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Volumn 84, Issue 5-6, 2002, Pages 381-389

Killing of E. coli cells by E group nuclease colicins

Author keywords

BtuB receptor; Colicin; DNase; H N H endonuclease; Translocation

Indexed keywords

COLICIN; DEOXYRIBONUCLEASE; ENDONUCLEASE; MEMBRANE RECEPTOR; PROTEIN; BTUB PROTEIN, E COLI; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; OUTER MEMBRANE PROTEIN; RECEPTOR;

EID: 0036589253     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(02)01450-5     Document Type: Review
Times cited : (79)

References (61)
  • 1
    • 0029949518 scopus 로고    scopus 로고
    • The biology of E colicins: Paradigms and paradoxes
    • R. James, C. Kleanthous, G.R. Moore, The biology of E colicins: paradigms and paradoxes, Mircobiology 142 (1996) 1569-1580.
    • (1996) Mircobiology , vol.142 , pp. 1569-1580
    • James, R.1    Kleanthous, C.2    Moore, G.R.3
  • 2
    • 0018883387 scopus 로고
    • Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragments
    • Y. Ohno-Iwashita, K. Imahori, Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragments. Biochemistry 19 (1980) 652-659.
    • (1980) Biochemistry , vol.19 , pp. 652-659
    • Ohno-Iwashita, Y.1    Imahori, K.2
  • 3
    • 0021759135 scopus 로고
    • Purification of a small receptor-binding peptide from the central region of the colicin E1 molecule
    • K. R. Brunden, W. A. Cramer, F. S. Cohen, Purification of a small receptor-binding peptide from the central region of the colicin E1 molecule. J. Biol. Chem. 259 (1984) 190-196.
    • (1984) J. Biol. Chem. , vol.259 , pp. 190-196
    • Brunden, K.R.1    Cramer, W.A.2    Cohen, F.S.3
  • 5
    • 0030754709 scopus 로고    scopus 로고
    • Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9
    • C. Garinot-Schneider, C.N. Penfold, G.R. Moore, C. Kleanthous, R. James, Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9, Microbiology 143 (1997) 2931-2938.
    • (1997) Microbiology , vol.143 , pp. 2931-2938
    • Garinot-Schneider, C.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4    James, R.5
  • 6
    • 0031034934 scopus 로고    scopus 로고
    • The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step
    • E. Bouveret, A. Rigal, C. Lazdunski, H. Bénédetti, The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step, Mol. Microbiol. 23 (1997) 909-920.
    • (1997) Mol. Microbiol. , vol.23 , pp. 909-920
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 7
    • 0031569354 scopus 로고    scopus 로고
    • A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1
    • P. Elkins, A. Bunker, W. A. Cramer, C. V. Stauffacher, A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1, Structure 5 (1997) 443-458.
    • (1997) Structure , vol.5 , pp. 443-458
    • Elkins, P.1    Bunker, A.2    Cramer, W.A.3    Stauffacher, C.V.4
  • 10
    • 0015132507 scopus 로고
    • Inactivation of ribosomes in vitro by colicin E3
    • T. Boon, Inactivation of ribosomes in vitro by colicin E3, Proc. Natl. Acad. Sci. USA 68 (1971) 2421-2425.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2421-2425
    • Boon, T.1
  • 11
    • 0015056478 scopus 로고
    • Effect of colicin E3 upon the 30S ribosomal subunit of Escherichia coli
    • B.W. Senior, I.B. Holland, Effect of colicin E3 upon the 30S ribosomal subunit of Escherichia coli, Proc. Natl. Acad. Sci. USA 68 (1971) 959-963.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 959-963
    • Senior, B.W.1    Holland, I.B.2
  • 12
    • 0033605708 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease targeting specific transfer RNA anticodons
    • T. Ogawa, K. Tomita, T. Ueda, K. Watanabe, T. Uozumi, H. Masaki, A cytotoxic ribonuclease targeting specific transfer RNA anticodons, Science 283 (1999) 2097-2100.
    • (1999) Science , vol.283 , pp. 2097-2100
    • Ogawa, T.1    Tomita, K.2    Ueda, T.3    Watanabe, K.4    Uozumi, T.5    Masaki, H.6
  • 13
    • 0035478958 scopus 로고    scopus 로고
    • Immunity proteins: Enzyme inhibitors that avoid the active site
    • C. Kleanthous, D. Walker, Immunity proteins: enzyme inhibitors that avoid the active site, Trends Biochem. Sci. 26 (2001) 624-631.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 624-631
    • Kleanthous, C.1    Walker, D.2
  • 15
    • 0002347541 scopus 로고    scopus 로고
    • The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein
    • T.P. Ko, C.C. Liao, W.Y. Ku, K.F. Chak, H.S. Yuan, The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein, Structure 7 (1999) 91-102.
    • (1999) Structure , vol.7 , pp. 91-102
    • Ko, T.P.1    Liao, C.C.2    Ku, W.Y.3    Chak, K.F.4    Yuan, H.S.5
  • 16
    • 0034665456 scopus 로고    scopus 로고
    • Inhibition of a ribosome-inactivating ribonuclease: The crystal structure of the cytotoxic domain of colicin E3 in complex with its immunity protein
    • S. Carr, D. Walker, R. James, C. Kleanthous, A.M. Hemmings, Inhibition of a ribosome-inactivating ribonuclease: the crystal structure of the cytotoxic domain of colicin E3 in complex with its immunity protein, Struct. Fold Des 8 (2000) 949-960.
    • (2000) Struct. Fold Des , vol.8 , pp. 949-960
    • Carr, S.1    Walker, D.2    James, R.3    Kleanthous, C.4    Hemmings, A.M.5
  • 17
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • S. Soelaiman, K. Jakes, N. Wu, C. Li, M. Shoham, Crystal structure of colicin E3: implications for cell entry and ribosome inactivation, Mol. Cell 8 (2001) 1053-1062.
    • (2001) Mol. Cell , vol.8 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 19
    • 0020388114 scopus 로고
    • Cloning of colicin E1 tolerant tolC (mtcB) gene of Escherichia coli K12 and identification of its gene product
    • N. Otsuji, T. Soejima, S. Maki, H. Shinagawa, Cloning of colicin E1 tolerant tolC (mtcB) gene of Escherichia coli K12 and identification of its gene product, Mol. Gen. Genet. 187 (1982) 30-36.
    • (1982) Mol. Gen. Genet. , vol.187 , pp. 30-36
    • Otsuji, N.1    Soejima, T.2    Maki, S.3    Shinagawa, H.4
  • 20
    • 0024789570 scopus 로고
    • Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli
    • H. Bénédetti, M. Frenette, D. Baty, R. Lloubès, V. Géli, C. Lazdunski, Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli, J. Gen. Microbiol. 135 (1989) 3413-3420.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 3413-3420
    • Bénédetti, H.1    Frenette, M.2    Baty, D.3    Lloubès, R.4    Géli, V.5    Lazdunski, C.6
  • 21
    • 0031718525 scopus 로고    scopus 로고
    • Displacement of OmpF loop 3 is not required for the membrane translocation of colicins N and A in vivo
    • G. Bainbridge, G.A. Armstrong, L.G. Dover, K.F. Whelan, J.H. Lakey, Displacement of OmpF loop 3 is not required for the membrane translocation of colicins N and A in vivo, FEBS Lett. 432 (1998) 117-122.
    • (1998) FEBS Lett. , vol.432 , pp. 117-122
    • Bainbridge, G.1    Armstrong, G.A.2    Dover, L.G.3    Whelan, K.F.4    Lakey, J.H.5
  • 23
    • 0027530729 scopus 로고
    • Role of tol genes in cloacin DF13 susceptibility of Escherichia coli K12 strains expressing the cloacin DF13-aerobactin receptor IutA
    • J.A. Thomas, M.A. Valvano, Role of tol genes in cloacin DF13 susceptibility of Escherichia coli K12 strains expressing the cloacin DF13-aerobactin receptor IutA, J. Bacteriol. 175 (1993) 548-552.
    • (1993) J. Bacteriol. , vol.175 , pp. 548-552
    • Thomas, J.A.1    Valvano, M.A.2
  • 24
    • 0021946983 scopus 로고
    • Correlation between degradation and ultrastructure of peptidoglycan during autolysis of Escherichia coli
    • M. Leduc, C. Frehel, J. van Heijenoort, Correlation between degradation and ultrastructure of peptidoglycan during autolysis of Escherichia coli, J. Bacteriol. 161 (1985) 627-635.
    • (1985) J. Bacteriol. , vol.161 , pp. 627-635
    • Leduc, M.1    Frehel, C.2    Van Heijenoort, J.3
  • 25
    • 0014346151 scopus 로고
    • Areas of adhesion between wall and membrane of Escherichia coli
    • M.E. Bayer, Areas of adhesion between wall and membrane of Escherichia coli, J. Gen. Microbiol. 53 (1968) 395-404.
    • (1968) J. Gen. Microbiol. , vol.53 , pp. 395-404
    • Bayer, M.E.1
  • 28
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • A.D. Ferguson, E. Hofmann, J.W. Coulton, K. Diederichs, W. Welte, Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide, Science 282 (1998) 2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 29
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • K.P. Locher, B. Rees, R. Koebnik, A. Mitschler, L. Moulinier, J.P. Rosenbusch, D. Moras, Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes, Cell 95 (1998) 771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 31
    • 0024404842 scopus 로고
    • Genetics and molecular biology of siderophore-mediated iron transport in bacteria
    • J.H. Crosa, Genetics and molecular biology of siderophore-mediated iron transport in bacteria, Microbiol. Rev. 53 (1989) 517-530.
    • (1989) Microbiol. Rev. , vol.53 , pp. 517-530
    • Crosa, J.H.1
  • 32
    • 0028905676 scopus 로고
    • Novel colicin 10: Assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation
    • H. Pilsl, V. Braun, Novel colicin 10: assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation, Mol. Microbiol. 16 (1995) 57-67.
    • (1995) Mol. Microbiol. , vol.16 , pp. 57-67
    • Pilsl, H.1    Braun, V.2
  • 33
    • 0031983893 scopus 로고    scopus 로고
    • Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli
    • E. Bouveret, A. Rigal, C. Lazdunski, H. Bénédetti, Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli, Mol. Microbiol. 27 (1998) 143-157.
    • (1998) Mol. Microbiol. , vol.27 , pp. 143-157
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 34
    • 0034650563 scopus 로고    scopus 로고
    • The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9
    • S. Carr, C.N. Penfold, V. Bamford, R. James, A.M. Hemmings, The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9, Struct. Fold Des 8 (2000) 57-66.
    • (2000) Struct. Fold Des , vol.8 , pp. 57-66
    • Carr, S.1    Penfold, C.N.2    Bamford, V.3    James, R.4    Hemmings, A.M.5
  • 35
    • 0025915509 scopus 로고
    • Protein import into Escherichia coli: Colicins A and E1 interact with a component of their translocation system
    • H. Bénédetti, C. Lazdunski, R. Llubès, Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system, Embo. J. 10 (1991) 1989-1995.
    • (1991) Embo. J. , vol.10 , pp. 1989-1995
    • Bénédetti, H.1    Lazdunski, C.2    Llubès, R.3
  • 36
    • 0031799096 scopus 로고    scopus 로고
    • Discovery of critical TolA-binding residues in the bactericidal toxin colicin N: A biophysical approach
    • E.M. Raggett, G. Bainbridge, L.J. Evans, A. Cooper, J.H. Lakey, Discovery of critical TolA-binding residues in the bactericidal toxin colicin N: a biophysical approach, Mol. Microbiol. 28 (1998) 1335-1343.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1335-1343
    • Raggett, E.M.1    Bainbridge, G.2    Evans, L.J.3    Cooper, A.4    Lakey, J.H.5
  • 39
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • V. Braun, Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins, FEMS Microbiol. Rev. 16 (1995) 295-307.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 40
    • 0034767924 scopus 로고    scopus 로고
    • Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm
    • L. Journet, E. Bouveret, A. Rigal, R. Lloubes, C. Lazdunski, H. Bénédetti, Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm, Mol. Microbiol. 42 (2001) 331-344.
    • (2001) Mol. Microbiol. , vol.42 , pp. 331-344
    • Journet, L.1    Bouveret, E.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Bénédetti, H.6
  • 41
    • 0032527793 scopus 로고    scopus 로고
    • The Ton system can functionally replace the TolB protein in the uptake of mutated colicin U
    • H. Pilsl, V. Braun. The Ton system can functionally replace the TolB protein in the uptake of mutated colicin U, FEMS Microbiol. Lett. 164 (1998) 363-367.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 363-367
    • Pilsl, H.1    Braun, V.2
  • 42
    • 0033510793 scopus 로고    scopus 로고
    • Channel-forming colicins: Translocation (and other deviant behaviour) associated with colicin Ia channel gating
    • K.S. Jakes, P.K. Kienker, A. Finkelstein, Channel-forming colicins: translocation (and other deviant behaviour) associated with colicin Ia channel gating, Q Rev. Biophys. 32 (1999) 189-205.
    • (1999) Q Rev. Biophys. , vol.32 , pp. 189-205
    • Jakes, K.S.1    Kienker, P.K.2    Finkelstein, A.3
  • 43
    • 0025897173 scopus 로고
    • The tol gene products and the import of macromolecules into Escherichia coli
    • R.E. Webster, The tol gene products and the import of macromolecules into Escherichia coli, Mol. Microbiol. 5 (1991) 1005-1011.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1005-1011
    • Webster, R.E.1
  • 45
    • 0032441768 scopus 로고    scopus 로고
    • Unraveling the structures and modes of action of bacterial toxins
    • D.B. Lacy, R.C. Stevens, Unraveling the structures and modes of action of bacterial toxins, Curr. Opin. Struct. Biol 8 (1998) 778-784.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 778-784
    • Lacy, D.B.1    Stevens, R.C.2
  • 46
    • 0033922714 scopus 로고    scopus 로고
    • Penetration of protein toxins into cells
    • P.O. Falnes, K. Sandvig, Penetration of protein toxins into cells, Curr. Opin. Cell. Biol. 12 (2000) 407-413.
    • (2000) Curr. Opin. Cell. Biol. , vol.12 , pp. 407-413
    • Falnes, P.O.1    Sandvig, K.2
  • 47
    • 0030564827 scopus 로고    scopus 로고
    • Identification of putative active-site residues in the DNase domain of colicin E9 by random mutagenesis
    • C. Garinot-Schneider, A.J. Pommer, G.R. Moore, C. Kleanthous, R. James, Identification of putative active-site residues in the DNase domain of colicin E9 by random mutagenesis, J. Mol. Biol. 260 (1996) 731-742.
    • (1996) J. Mol. Biol. , vol.260 , pp. 731-742
    • Garinot-Schneider, C.1    Pommer, A.J.2    Moore, G.R.3    Kleanthous, C.4    James, R.5
  • 48
    • 0034881923 scopus 로고    scopus 로고
    • Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase Lepb
    • M. de Zamaroczy, L. Mora, A. Lecuyer, V. Geli, R.H. Buckingham, Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase Lepb, Mol. Cell 8 (2001) 159-168.
    • (2001) Mol. Cell , vol.8 , pp. 159-168
    • De Zamaroczy, M.1    Mora, L.2    Lecuyer, A.3    Geli, V.4    Buckingham, R.H.5
  • 49
    • 0034815872 scopus 로고    scopus 로고
    • Processing of DNAse Domain during Translocation of Colicin E7 across the membrane of Escherichia coli
    • C.C. Liao, K.C. Hsiao, Y.W. Liu, P.H. Leng, H.S. Yuen, K.F. Chak, Processing of DNAse Domain during Translocation of Colicin E7 across the membrane of Escherichia coli, Biochem. Biophys. Res. Commun 284 (2001) 556-562.
    • (2001) Biochem. Biophys. Res. Commun , vol.284 , pp. 556-562
    • Liao, C.C.1    Hsiao, K.C.2    Liu, Y.W.3    Leng, P.H.4    Yuen, H.S.5    Chak, K.F.6
  • 50
    • 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
    • E. Vives, P. Brodin, B. Lebleu, A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus, J. Biol. Chem. 272 (1997) 16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 51
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • D. Derossi, A.H. Joliot, G. Chassaing, A. Prochiantz, The third helix of the Antennapedia homeodomain translocates through biological membranes, J. Biol. Chem. 269 (1994) 10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 52
    • 0022558797 scopus 로고
    • Mechanism of membrane damage mediated by human eosinophil cationic protein
    • J.D. Young, C.G. Peterson, P. Venge, Z.A. Cohn, Mechanism of membrane damage mediated by human eosinophil cationic protein, Nature 321 (1986) 613-616.
    • (1986) Nature , vol.321 , pp. 613-616
    • Young, J.D.1    Peterson, C.G.2    Venge, P.3    Cohn, Z.A.4
  • 53
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • M.C. Morris, J. Depollier, J. Mery, F. Heitz, G. Divita, A peptide carrier for the delivery of biologically active proteins into mammalian cells, Nat. Biotechnol. 19 (2001) 1173-1176.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 54
    • 0028151655 scopus 로고
    • Amino acid sequence motif of group I intron endonucleases is conserved in open reading frames of group II introns
    • D.A. Shub, H. Goodrich-Blair, S.R. Eddy, Amino acid sequence motif of group I intron endonucleases is conserved in open reading frames of group II introns, Trends Biochem. Sci. 19 (1994) 402-404.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 402-404
    • Shub, D.A.1    Goodrich-Blair, H.2    Eddy, S.R.3
  • 55
    • 0030812487 scopus 로고    scopus 로고
    • Homing endonucleases: Keeping the house in order
    • M. Belfort, R.J. Roberts, Homing endonucleases: keeping the house in order, Nucl. Acids Res. 25 (1997) 3379-3388.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3379-3388
    • Belfort, M.1    Roberts, R.J.2
  • 57
    • 0032169937 scopus 로고    scopus 로고
    • Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli
    • A.J. Pommer, R. Wallis, G.R. Moore, R. James, C. Kleanthous, Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli, Biochem. J. 334 (1998) 387-392.
    • (1998) Biochem. J. , vol.334 , pp. 387-392
    • Pommer, A.J.1    Wallis, R.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 59
    • 0033459467 scopus 로고    scopus 로고
    • Structural parsimony in endonuclease active sites: Should the number of homing endonuclease families be redefined?
    • U.C. Kûhlmann, G.R. Moore, R. James, C. Kleanthous, A.M. Hemmings, Structural parsimony in endonuclease active sites: should the number of homing endonuclease families be redefined? FEBS Lett. 463 (1999) 1-2.
    • (1999) FEBS Lett. , vol.463 , pp. 1-2
    • Kûhlmann, U.C.1    Moore, G.R.2    James, R.3    Kleanthous, C.4    Hemmings, A.M.5
  • 60
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNa during apoptosis, and its inhibitor ICAD
    • M. Enari, H. Sakahira, H. Yokoyama, K. Okawa, A. Iwamatsu, S. Nagata, A caspase-activated DNase that degrades DNa during apoptosis, and its inhibitor ICAD, Nature 391 (1998) 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 61
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • H. Sakahira, M. Enari, S. Nagata, Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis, Nature 391 (1998) 96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3


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