메뉴 건너뛰기




Volumn 1, Issue 4, 2001, Pages 515-525

The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; DNM1L PROTEIN, HUMAN; GUANOSINE TRIPHOSPHATASE; MICROTUBULE ASSOCIATED PROTEIN; MITOCHONDRIAL PROTEIN; ONCOPROTEIN; PROTEIN; PROTEIN BAX; PROTEIN BCL 2;

EID: 0035487808     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1534-5807(01)00055-7     Document Type: Article
Times cited : (1564)

References (59)
  • 1
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams J.M., Cory S. The Bcl-2 protein family. arbiters of cell survival Science. 281:1998;1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 3
    • 0035149539 scopus 로고    scopus 로고
    • Division of mitochondria requires a novel DNM1-interacting protein, Net2p
    • Cerveny K.L., McCaffery J.M., Jensen R.E. Division of mitochondria requires a novel DNM1-interacting protein, Net2p. Mol. Biol. Cell. 12:2001;309-321.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 309-321
    • Cerveny, K.L.1    McCaffery, J.M.2    Jensen, R.E.3
  • 4
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10:2000;369-377.
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 5
    • 0034676062 scopus 로고    scopus 로고
    • Gag3p, an outer membrane protein required for fission of mitochondrial tubules
    • Fekkes P., Shepard K.A., Yaffe M.P. Gag3p, an outer membrane protein required for fission of mitochondrial tubules. J. Cell Biol. 151:2000;333-340.
    • (2000) J. Cell Biol. , vol.151 , pp. 333-340
    • Fekkes, P.1    Shepard, K.A.2    Yaffe, M.P.3
  • 6
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein J.C., Waterhouse N.J., Juin P., Evan G.I., Green D.R. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2:2000;156-162.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 7
    • 0027269557 scopus 로고
    • Detection of DNA strand breaks in individual apoptotic cells by the in situ terminal deoxynucleotidyl transferase and nick translation assays
    • Gorczyca W., Gong J., Darzynkiewicz Z. Detection of DNA strand breaks in individual apoptotic cells by the in situ terminal deoxynucleotidyl transferase and nick translation assays. Cancer Res. 53:1993;1945-1951.
    • (1993) Cancer Res. , vol.53 , pp. 1945-1951
    • Gorczyca, W.1    Gong, J.2    Darzynkiewicz, Z.3
  • 8
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: Paper wraps stone blunts scissors
    • Green D.R. Apoptotic pathways. paper wraps stone blunts scissors Cell. 102:2000;1-4.
    • (2000) Cell , vol.102 , pp. 1-4
    • Green, D.R.1
  • 9
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 10
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A., Jockel J., Wei M.C., Korsmeyer S.J. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17:1998;3878-3885.
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 11
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A., McDonnell J.M., Korsmeyer S.J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13:1999;1899-1911.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 12
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw J.E. Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16:2000;483-519.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 13
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu Y.T., Wolter K.G., Youle R.J. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc. Natl. Acad. Sci. USA. 94:1997;3668-3672.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 14
    • 0031799717 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p
    • Imoto M., Tachibana I., Urrutia R. Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p. J. Cell Sci. 111:1998;1341-1349.
    • (1998) J. Cell Sci. , vol.111 , pp. 1341-1349
    • Imoto, M.1    Tachibana, I.2    Urrutia, R.3
  • 16
    • 0031985126 scopus 로고    scopus 로고
    • Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells
    • Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M. Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells. J. Biol. Chem. 273:1998;1044-1051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1044-1051
    • Kamimoto, T.1    Nagai, Y.2    Onogi, H.3    Muro, Y.4    Wakabayashi, T.5    Hagiwara, M.6
  • 17
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria. a primary site for Bcl-2 regulation of apoptosis Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 19
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat. Med. 3:1997;614-620.
    • (1997) Nat. Med. , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 20
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G., Dallaporta B., Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu. Rev. Physiol. 60:1998;619-642.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 21
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., Reed J.C. Mitochondrial control of cell death. Nat. Med. 6:2000;513-519.
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 22
    • 0033231549 scopus 로고    scopus 로고
    • C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane
    • Labrousse A.M., Zappaterra M.D., Rube D.A., van der Bliek A.M. C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane. Mol. Cell. 4:1999;815-826.
    • (1999) Mol. Cell , vol.4 , pp. 815-826
    • Labrousse, A.M.1    Zappaterra, M.D.2    Rube, D.A.3    Van Der Bliek, A.M.4
  • 23
  • 24
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts. requirement for dATP and cytochrome c Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 25
    • 0033535345 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event
    • Martinou I., Desagher S., Eskes R., Antonsson B., Andre E., Fakan S., Martinou J.C. The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event. J. Cell Biol. 144:1999;883-889.
    • (1999) J. Cell Biol. , vol.144 , pp. 883-889
    • Martinou, I.1    Desagher, S.2    Eskes, R.3    Antonsson, B.4    Andre, E.5    Fakan, S.6    Martinou, J.C.7
  • 26
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S., Llopis J., Deveraux Q.L., Tsien R.Y., Reed J.C. Changes in intramitochondrial and cytosolic pH. early events that modulate caspase activation during apoptosis Nat. Cell Biol. 2:2000;318-325.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 27
    • 0034161330 scopus 로고    scopus 로고
    • The dynamin family of mechanoenzymes: Pinching in new places
    • McNiven M.A., Cao H., Pitts K.R., Yoon Y. The dynamin family of mechanoenzymes. pinching in new places Trends Biochem. Sci. 25:2000;115-120.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 28
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated Mitochondrial Fission Is a Multi-step Process Requiring the Novel Integral Membrane Component Fis1p
    • Mozdy A.D., McCaffery J.M., Shaw J.M. Dnm1p GTPase-mediated Mitochondrial Fission Is a Multi-step Process Requiring the Novel Integral Membrane Component Fis1p. J. Cell Biol. 151:2000;367-380.
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 29
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A., Smith C.L., Hsu Y.T., Youle R.J. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18:1999;2330-2341.
    • (1999) EMBO J. , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 30
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A., Smith C.L., Lamensdorf I., Yoon S.H., Youle R.J. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 153:2001;1265-1276.
    • (2001) J. Cell Biol. , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 32
    • 0032502866 scopus 로고    scopus 로고
    • Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: The impact of irreversible permeability transition
    • Petit P.X., Goubern M., Diolez P., Susin S.A., Zamzami N., Kroemer G. Disruption of the outer mitochondrial membrane as a result of large amplitude swelling. the impact of irreversible permeability transition FEBS Lett. 426:1998;111-116.
    • (1998) FEBS Lett. , vol.426 , pp. 111-116
    • Petit, P.X.1    Goubern, M.2    Diolez, P.3    Susin, S.A.4    Zamzami, N.5    Kroemer, G.6
  • 33
    • 0032734577 scopus 로고    scopus 로고
    • The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells
    • Pitts K.R., Yoon Y., Krueger E.W., McNiven M.A. The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells. Mol. Biol. Cell. 10:1999;4403-4417.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4403-4417
    • Pitts, K.R.1    Yoon, Y.2    Krueger, E.W.3    McNiven, M.A.4
  • 34
    • 0026659512 scopus 로고
    • Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin
    • Rizzuto R., Simpson A.W., Brini M., Pozzan T. Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin. Nature. 358:1992;325-327.
    • (1992) Nature , vol.358 , pp. 325-327
    • Rizzuto, R.1    Simpson, A.W.2    Brini, M.3    Pozzan, T.4
  • 36
    • 0034705684 scopus 로고    scopus 로고
    • Changes in mitochondrial membrane potential during staurosporine-induced apoptosis in Jurkat cells
    • Scarlett J.L., Sheard P.W., Hughes G., Ledgerwood E.C., Ku H.H., Murphy M.P. Changes in mitochondrial membrane potential during staurosporine-induced apoptosis in Jurkat cells. FEBS Lett. 475:2000;267-272.
    • (2000) FEBS Lett. , vol.475 , pp. 267-272
    • Scarlett, J.L.1    Sheard, P.W.2    Hughes, G.3    Ledgerwood, E.C.4    Ku, H.H.5    Murphy, M.P.6
  • 38
    • 0033571410 scopus 로고    scopus 로고
    • Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape
    • Sesaki H., Jensen R.E. Division versus fusion. Dnm1p and Fzo1p antagonistically regulate mitochondrial shape J. Cell Biol. 147:1999;699-706.
    • (1999) J. Cell Biol. , vol.147 , pp. 699-706
    • Sesaki, H.1    Jensen, R.E.2
  • 39
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
    • Sever S., Muhlberg A.B., Schmid S.L. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature. 398:1999;481-486.
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3
  • 40
    • 0030817913 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p
    • Shin H.W., Shinotsuka C., Torii S., Murakami K., Nakayama K. Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J. Biochem. 122:1997;525-530.
    • (1997) J. Biochem. , vol.122 , pp. 525-530
    • Shin, H.W.1    Shinotsuka, C.2    Torii, S.3    Murakami, K.4    Nakayama, K.5
  • 41
    • 0024342278 scopus 로고
    • Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules
    • Shpetner H.S., Vallee R.B. Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Cell. 59:1989;421-432.
    • (1989) Cell , vol.59 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 43
    • 0035166814 scopus 로고    scopus 로고
    • The dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E., Griparic L., Shurland D.L., van der Bliek A.M. The dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell. in press:2001.
    • (2001) Mol. Biol. Cell
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    Van Der Bliek, A.M.4
  • 44
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell M.H., Marks B., Wigge P., McMahon H.T. Nucleotide-dependent conformational changes in dynamin. evidence for a mechanochemical molecular spring Nat. Cell Biol. 1:1999;27-32.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 27-32
    • Stowell, M.H.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 45
    • 0030785790 scopus 로고    scopus 로고
    • The central executioner of apoptosis: Multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- And ceramide-induced apoptosis
    • Susin S.A., Zamzami N., Castedo M., Daugas E., Wang H.G., Geley S., Fassy F., Reed J.C., Kroemer G. The central executioner of apoptosis. multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis J. Exp. Med. 186:1997;25-37.
    • (1997) J. Exp. Med. , vol.186 , pp. 25-37
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3    Daugas, E.4    Wang, H.G.5    Geley, S.6    Fassy, F.7    Reed, J.C.8    Kroemer, G.9
  • 46
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin S.A., Zamzami N., Kroemer G. Mitochondria as regulators of apoptosis. doubt no more Biochim. Biophys. Acta. 1366:1998;151-165.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 47
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer S.M., Hinshaw J.E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell. 93:1998;1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 48
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature. 374:1995;186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 49
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p Is a WD Repeat Protein that Interacts with the Dynamin-related GTPase, Dnm1p, to Trigger Mitochondrial Division
    • Tieu Q., Nunnari J. Mdv1p Is a WD Repeat Protein that Interacts with the Dynamin-related GTPase, Dnm1p, to Trigger Mitochondrial Division. J. Cell Biol. 151:2000;353-366.
    • (2000) J. Cell Biol. , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 50
    • 0033105560 scopus 로고    scopus 로고
    • Functional diversity in the dynamin family
    • van der Bliek A.M. Functional diversity in the dynamin family. Trends Cell Biol. 9:1999;96-102.
    • (1999) Trends Cell Biol. , vol.9 , pp. 96-102
    • Van Der Bliek, A.M.1
  • 51
    • 0034676093 scopus 로고    scopus 로고
    • A mitochondrial division apparatus takes shape
    • van der Bliek A.M. A mitochondrial division apparatus takes shape. J. Cell Biol. 151:2000;F1-F4.
    • (2000) J. Cell Biol. , vol.151
    • Van Der Bliek, A.M.1
  • 53
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis?
    • Vander Heiden M.G., Thompson C.B. Bcl-2 proteins. regulators of apoptosis or of mitochondrial homeostasis? Nat. Cell Biol. 1:1999;E209-E216.
    • (1999) Nat. Cell Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 54
    • 0031660082 scopus 로고    scopus 로고
    • Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing
    • Wang K., Gross A., Waksman G., Korsmeyer S.J. Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing. Mol. Cell. Biol. 18:1998;6083-6089.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6083-6089
    • Wang, K.1    Gross, A.2    Waksman, G.3    Korsmeyer, S.J.4
  • 55
    • 0030046508 scopus 로고    scopus 로고
    • Life, death, and the pursuit of apoptosis
    • White E. Life, death, and the pursuit of apoptosis. Genes Dev. 10:1996;1-15.
    • (1996) Genes Dev. , vol.10 , pp. 1-15
    • White, E.1
  • 58
    • 0032559599 scopus 로고    scopus 로고
    • A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells
    • Yoon Y., Pitts K.R., Dahan S., McNiven M.A. A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. J. Cell Biol. 140:1998;779-793.
    • (1998) J. Cell Biol. , vol.140 , pp. 779-793
    • Yoon, Y.1    Pitts, K.R.2    Dahan, S.3    McNiven, M.A.4
  • 59
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami N., Marchetti P., Castedo M., Zanin C., Vayssiere J.L., Petit P.X., Kroemer G. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181:1995;1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssiere, J.L.5    Petit, P.X.6    Kroemer, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.