메뉴 건너뛰기




Volumn 8, Issue 3, 2003, Pages 277-289

Helix 6 of tBid is necessary but not sufficient for mitochondrial binding activity

Author keywords

Apoptosis; BH3 domain; Cytochrome c; Mitochondria; TBid

Indexed keywords

CYTOCHROME C; PROTEIN BID;

EID: 0038236374     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023676906857     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev 2001; 15: 2922-2933.
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 2
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone RW, Ruefli AA, Lowe SW. Apoptosis: A link between cancer genetics and chemotherapy. Cell 2002; 108: 153-164.
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 3
    • 0036498865 scopus 로고    scopus 로고
    • Genetic analysis of the mammalian cell death machinery
    • Joza N, Kroemer G, Penninger JM. Genetic analysis of the mammalian cell death machinery. TIGS 2002; 18: 142-149.
    • (2002) TIGS , vol.18 , pp. 142-149
    • Joza, N.1    Kroemer, G.2    Penninger, J.M.3
  • 4
    • 0036195503 scopus 로고    scopus 로고
    • Apoptosome: The seven-spoked death machine
    • Salvesen GS, Renatus M. Apoptosome: The seven-spoked death machine. Dev Cell 2002; 2: 256-257.
    • (2002) Dev Cell , vol.2 , pp. 256-257
    • Salvesen, G.S.1    Renatus, M.2
  • 5
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw WC, Martins LM, Kaufmann SH. Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 1999; 68: 383-424.
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 7
    • 0035377522 scopus 로고    scopus 로고
    • Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension
    • Kataoka T, Holler N, Micheau O, et al. Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension. J Biol Chem 2001; 276: 19548-19554.
    • (2001) J Biol Chem , vol.276 , pp. 19548-19554
    • Kataoka, T.1    Holler, N.2    Micheau, O.3
  • 8
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death. Cell 1993; 74: 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 9
    • 0028986876 scopus 로고
    • Induction of apoptosis by the Bcl-2 homologue Bak
    • Chittenden T, Harrington EA, O'Connor R, et al. Induction of apoptosis by the Bcl-2 homologue Bak. Nature 1995; 374: 733-736.
    • (1995) Nature , vol.374 , pp. 733-736
    • Chittenden, T.1    Harrington, E.A.2    O'Connor, R.3
  • 10
    • 0028946015 scopus 로고
    • Cloning of a Bcl-2 homologue by interaction with adenovirus E1B 19K
    • Farrow SN, White JHM, Martinou I, et al. Cloning of a Bcl-2 homologue by interaction with adenovirus E1B 19K. Nature 1995; 374: 731-733.
    • (1995) Nature , vol.374 , pp. 731-733
    • Farrow, S.N.1    White, J.H.M.2    Martinou, I.3
  • 11
    • 0028904163 scopus 로고
    • Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak
    • Kiefer MC, Brauer MJ, Powers VC, et al. Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. Nature 1995; 374: 736-739.
    • (1995) Nature , vol.374 , pp. 736-739
    • Kiefer, M.C.1    Brauer, M.J.2    Powers, V.C.3
  • 12
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins - Essential initiators of apoptotic cell death
    • Huang DCS, Strasser A. BH3-only proteins - Essential initiators of apoptotic cell death. Cell 2000; 103: 839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.S.1    Strasser, A.2
  • 13
    • 0036791637 scopus 로고    scopus 로고
    • The roles of Bid
    • Degli Esposti M. The roles of Bid. Apoptosis 2002; 7: 433-440.
    • (2002) Apoptosis , vol.7 , pp. 433-440
    • Degli Esposti, M.1
  • 15
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell 1999; 96: 615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 16
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists
    • McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists. Cell 1999; 96: 625-634.
    • (1999) Cell , vol.96 , pp. 625-634
    • McDonnell, J.M.1    Fushman, D.2    Milliman, C.L.3    Korsmeyer, S.J.4    Cowburn, D.5
  • 17
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu C-J, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998; 94: 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.-J.3    Yuan, J.4
  • 18
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 19
    • 0034107096 scopus 로고    scopus 로고
    • Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid
    • Barry M, Heibein JA, Pinkoski MJ, et al. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid. Mol Cell Biol 2000; 20: 3781-3794.
    • (2000) Mol Cell Biol , vol.20 , pp. 3781-3794
    • Barry, M.1    Heibein, J.A.2    Pinkoski, M.J.3
  • 20
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of Bid, not procaspases, is the most likely route
    • Stoka V, Turk B, Schendel SL, et al. Lysosomal protease pathways to apoptosis. Cleavage of Bid, not procaspases, is the most likely route. J Biol Chem 2001; 276: 3149-3157.
    • (2001) J Biol Chem , vol.276 , pp. 3149-3157
    • Stoka, V.1    Turk, B.2    Schendel, S.L.3
  • 21
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • Chen M, He H, Zhan S, Krajewski S, Reed JC, Gottlieb RA. Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J Biol Chem 2001; 276: 30724-30728.
    • (2001) J Biol Chem , vol.276 , pp. 30724-30728
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 22
    • 0036236471 scopus 로고    scopus 로고
    • Calpain-mediated Bid cleavage and calpain-independent Bak modulation: Two separate pathways in cisplatin-induced apoptosis
    • Mandic A, Viktorsson K, Strandberg L, et al. Calpain-mediated Bid cleavage and calpain-independent Bak modulation: Two separate pathways in cisplatin-induced apoptosis. Mol Cell Biol 2002; 22: 3003-3013.
    • (2002) Mol Cell Biol , vol.22 , pp. 3003-3013
    • Mandic, A.1    Viktorsson, K.2    Strandberg, L.3
  • 23
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, Schlesinger PH. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ 2000; 7: 1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 24
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • Scorrano L, Ashiya M, Buttle K, et al. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev Cell 2002; 2: 55-67.
    • (2002) Dev Cell , vol.2 , pp. 55-67
    • Scorrano, L.1    Ashiya, M.2    Buttle, K.3
  • 25
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
    • Lindsten T, Ross AJ, King A, et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol Cell 2000; 6: 1389-1399.
    • (2000) Mol Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1    Ross, A.J.2    King, A.3
  • 26
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death. Science 2001; 292: 727-730.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 27
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong WX, Lindsten T, Ross AJ, MacGregor GR, Thompson CB. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 2001; 15: 1481-1486.
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 28
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou J-C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000; 20: 929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.-C.4
  • 29
    • 0034663829 scopus 로고    scopus 로고
    • tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei MC, Lindsten T, Mootha VK, et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev 2000; 14: 2060-2071.
    • (2000) Genes Dev , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 30
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T, Mackey MR, Perkins G, et al. Bid, Bax and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 2002; 111: 331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3
  • 31
    • 9844257587 scopus 로고    scopus 로고
    • Inhibition of Bax channel-forming activity by Bcl-2
    • Antonsson B, Conti F, Ciavatta A, et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 1997; 277: 370-372.
    • (1997) Science , vol.277 , pp. 370-372
    • Antonsson, B.1    Conti, F.2    Ciavatta, A.3
  • 32
    • 0030779846 scopus 로고    scopus 로고
    • Comparison of the ion channel characteristics of proapoptotic BAX and anti-apoptotic BCL-2
    • Schlesinger PH, Gross A, Yin XM, et al. Comparison of the ion channel characteristics of proapoptotic BAX and anti-apoptotic BCL-2. Proc Natl Acad Sci USA 1997; 94: 11357-11362.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11357-11362
    • Schlesinger, P.H.1    Gross, A.2    Yin, X.M.3
  • 34
    • 0034725630 scopus 로고    scopus 로고
    • The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment
    • Kudla G, Montessuit S, Eskes R, et al. The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment. J Biol Chem 2000; 275: 22713-22718.
    • (2000) J Biol Chem , vol.275 , pp. 22713-22718
    • Kudla, G.1    Montessuit, S.2    Eskes, R.3
  • 35
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter M, Fang M, Luo X, Nishijima M, Xie X, Wang X. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat Cell Biol 2000; 2: 754-761.
    • (2000) Nat Cell Biol , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 36
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha J, Weiler S, Oh KJ, Wei MC, Korsmeyer SJ. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000; 290: 1761-1765.
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 37
    • 0033534446 scopus 로고    scopus 로고
    • L prevents this release but not tumor necrosis factor-R1/Fas death
    • L prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem 1999; 274: 1156-1163.
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 38
    • 0029965057 scopus 로고    scopus 로고
    • Isolation and characterization of an apoptosis-resistant mutant of human leukemia HL-60 cells that has switched expression from bcl-2 to bcl-x
    • Han Z, Chatterjee D, Early J, Pantazis P, Hendrickson EA, Wyche JH. Isolation and characterization of an apoptosis-resistant mutant of human leukemia HL-60 cells that has switched expression from bcl-2 to bcl-x. Cancer Res 1996; 56: 1621-1628.
    • (1996) Cancer Res , vol.56 , pp. 1621-1628
    • Han, Z.1    Chatterjee, D.2    Early, J.3    Pantazis, P.4    Hendrickson, E.A.5    Wyche, J.H.6
  • 39
    • 0031817864 scopus 로고    scopus 로고
    • A cytosolic factor is required for mitochondrial cytochrome c efflux during apoptosis
    • Han Z, Li G, Bremner TA, Lange TS, et al. A cytosolic factor is required for mitochondrial cytochrome c efflux during apoptosis. Cell Death Differ 1998; 5: 469-479.
    • (1998) Cell Death Differ , vol.5 , pp. 469-479
    • Han, Z.1    Li, G.2    Bremner, T.A.3    Lange, T.S.4
  • 40
    • 0000002537 scopus 로고    scopus 로고
    • Cif (Cytochrome c efflux-inducing factor) activity is regulated by Bcl-2 and caspases and correlates with the activation of Bid
    • Han Z, Bhalla K, Pantazis P, Hendrickson EA, Wyche JH. Cif (Cytochrome c efflux-inducing factor) activity is regulated by Bcl-2 and caspases and correlates with the activation of Bid. Mol Cell Biol 1999; 19: 1381-1389.
    • (1999) Mol Cell Biol , vol.19 , pp. 1381-1389
    • Han, Z.1    Bhalla, K.2    Pantazis, P.3    Hendrickson, E.A.4    Wyche, J.H.5
  • 41
    • 0033531926 scopus 로고    scopus 로고
    • L function and induce apoptosis through cytochrome c-independent activation of caspases
    • L function and induce apoptosis through cytochrome c-independent activation of caspases. J Biol Chem 1999; 274: 13298-13304.
    • (1999) J Biol Chem , vol.274 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 42
    • 0035851110 scopus 로고    scopus 로고
    • BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability
    • Polster BM, Kinnally KW, Fiskum G. BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability. J Biol Chem 2001; 276: 37887-37894.
    • (2001) J Biol Chem , vol.276 , pp. 37887-37894
    • Polster, B.M.1    Kinnally, K.W.2    Fiskum, G.3
  • 44
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives E, Brodin P, Lebleu B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem 1997; 272: 16010-16017.
    • (1997) J Biol Chem , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 45
    • 0037023739 scopus 로고    scopus 로고
    • tBID homooligomerizes in the mitochondrial membrane to induce apoptosis
    • Grinberg M, Sarig R, Zaltsman Y, et al. tBID Homooligomerizes in the mitochondrial membrane to induce apoptosis. J Biol Chem 2002; 277: 12237-12245.
    • (2002) J Biol Chem , vol.277 , pp. 12237-12245
    • Grinberg, M.1    Sarig, R.2    Zaltsman, Y.3
  • 46
    • 0030002801 scopus 로고    scopus 로고
    • Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD-fmk) inhibits apoptosis by blocking the processing of CPP32
    • Slee EA, Zhu H, Chow SC, MacFarlane M, Nicholson DW, Cohen GM. Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD-fmk) inhibits apoptosis by blocking the processing of CPP32. Biochem J 1996; 315: 21-24.
    • (1996) Biochem J , vol.315 , pp. 21-24
    • Slee, E.A.1    Zhu, H.2    Chow, S.C.3    MacFarlane, M.4    Nicholson, D.W.5    Cohen, G.M.6
  • 47
    • 0035914468 scopus 로고    scopus 로고
    • A Fas-associated death domain protein-dependent mechanism mediates the apoptotic action of non-steroidal anti-inflammatory drugs in the human leukemic Jurkat cell line
    • Han Z, Pantazis P, Wyche JH, Kouttab N, Kidd VJ, Hendrickson EA. A Fas-associated death domain protein-dependent mechanism mediates the apoptotic action of non-steroidal anti-inflammatory drugs in the human leukemic Jurkat cell line. J Biol Chem 2001; 276: 38748-38754.
    • (2001) J Biol Chem , vol.276 , pp. 38748-38754
    • Han, Z.1    Pantazis, P.2    Wyche, J.H.3    Kouttab, N.4    Kidd, V.J.5    Hendrickson, E.A.6
  • 48
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144: 891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 49
    • 0030614915 scopus 로고    scopus 로고
    • L-Bak peptide complex: Recognition between regulators of apoptosis
    • L-Bak peptide complex: Recognition between regulators of apoptosis. Science 1997; 275: 983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3
  • 50
    • 0033545722 scopus 로고    scopus 로고
    • L, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations
    • L, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations. Proc Natl Acad Sci USA 1999; 96: 5492-5497.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5492-5497
    • Basanez, G.1    Nechushtan, A.2    Drozhinin, O.3
  • 53
    • 1842332735 scopus 로고    scopus 로고
    • L forms an ion channel in synthetic membranes
    • L forms an ion channel in synthetic membranes. Nature 1997; 385: 353-357.
    • (1997) Nature , vol.385 , pp. 353-357
    • Minn, A.J.1    Velez, P.2    Schendel, S.L.3
  • 54
    • 0026581661 scopus 로고
    • Refined structure of the pore-forming domain of colicin A at 2.4 A resolution
    • Parker MW, Postma JP, Pattus F, Tucker AD, Tsernoglou D. Refined structure of the pore-forming domain of colicin A at 2.4 A resolution. J Mol Biol 1992; 224: 639-657.
    • (1992) J Mol Biol , vol.224 , pp. 639-657
    • Parker, M.W.1    Postma, J.P.2    Pattus, F.3    Tucker, A.D.4    Tsernoglou, D.5
  • 55
    • 0032568830 scopus 로고    scopus 로고
    • Unfolding of diphtheria toxin. Identification of hydrophobic sites exposed on lowering of pH by photolabeling
    • D'Silva PR, Lala AK. Unfolding of diphtheria toxin. Identification of hydrophobic sites exposed on lowering of pH by photolabeling. J Biol Chem 1998; 273: 16216-16222.
    • (1998) J Biol Chem , vol.273 , pp. 16216-16222
    • D'Silva, P.R.1    Lala, A.K.2
  • 56
    • 0032478734 scopus 로고    scopus 로고
    • Diphtheria toxin translocation across endosome membranes. A novel cell permeabilization assay reveals new diphtheria toxin fragments in endocytic vesicles
    • Umata T, Mekada E. Diphtheria toxin translocation across endosome membranes. A novel cell permeabilization assay reveals new diphtheria toxin fragments in endocytic vesicles. J Biol Chem 1998; 273: 8351-8359.
    • (1998) J Biol Chem , vol.273 , pp. 8351-8359
    • Umata, T.1    Mekada, E.2
  • 58
    • 0035797909 scopus 로고    scopus 로고
    • Why do regulators of apoptosis look like bacterial toxins?
    • Lazebnik Y. Why do regulators of apoptosis look like bacterial toxins? Curr Biol 2001; 11: R767-R768.
    • (2001) Curr Biol , vol.11
    • Lazebnik, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.