031000083107
    • DJ Morré DM Morré 2003 Free Radical Res 37 795 808 10.1080/1071576031000083107 (Pubitemid 36939596)
    • (2003) Free Radical Research , vol.37 , Issue.8 , pp. 795-808
    • Morre, D.J.1    Morre, D.M.2
  • 16
    • 0032420741 scopus 로고    scopus 로고
    • The sulfonylurea-inhibited NADH oxidase activity of HeLa cell plasma membranes has properties of a protein disulfide-thiol oxidoreductase with protein disulfide-thiol interchange activity
    • DOI 10.1023/A:1020594214379
    • DJ Morré P-J Chueh J Lawler DM Morré 1998 J Bioenerg Biomemb 30 477 487 10.1023/A:1020594214379 (Pubitemid 29051599)
    • (1998) Journal of Bioenergetics and Biomembranes , vol.30 , Issue.5 , pp. 477-487
    • Morre, D.J.1    Chueh, P.-J.2    Lawler, J.3    Morre, D.M.4
  • 21
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • PK Smith RI Krohn GT Hermanson AK Mailia FH Gartner MD Provenzano EK Fujimoto NM Goeke BJ Olson DC Klenk 1985 Anal Biochem 150 70 76 10.1016/0003-2697(85)90442-7 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 22
    • 35648944675 scopus 로고    scopus 로고
    • Alternative splicing as the basis for specific localization of tNOX, a unique hydroquinone (NADH) oxidase, to the cancer cell surface
    • DOI 10.1021/bi700973k
    • X Tang Z Tian P-J Chueh S Chen DM Morré DJ Morré 2007 Biochemistry 46 12337 12346 1:CAS:528:DC%2BD2sXhtFaqsLzL 10.1021/bi700973k (Pubitemid 350022388)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12337-12346
    • Tang, X.1    Tian, Z.2    Chueh, P.-J.3    Chen, S.4    Morre, D.M.5    Morre, D.J.6
  • 23
    • 0035919192 scopus 로고    scopus 로고
    • NADH oxidase activity (NOX) and enlargement of HeLa cells oscillate with two different temperature-compensated period lengths of 22 and 24 minutes corresponding to different NOX forms
    • DOI 10.1016/S0167-4889(01)00107-0, PII S0167488901001070
    • S Wang R Pogue DM Morré DJ Morré 2001 Biochim Biophys Acta 1539 192 204 1:CAS:528:DC%2BD3MXksVGltr0%3D 10.1016/S0167-4889(01)00107-0 (Pubitemid 32566216)
    • (2001) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1539 , Issue.3 , pp. 192-204
    • Wang, S.1    Pogue, R.2    Morre, D.M.3    Morre, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.