메뉴 건너뛰기




Volumn 41, Issue 11, 2014, Pages 7705-7714

Structure, function, and epigenetic regulation of BNIP3: A pathophysiological relevance

Author keywords

Apoptosis; Autophagy; BNIP3; Epigenetic regulations; Mitochondrial permeabilization

Indexed keywords

BH3 PROTEIN; PROTEIN BNIP3; BNIP3 PROTEIN, HUMAN; MEMBRANE PROTEIN; ONCOPROTEIN;

EID: 84917743242     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-014-3664-x     Document Type: Article
Times cited : (42)

References (70)
  • 1
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19 K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • PID: 9575197, COI: 1:CAS:528:DyaK1cXjtlSgtb0%3D
    • Yasuda M, Theodorakis P, Subramanian T, Chinnadurai G (1998) Adenovirus E1B-19 K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J Biol Chem 273:12415–12421
    • (1998) J Biol Chem , vol.273 , pp. 12415-12421
    • Yasuda, M.1    Theodorakis, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 2
    • 0028113218 scopus 로고
    • Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
    • PID: 7954800, COI: 1:CAS:528:DyaK2MXhvFWrtr4%3D
    • Boyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B et al (1994) Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins. Cell 79:341–351
    • (1994) Cell , vol.79 , pp. 341-351
    • Boyd, J.M.1    Malstrom, S.2    Subramanian, T.3    Venkatesh, L.K.4    Schaeper, U.5    Elangovan, B.6
  • 3
    • 0031455410 scopus 로고    scopus 로고
    • The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis
    • PID: 9396766, COI: 1:CAS:528:DyaK2sXotVGhs7k%3D
    • Chen G, Ray R, Dubik D, Shi L, Cizeau J, Bleackley RC et al (1997) The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis. J Exp Med 186:1975–1983
    • (1997) J Exp Med , vol.186 , pp. 1975-1983
    • Chen, G.1    Ray, R.2    Dubik, D.3    Shi, L.4    Cizeau, J.5    Bleackley, R.C.6
  • 4
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • PID: 2876518, COI: 1:CAS:528:DyaL28XmtVGjsb4%3D
    • Rogers S, Wells R, Rechsteiner M (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234:364–368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 5
    • 57049172037 scopus 로고    scopus 로고
    • Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion
    • PID: 18790835, COI: 1:CAS:528:DC%2BD1cXhsVWktb3M
    • Kubli DA, Quinsay MN, Lee Y, Gustafsson AB (2008) Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion. Am J Physiol Heart Circ Physiol 295:H2025–H2031
    • (2008) Am J Physiol Heart Circ Physiol , vol.295 , pp. H2025-H2031
    • Kubli, D.A.1    Quinsay, M.N.2    Lee, Y.3    Gustafsson, A.B.4
  • 7
    • 0033068143 scopus 로고    scopus 로고
    • BNIP3alpha: A human homolog of mitochondrial proapoptotic protein BNIP3
    • PID: 9973195, COI: 1:CAS:528:DyaK1MXhtV2rsrc%3D
    • Yasuda M, Han JW, Dionne CA, Boyd JM, Chinnadurai G (1999) BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3. Cancer Res 59(3):533–537
    • (1999) Cancer Res , vol.59 , Issue.3 , pp. 533-537
    • Yasuda, M.1    Han, J.W.2    Dionne, C.A.3    Boyd, J.M.4    Chinnadurai, G.5
  • 9
    • 27944470616 scopus 로고    scopus 로고
    • Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators
    • PID: 16093567, COI: 1:CAS:528:DC%2BD2MXht1KgtLnI
    • Aouacheria A, Brunet F, Gouy M (2005) Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators. Mol Biol Evol 22(12):2395–2416
    • (2005) Mol Biol Evol , vol.22 , Issue.12 , pp. 2395-2416
    • Aouacheria, A.1    Brunet, F.2    Gouy, M.3
  • 10
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
    • PID: 10639121, COI: 1:CAS:528:DC%2BD3cXot1ajtA%3D%3D
    • Shimizu S, Tsujimoto Y (2000) Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proc Natl Acad Sci USA 97(2):577–582
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.2 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2
  • 11
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix–helix association
    • PID: 10677291, COI: 1:CAS:528:DC%2BD3cXhtFakt74%3D
    • Russ WP, Engelman DM (2000) The GxxxG motif: a framework for transmembrane helix–helix association. J Mol Biol 296:911–919
    • (2000) J Mol Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 12
    • 0345802999 scopus 로고    scopus 로고
    • Sequence-specific dimerization of the transmembrane domain of the “BH3-only” protein BNIP3 in membranes and detergent
    • PID: 14532263, COI: 1:CAS:528:DC%2BD3sXpslOgu7w%3D
    • Sulistijo ES, Jaszewski TM, MacKenzie KR (2003) Sequence-specific dimerization of the transmembrane domain of the “BH3-only” protein BNIP3 in membranes and detergent. J Biol Chem 278:51950–51956
    • (2003) J Biol Chem , vol.278 , pp. 51950-51956
    • Sulistijo, E.S.1    Jaszewski, T.M.2    MacKenzie, K.R.3
  • 13
    • 33947401373 scopus 로고    scopus 로고
    • Mutagenesis data in the automated prediction of transmembrane helix dimers
    • Metcal DG, Law PB, DeGrado WF (2007) Mutagenesis data in the automated prediction of transmembrane helix dimers. Proteins 67:375–384
    • (2007) Proteins , vol.67 , pp. 375-384
    • Metcal, D.G.1    Law, P.B.2    DeGrado, W.F.3
  • 14
    • 33751088317 scopus 로고    scopus 로고
    • Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix–helix interactions
    • PID: 17049556, COI: 1:CAS:528:DC%2BD28Xht1eqtbfF
    • Sulistijo ES, MacKenzie KR (2006) Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix–helix interactions. J Mol Biol 364:974–990
    • (2006) J Mol Biol , vol.364 , pp. 974-990
    • Sulistijo, E.S.1    MacKenzie, K.R.2
  • 15
    • 26444611461 scopus 로고    scopus 로고
    • Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins
    • PID: 16179394, COI: 1:CAS:528:DC%2BD2MXhtFChu7fL
    • Kim S, Jeon TJ, Oberai A, Yang D, Schmidt JJ, Bowie JU (2005) Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc Natl Acad Sci USA 102:14278–14283
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14278-14283
    • Kim, S.1    Jeon, T.J.2    Oberai, A.3    Yang, D.4    Schmidt, J.J.5    Bowie, J.U.6
  • 17
    • 0035030534 scopus 로고    scopus 로고
    • Hypoxia induces the expression of the pro-apoptotic gene BNIP3
    • PID: 11550088, COI: 1:CAS:528:DC%2BD3MXktVOmsbY%3D
    • Guo K, Searfoss G, Krolikowski D, Pagnoni M, Franks C, Clark K et al (2001) Hypoxia induces the expression of the pro-apoptotic gene BNIP3. Cell Death Differ 8:367–376
    • (2001) Cell Death Differ , vol.8 , pp. 367-376
    • Guo, K.1    Searfoss, G.2    Krolikowski, D.3    Pagnoni, M.4    Franks, C.5    Clark, K.6
  • 18
    • 0034255036 scopus 로고    scopus 로고
    • Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia
    • PID: 10922063, COI: 1:CAS:528:DC%2BD3cXls12ksrg%3D
    • Bruick RK (2000) Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc Natl Acad Sci USA 97:9082–9087
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9082-9087
    • Bruick, R.K.1
  • 19
    • 0035884701 scopus 로고    scopus 로고
    • HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors
    • PID: 11559532, COI: 1:CAS:528:DC%2BD3MXntFaisrc%3D
    • Sowter HM, Ratcliffe PJ, Watson P, Greenberg AH, Harris AL (2001) HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors. Cancer Res 61:6669–6673
    • (2001) Cancer Res , vol.61 , pp. 6669-6673
    • Sowter, H.M.1    Ratcliffe, P.J.2    Watson, P.3    Greenberg, A.H.4    Harris, A.L.5
  • 20
    • 77952672872 scopus 로고    scopus 로고
    • Bnip3 mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism
    • PID: 20025887, COI: 1:CAS:528:DC%2BC3cXlvVels7g%3D
    • Quinsay Melissa N, Lee Y, Shivaji Rikka M, Sayen R, Molkentin Jeffery D, Gottlieb Roberta A, Gustafsson ÅB (2010) Bnip3 mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism. J Mol Cell Cardiol 48(6):1146–1156
    • (2010) J Mol Cell Cardiol , vol.48 , Issue.6 , pp. 1146-1156
    • Quinsay, M.N.1    Lee, Y.2    Shivaji Rikka, M.3    Sayen, R.4    Molkentin, J.D.5    Gottlieb, R.A.6    Gustafsson, Å.B.7
  • 21
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind prosurvival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • PID: 11410528, COI: 1:CAS:528:DC%2BD3MXksFKgtbg%3D
    • Zong WX, Lindsten T, Ross AJ, MacGregor GR, Thompson CB (2001) BH3-only proteins that bind prosurvival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 15(12):1481–1486
    • (2001) Genes Dev , vol.15 , Issue.12 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 22
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • PID: 11326099, COI: 1:CAS:528:DC%2BD3MXjt1eltr0%3D
    • Wei MC, Zong WX, Cheng EH, Lindsten T, Panoutsakopoulou V, Ross AJ et al (2001) Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292(5517):727–730
    • (2001) Science , vol.292 , Issue.5517 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3    Lindsten, T.4    Panoutsakopoulou, V.5    Ross, A.J.6
  • 23
    • 0036789917 scopus 로고    scopus 로고
    • Hypoxia and acidosis activate cardiac myocyte death through the Bcl-2 family protein BNIP3
    • PID: 12226479, COI: 1:CAS:528:DC%2BD38XnvFGhsbo%3D
    • Kubasiak LA, Hernandez OM, Bishopric NH, Webster KA (2002) Hypoxia and acidosis activate cardiac myocyte death through the Bcl-2 family protein BNIP3. Proc Natl Acad Sci USA 99:12825–12830
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12825-12830
    • Kubasiak, L.A.1    Hernandez, O.M.2    Bishopric, N.H.3    Webster, K.A.4
  • 24
    • 0037047647 scopus 로고    scopus 로고
    • Inducible expression of BNIP3 provokes mitochondrial defects and hypoxiamediated cell death of ventricular myocytes
    • PID: 12169648, COI: 1:CAS:528:DC%2BD38Xmt12jtb8%3D
    • Regula KM, Ens K, Kirshenbaum LA (2002) Inducible expression of BNIP3 provokes mitochondrial defects and hypoxiamediated cell death of ventricular myocytes. Circ Res 91:226–231
    • (2002) Circ Res , vol.91 , pp. 226-231
    • Regula, K.M.1    Ens, K.2    Kirshenbaum, L.A.3
  • 25
    • 34547471625 scopus 로고    scopus 로고
    • Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak
    • PID: 17447897, COI: 1:CAS:528:DC%2BD2sXns12gsrw%3D
    • Kubli DA, Ycaza JE, Gustafsson AB (2007) Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak. Biochem J 405:407–415
    • (2007) Biochem J , vol.405 , pp. 407-415
    • Kubli, D.A.1    Ycaza, J.E.2    Gustafsson, A.B.3
  • 26
    • 77952672872 scopus 로고    scopus 로고
    • Bnip3 mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism
    • PID: 20025887, COI: 1:CAS:528:DC%2BC3cXlvVels7g%3D
    • Quinsay MN, Lee Y, Rikka S, Sayen MR, Molkentin JD, Gottlieb RA, Gustafsson AB (2010) Bnip3 mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism. J Mol Cell Cardiol 48:1146–1156
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 1146-1156
    • Quinsay, M.N.1    Lee, Y.2    Rikka, S.3    Sayen, M.R.4    Molkentin, J.D.5    Gottlieb, R.A.6    Gustafsson, A.B.7
  • 27
    • 77953123212 scopus 로고    scopus 로고
    • The BH3-only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms
    • PID: 20436456, COI: 1:CAS:528:DC%2BC3cXltl2lsbg%3D
    • Landes T, Emorine LJ, Courilleau D, Rojo M, Belenguer P, Arnaune-Pelloquin L (2010) The BH3-only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms. EMBO Rep 11:459–465
    • (2010) EMBO Rep , vol.11 , pp. 459-465
    • Landes, T.1    Emorine, L.J.2    Courilleau, D.3    Rojo, M.4    Belenguer, P.5    Arnaune-Pelloquin, L.6
  • 29
    • 33745272512 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by the inhibition of fatty acid synthase in breast cancer cells
    • PID: 16740734, COI: 1:CAS:528:DC%2BD28XltFyjurY%3D
    • Bandyopadhyay S, Zhan R, Wang Y, Pai SK, Hirota S, Hosobe S et al (2006) Mechanism of apoptosis induced by the inhibition of fatty acid synthase in breast cancer cells. Cancer Res 66:5934–5940
    • (2006) Cancer Res , vol.66 , pp. 5934-5940
    • Bandyopadhyay, S.1    Zhan, R.2    Wang, Y.3    Pai, S.K.4    Hirota, S.5    Hosobe, S.6
  • 30
    • 0029910628 scopus 로고    scopus 로고
    • Loss of Rb activates both p53-dependent and -independent cell death pathways in the developing mouse nervous system
    • PID: 8947040, COI: 1:CAS:528:DyaK28XnsFKrt7c%3D
    • Macleod K, Hu Y, Jacks T (1996) Loss of Rb activates both p53-dependent and -independent cell death pathways in the developing mouse nervous system. EMBO J 15:6178–6188
    • (1996) EMBO J , vol.15 , pp. 6178-6188
    • Macleod, K.1    Hu, Y.2    Jacks, T.3
  • 31
    • 34548235820 scopus 로고    scopus 로고
    • BNIP3 is an RB/E2F target gene required for hypoxia-induced autophagy
    • PID: 17576813, COI: 1:CAS:528:DC%2BD2sXpvFGgt7Y%3D
    • Tracy K, Dibling BC, Spike BT, Knabb JR, Schumacker P, Macleod KF (2007) BNIP3 is an RB/E2F target gene required for hypoxia-induced autophagy. Mol Cell Biol 27:6229–6242
    • (2007) Mol Cell Biol , vol.27 , pp. 6229-6242
    • Tracy, K.1    Dibling, B.C.2    Spike, B.T.3    Knabb, J.R.4    Schumacker, P.5    Macleod, K.F.6
  • 32
    • 41949101511 scopus 로고    scopus 로고
    • The cell cycle factor E2F-1 activates Bnip3 and the intrinsic death pathway in ventricular myocytes
    • PID: 18096822, COI: 1:CAS:528:DC%2BD1cXitl2jsrk%3D
    • Yurkova N, Shaw J, Blackie K, Weidman D, Jayas R, Flynn B et al (2008) The cell cycle factor E2F-1 activates Bnip3 and the intrinsic death pathway in ventricular myocytes. Circ Res 102:472–479
    • (2008) Circ Res , vol.102 , pp. 472-479
    • Yurkova, N.1    Shaw, J.2    Blackie, K.3    Weidman, D.4    Jayas, R.5    Flynn, B.6
  • 33
    • 0037013206 scopus 로고    scopus 로고
    • A zinc-finger protein, PLAGL2, induces the expression of a proapoptotic protein Nip3, leading to cellular apoptosis
    • PID: 11832486, COI: 1:CAS:528:DC%2BD38Xjs1Wjsbc%3D
    • Mizutani A, Furukawa T, Adachi Y, Ikehara S, Taketani S (2002) A zinc-finger protein, PLAGL2, induces the expression of a proapoptotic protein Nip3, leading to cellular apoptosis. J Biol Chem 277:15851–15858
    • (2002) J Biol Chem , vol.277 , pp. 15851-15858
    • Mizutani, A.1    Furukawa, T.2    Adachi, Y.3    Ikehara, S.4    Taketani, S.5
  • 34
    • 43949109275 scopus 로고    scopus 로고
    • Downstream of Akt: Foxo3 and mTOR in the regulation of autophagy in skeletal muscle
    • PID: 18367868, COI: 1:CAS:528:DC%2BD1cXntFymsrw%3D
    • Mammucari C, Schiaffino S, Sandri M (2008) Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle. Autophagy 4:524–526
    • (2008) Autophagy , vol.4 , pp. 524-526
    • Mammucari, C.1    Schiaffino, S.2    Sandri, M.3
  • 35
    • 33845612203 scopus 로고    scopus 로고
    • Transcriptional silencing of the death gene BNIP3 by cooperative action of NF-kappaB and histone deacetylase 1 in ventricular myocytes
    • PID: 17082476, COI: 1:CAS:528:DC%2BD28Xht1Ohu77L
    • Shaw J, Zhang T, Rzeszutek M, Yurkova N, Baetz D, Davie JR, Kirshenbaum LA (2006) Transcriptional silencing of the death gene BNIP3 by cooperative action of NF-kappaB and histone deacetylase 1 in ventricular myocytes. Circ Res 99:1347–1354
    • (2006) Circ Res , vol.99 , pp. 1347-1354
    • Shaw, J.1    Zhang, T.2    Rzeszutek, M.3    Yurkova, N.4    Baetz, D.5    Davie, J.R.6    Kirshenbaum, L.A.7
  • 36
    • 58549107366 scopus 로고    scopus 로고
    • Antagonism of E2F-1 regulated Bnip3 transcription by NF-kappaB is essential for basal cell survival
    • PID: 19088195, COI: 1:CAS:528:DC%2BD1MXks1Glug%3D%3D
    • Shaw J, Yurkova N, Zhang T, Gang H, Aguilar F, Weidman D et al (2008) Antagonism of E2F-1 regulated Bnip3 transcription by NF-kappaB is essential for basal cell survival. Proc Natl Acad Sci USA 105:20734–20739
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20734-20739
    • Shaw, J.1    Yurkova, N.2    Zhang, T.3    Gang, H.4    Aguilar, F.5    Weidman, D.6
  • 37
    • 34548856780 scopus 로고    scopus 로고
    • Mitochondrial proteins Bnip3 and Bnip3L are involved in anthrax lethal toxin-induced macrophage cell death
    • PID: 17623653, COI: 1:CAS:528:DC%2BD2sXpslGjtrs%3D
    • Ha SD, Ng D, Lamothe J, Valvano MA, Han J, Kim SO (2007) Mitochondrial proteins Bnip3 and Bnip3L are involved in anthrax lethal toxin-induced macrophage cell death. J Biol Chem 282:26275–26283
    • (2007) J Biol Chem , vol.282 , pp. 26275-26283
    • Ha, S.D.1    Ng, D.2    Lamothe, J.3    Valvano, M.A.4    Han, J.5    Kim, S.O.6
  • 38
    • 34547875432 scopus 로고    scopus 로고
    • Regulation of bnip3 death pathways by calcium, phosphorylation, and hypoxia-reoxygenation
    • PID: 17638546, COI: 1:CAS:528:DC%2BD2sXosVykurs%3D
    • Graham RM, Thompson JW, Wei J, Bishopric NH, Webster KA (2007) Regulation of bnip3 death pathways by calcium, phosphorylation, and hypoxia-reoxygenation. Antioxid Redox Signal 9:1309–1316
    • (2007) Antioxid Redox Signal , vol.9 , pp. 1309-1316
    • Graham, R.M.1    Thompson, J.W.2    Wei, J.3    Bishopric, N.H.4    Webster, K.A.5
  • 39
  • 40
    • 0029753768 scopus 로고    scopus 로고
    • Genetic instability induced by the tumor microenvironment
    • PID: 8971187, COI: 1:CAS:528:DyaK2sXjtlGq
    • Reynolds TY, Rockwell S, Glazer PM (1996) Genetic instability induced by the tumor microenvironment. Cancer Res 56:5754–5757
    • (1996) Cancer Res , vol.56 , pp. 5754-5757
    • Reynolds, T.Y.1    Rockwell, S.2    Glazer, P.M.3
  • 41
    • 68149147330 scopus 로고    scopus 로고
    • BNIP3 subfamily BH3-only proteins—mitochondrial stress sensors in normal and pathological functions
    • PID: 19641497, COI: 1:CAS:528:DC%2BD1MXpt1Wgurs%3D
    • Chinnadurai G, Vijayalingam S, Gibson Spencer B (2008) BNIP3 subfamily BH3-only proteins—mitochondrial stress sensors in normal and pathological functions. Oncogene 27(Suppl 1):S114–S127
    • (2008) Oncogene , vol.27 , pp. S114-S127
    • Chinnadurai, G.1    Vijayalingam, S.2    Gibson, S.B.3
  • 42
    • 4143106872 scopus 로고    scopus 로고
    • BNIP3 expression is linked with hypoxia-regulated protein expression and with poor prognosis in nonsmall cell lung cancer
    • PID: 15328198, COI: 1:CAS:528:DC%2BD2cXmvFSlur8%3D
    • Giatromanolaki A, Koukourakis MI, Sowter HM, Sivridis E, Gibson S, Gatter KC et al (2004) BNIP3 expression is linked with hypoxia-regulated protein expression and with poor prognosis in nonsmall cell lung cancer. Clin Cancer Res 10:5566–5571
    • (2004) Clin Cancer Res , vol.10 , pp. 5566-5571
    • Giatromanolaki, A.1    Koukourakis, M.I.2    Sowter, H.M.3    Sivridis, E.4    Gibson, S.5    Gatter, K.C.6
  • 43
    • 0043091971 scopus 로고    scopus 로고
    • BNIP3 plays a role in hypoxic cell death in human epithelial cells that is inhibited by growth factors EGF and IGF
    • PID: 12879018, COI: 1:CAS:528:DC%2BD3sXls1GjtLs%3D
    • Kothari S, Cizeau J, McMillan-Ward E, Israels SJ, Bailes M, Ens K et al (2003) BNIP3 plays a role in hypoxic cell death in human epithelial cells that is inhibited by growth factors EGF and IGF. Oncogene 22:4734–4744
    • (2003) Oncogene , vol.22 , pp. 4734-4744
    • Kothari, S.1    Cizeau, J.2    McMillan-Ward, E.3    Israels, S.J.4    Bailes, M.5    Ens, K.6
  • 44
    • 21744434389 scopus 로고    scopus 로고
    • Loss of BNIP3 expression is a late event in pancreatic cancer contributing to chemoresistance and worsened prognosis
    • PID: 15856026, COI: 1:CAS:528:DC%2BD2MXlsVWmt7Y%3D
    • Erkan M, Kleeff J, Esposito I, Giese T, Ketterer K, Buchler MW et al (2005) Loss of BNIP3 expression is a late event in pancreatic cancer contributing to chemoresistance and worsened prognosis. Oncogene 24:4421–4432
    • (2005) Oncogene , vol.24 , pp. 4421-4432
    • Erkan, M.1    Kleeff, J.2    Esposito, I.3    Giese, T.4    Ketterer, K.5    Buchler, M.W.6
  • 45
    • 3442888541 scopus 로고    scopus 로고
    • Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer
    • PID: 15289340, COI: 1:CAS:528:DC%2BD2cXmtF2murg%3D
    • Okami J, Simeone DM, Logsdon CD (2004) Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer. Cancer Res 64:5338–5346
    • (2004) Cancer Res , vol.64 , pp. 5338-5346
    • Okami, J.1    Simeone, D.M.2    Logsdon, C.D.3
  • 46
    • 20444437669 scopus 로고    scopus 로고
    • Upregulation of BNIP3 by 5-aza-2′-deoxycytidine sensitizes pancreatic cancer cells to hypoxia mediated cell death
    • PID: 15942716, COI: 1:CAS:528:DC%2BD2MXlslGmtrw%3D
    • Abe T, Toyota M, Suzuki H, Murai M, Akino K, Ueno M et al (2005) Upregulation of BNIP3 by 5-aza-2′-deoxycytidine sensitizes pancreatic cancer cells to hypoxia mediated cell death. J Gastroenterol 40:504–510
    • (2005) J Gastroenterol , vol.40 , pp. 504-510
    • Abe, T.1    Toyota, M.2    Suzuki, H.3    Murai, M.4    Akino, K.5    Ueno, M.6
  • 47
    • 19944433480 scopus 로고    scopus 로고
    • Aberrant methylation and silencing of the BNIP3 gene in colorectal and gastric cancer
    • PID: 15709167, COI: 1:CAS:528:DC%2BD2MXht1ynsbg%3D
    • Murai M, Toyota M, Suzuki H, Satoh A, Sasaki Y, Akino K et al (2005) Aberrant methylation and silencing of the BNIP3 gene in colorectal and gastric cancer. Clin Cancer Res 11:1021–1027
    • (2005) Clin Cancer Res , vol.11 , pp. 1021-1027
    • Murai, M.1    Toyota, M.2    Suzuki, H.3    Satoh, A.4    Sasaki, Y.5    Akino, K.6
  • 48
    • 33645239843 scopus 로고    scopus 로고
    • A potential molecular link between aerobic glycolysis and cancer
    • PID: 16479166, COI: 1:CAS:528:DC%2BD28XkslaqtL0%3D
    • Manka D, Millhorn DE (2006) A potential molecular link between aerobic glycolysis and cancer. Cell Cycle 5:343–344
    • (2006) Cell Cycle , vol.5 , pp. 343-344
    • Manka, D.1    Millhorn, D.E.2
  • 49
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced Autophagy is mediated through HIF-induction of BNIP3 and BNIP3L via their BH3-domains
    • PID: 19273585, COI: 1:CAS:528:DC%2BD1MXlvFSqu70%3D
    • Bellot G, Garcia-Medina R, Gounon P, Chiche J, Roux D, Pouysségur J, Mazure NM (2009) Hypoxia-induced Autophagy is mediated through HIF-induction of BNIP3 and BNIP3L via their BH3-domains. Mol Cell Biol 29:2570–2581
    • (2009) Mol Cell Biol , vol.29 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3    Chiche, J.4    Roux, D.5    Pouysségur, J.6    Mazure, N.M.7
  • 50
    • 69449107689 scopus 로고    scopus 로고
    • Atypical BH3-domains of BNIP3 and BNIP3L lead to autophagy in hypoxia
    • PID: 19587545
    • Mazure Nathalie M, Pouysségur J (2009) Atypical BH3-domains of BNIP3 and BNIP3L lead to autophagy in hypoxia. Autophagy 5(6):868–869
    • (2009) Autophagy , vol.5 , Issue.6 , pp. 868-869
    • Mazure, N.M.1    Pouysségur, J.2
  • 51
    • 34848851131 scopus 로고    scopus 로고
    • Regulation of apoptosis in fibroblast-like synoviocytes by the hypoxia-induced Bcl-2 family member Bcl-2/adenovirus E1B 19-kd protein-interacting protein 3
    • PID: 17763440, COI: 1:CAS:528:DC%2BD2sXht1GgtbzN
    • Kammouni W, Wong K, Ma G, Firestein GS, Gibson SB, El-Gabalawy HS (2007) Regulation of apoptosis in fibroblast-like synoviocytes by the hypoxia-induced Bcl-2 family member Bcl-2/adenovirus E1B 19-kd protein-interacting protein 3. Arthritis Rheum 56:2854–2863
    • (2007) Arthritis Rheum , vol.56 , pp. 2854-2863
    • Kammouni, W.1    Wong, K.2    Ma, G.3    Firestein, G.S.4    Gibson, S.B.5    El-Gabalawy, H.S.6
  • 52
    • 1242314873 scopus 로고    scopus 로고
    • Nuclear localization of the hypoxia-regulated pro-apoptotic protein BNIP3 after global brain ischemia in the rat hippocampus
    • PID: 14972662, COI: 1:CAS:528:DC%2BD2cXht1yrs78%3D
    • Schmidt-Kastner R, Aguirre-Chen C, Kietzmann T, Saul I, Busto R, Ginsberg MD (2004) Nuclear localization of the hypoxia-regulated pro-apoptotic protein BNIP3 after global brain ischemia in the rat hippocampus. Brain Res 1001:133–142
    • (2004) Brain Res , vol.1001 , pp. 133-142
    • Schmidt-Kastner, R.1    Aguirre-Chen, C.2    Kietzmann, T.3    Saul, I.4    Busto, R.5    Ginsberg, M.D.6
  • 53
    • 34247572412 scopus 로고    scopus 로고
    • BNIP3 upregulation and EndoG translocation in delayed neuronal death in stroke and in hypoxia
    • PID: 17379825, COI: 1:CAS:528:DC%2BD2sXktlSmsrY%3D
    • Zhang Z, Yang X, Zhang S, Ma X, Kong J (2007) BNIP3 upregulation and EndoG translocation in delayed neuronal death in stroke and in hypoxia. Stroke 38:1606–1613
    • (2007) Stroke , vol.38 , pp. 1606-1613
    • Zhang, Z.1    Yang, X.2    Zhang, S.3    Ma, X.4    Kong, J.5
  • 55
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • PID: 12042769, COI: 1:CAS:528:DC%2BD38XksFOmsrw%3D
    • Jones PA, Baylin SB (2002) The fundamental role of epigenetic events in cancer. Nat Rev Genet 3:415–428
    • (2002) Nat Rev Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 56
    • 0842278570 scopus 로고    scopus 로고
    • Epigenetic changes in colorectal cancer
    • PID: 15000147, COI: 1:CAS:528:DC%2BD3sXnsFansr0%3D
    • Kondo Y, Issa JP (2004) Epigenetic changes in colorectal cancer. Cancer Metastasis Rev 23:29–39
    • (2004) Cancer Metastasis Rev , vol.23 , pp. 29-39
    • Kondo, Y.1    Issa, J.P.2
  • 57
    • 7944230161 scopus 로고    scopus 로고
    • Epigenetic silencing mediated by CpG island methylation: Potential as a therapeutic target and as a biomarker
    • PID: 15533764, COI: 1:CAS:528:DC%2BD2cXpsVOksr4%3D
    • Teodoridis JM, Strathdee G, Brown R (2004) Epigenetic silencing mediated by CpG island methylation: potential as a therapeutic target and as a biomarker. Drug Resist Updat 7:267–278
    • (2004) Drug Resist Updat , vol.7 , pp. 267-278
    • Teodoridis, J.M.1    Strathdee, G.2    Brown, R.3
  • 58
    • 32944481037 scopus 로고    scopus 로고
    • Chemical genomic screening for methylation- silenced genes in gastric cancer cell lines using 5-aza-2′-deoxycytidine treatment and oligonucleotide microarray
    • PID: 16367923, COI: 1:CAS:528:DC%2BD28Xht1Kqtro%3D
    • Yamashita S, Tsujino Y, Moriguchi K et al (2006) Chemical genomic screening for methylation- silenced genes in gastric cancer cell lines using 5-aza-2′-deoxycytidine treatment and oligonucleotide microarray. Cancer Sci 97:64–71
    • (2006) Cancer Sci , vol.97 , pp. 64-71
    • Yamashita, S.1    Tsujino, Y.2    Moriguchi, K.3
  • 59
    • 34848881905 scopus 로고    scopus 로고
    • Mechanistic and prognostic significance of aberrant methylation in the molecular pathogenesis of human hepatocellular carcinoma
    • PID: 17717605, COI: 1:CAS:528:DC%2BD2sXhtVCms7nE
    • Calvisi DF, Ladu S, Gorden A, Farina M, Lee JS, Conner EA et al (2007) Mechanistic and prognostic significance of aberrant methylation in the molecular pathogenesis of human hepatocellular carcinoma. J Clin Invest 117:2713–2722
    • (2007) J Clin Invest , vol.117 , pp. 2713-2722
    • Calvisi, D.F.1    Ladu, S.2    Gorden, A.3    Farina, M.4    Lee, J.S.5    Conner, E.A.6
  • 60
    • 0033984094 scopus 로고    scopus 로고
    • BNIP3heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3(BH) domain at both mitochondrial and nonmitochondrial sites
    • PID: 10625696, COI: 1:CAS:528:DC%2BD3cXntleksA%3D%3D
    • Ray R, Chen G, Vande Velde C et al (2000) BNIP3heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3(BH) domain at both mitochondrial and nonmitochondrial sites. J Biol Chem 275:1439–1448
    • (2000) J Biol Chem , vol.275 , pp. 1439-1448
    • Ray, R.1    Chen, G.2    Vande Velde, C.3
  • 61
    • 1342333155 scopus 로고    scopus 로고
    • Expression of the cell death gene BNip3 and NIX in ductal carcinoma in situ of the breast; correlation of BNip3 levels with necrosis and grade
    • PID: 14648660, COI: 1:CAS:528:DC%2BD2cXlsVGmsQ%3D%3D
    • Sowter HM, Ferguson M, Pym C et al (2003) Expression of the cell death gene BNip3 and NIX in ductal carcinoma in situ of the breast; correlation of BNip3 levels with necrosis and grade. J Pathol 201:573–580
    • (2003) J Pathol , vol.201 , pp. 573-580
    • Sowter, H.M.1    Ferguson, M.2    Pym, C.3
  • 62
    • 20244368980 scopus 로고    scopus 로고
    • Aberrant DNA methylation associated with silencing BNIP3 gene expression in haematopoietic tumours
    • PID: 15756280, COI: 1:CAS:528:DC%2BD2MXisVyisb0%3D
    • Murai M, Toyota M, Satoh A, Suzuki H, Akino K, Mita H et al (2005) Aberrant DNA methylation associated with silencing BNIP3 gene expression in haematopoietic tumours. Br J Cancer 92:1165–1172
    • (2005) Br J Cancer , vol.92 , pp. 1165-1172
    • Murai, M.1    Toyota, M.2    Satoh, A.3    Suzuki, H.4    Akino, K.5    Mita, H.6
  • 63
    • 0035542974 scopus 로고    scopus 로고
    • Methyl CpG-binding proteins and transcriptional repression
    • PID: 11746232, COI: 1:CAS:528:DC%2BD38XksFOluw%3D%3D
    • Wade PA (2001) Methyl CpG-binding proteins and transcriptional repression. BioEssays 23:1131–1137
    • (2001) BioEssays , vol.23 , pp. 1131-1137
    • Wade, P.A.1
  • 64
    • 0035158704 scopus 로고    scopus 로고
    • Loss of genomic methylation causes p53-dependent apoptosis and epigenetic deregulation
    • PID: 11137995, COI: 1:CAS:528:DC%2BD3MXis1yksw%3D%3D
    • Jackson-Grusby L, Beard C, Possemato R et al (2001) Loss of genomic methylation causes p53-dependent apoptosis and epigenetic deregulation. Nat Genet 27:31–39
    • (2001) Nat Genet , vol.27 , pp. 31-39
    • Jackson-Grusby, L.1    Beard, C.2    Possemato, R.3
  • 65
    • 79960595659 scopus 로고    scopus 로고
    • Silencing of BNIP3 results from promoter methylation by DNA methyltransferase 1 induced by the mitogen-activated protein kinase pathway
    • PID: 21573703, COI: 1:CAS:528:DC%2BC3MXns12ktb8%3D
    • An HJ, Lee H, Paik SG (2011) Silencing of BNIP3 results from promoter methylation by DNA methyltransferase 1 induced by the mitogen-activated protein kinase pathway. Mol Cells 31(6):579–583
    • (2011) Mol Cells , vol.31 , Issue.6 , pp. 579-583
    • An, H.J.1    Lee, H.2    Paik, S.G.3
  • 66
    • 84892800436 scopus 로고    scopus 로고
    • GCPII modulates oxidative stress and prostate cancer susceptibility through changes in methylation of RASSF1, BNIP3, GSTP1 and Ec-SOD
    • PID: 23979608, COI: 1:CAS:528:DC%2BC3sXhtlCgtbvK
    • Divyya S, Naushad SM, Murthy PV, Reddy ChR, Kutala VK (2013) GCPII modulates oxidative stress and prostate cancer susceptibility through changes in methylation of RASSF1, BNIP3, GSTP1 and Ec-SOD. Mol Biol Rep 40(10):5541–5550
    • (2013) Mol Biol Rep , vol.40 , Issue.10 , pp. 5541-5550
    • Divyya, S.1    Naushad, S.M.2    Murthy, P.V.3    Reddy, C.R.4    Kutala, V.K.5
  • 67
    • 85027953973 scopus 로고    scopus 로고
    • Bcl-2/adenovirus E1B 19 kDa-interacting protein 3 (BNIP3) expression is epigenetically regulated by one-carbon metabolism in invasive duct cell carcinoma of breast
    • PID: 21987236, COI: 1:CAS:528:DC%2BC3MXhs1OqsrzF
    • Naushad SM, Prayaga A, Digumarti RR, Gottumukkala SR, Kutala VK (2012) Bcl-2/adenovirus E1B 19 kDa-interacting protein 3 (BNIP3) expression is epigenetically regulated by one-carbon metabolism in invasive duct cell carcinoma of breast. Mol Cell Biochem 361(1–2):189–195
    • (2012) Mol Cell Biochem , vol.361 , Issue.1-2 , pp. 189-195
    • Naushad, S.M.1    Prayaga, A.2    Digumarti, R.R.3    Gottumukkala, S.R.4    Kutala, V.K.5
  • 70
    • 84905158252 scopus 로고    scopus 로고
    • Molecular insights into the association of obesity with breast cancer risk: Relevance to xenobiotic metabolism and CpG island methylation of tumor suppressor genes
    • PID: 24676543, COI: 1:CAS:528:DC%2BC2cXltleltrw%3D
    • Naushad SM, Hussain T, Al-Attas OS, Prayaga AA, Digumarti RR, Gottumukkala SR, Kutala VK (2014) Molecular insights into the association of obesity with breast cancer risk: relevance to xenobiotic metabolism and CpG island methylation of tumor suppressor genes. Mol Cell Biochem 392(1–2):273–280
    • (2014) Mol Cell Biochem , vol.392 , Issue.1-2 , pp. 273-280
    • Naushad, S.M.1    Hussain, T.2    Al-Attas, O.S.3    Prayaga, A.A.4    Digumarti, R.R.5    Gottumukkala, S.R.6    Kutala, V.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.