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Volumn 6, Issue 4, 1999, Pages 482-497

Metabolic instability of plasmid DNA in the cytosol: A potential barrier to gene transfer

Author keywords

Degradation; DNase; Gene transfer; Microinjection; Plasmid DNA; Turnover

Indexed keywords

CELL ENZYME; DEOXYRIBONUCLEASE; DNA NUCLEOTIDYLEXOTRANSFERASE; DOUBLE STRANDED DNA; NUCLEASE; PHOSPHOLIPID; PLASMID DNA; SINGLE STRANDED DNA;

EID: 0032962975     PISSN: 09697128     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.gt.3300867     Document Type: Article
Times cited : (534)

References (67)
  • 1
    • 0029056088 scopus 로고
    • Cellular and molecular barriers to gene transfer by a cationic lipid
    • Zabner J et al. Cellular and molecular barriers to gene transfer by a cationic lipid. J Biol Chem 1995; 270: 18997-19007.
    • (1995) J Biol Chem , vol.270 , pp. 18997-19007
    • Zabner, J.1
  • 2
    • 0030937585 scopus 로고    scopus 로고
    • Complexes of adenovirus with polycationic polymers and cationic lipids increase the efficiency of gene transfer in vitro and in vivo
    • Fasbender A et al. Complexes of adenovirus with polycationic polymers and cationic lipids increase the efficiency of gene transfer in vitro and in vivo. J Biol Chem 1997; 272: 6479-6489.
    • (1997) J Biol Chem , vol.272 , pp. 6479-6489
    • Fasbender, A.1
  • 3
    • 0030050983 scopus 로고    scopus 로고
    • Microtubular disruption prolongs the expression of human bilirubin-uridinediphosphoglucuronate-glucuronyltransferase-1 gene transferred into Gunn rat livers
    • Chowdhury NR et al. Microtubular disruption prolongs the expression of human bilirubin-uridinediphosphoglucuronate-glucuronyltransferase-1 gene transferred into Gunn rat livers. J Biol Chem 1996; 271: 2341-2346.
    • (1996) J Biol Chem , vol.271 , pp. 2341-2346
    • Chowdhury, N.R.1
  • 4
    • 0031435917 scopus 로고    scopus 로고
    • On the mechanism of DNA transfection: Efficient gene transfer without viruses
    • Coonrod A, Li F-Q, Horwitz M. On the mechanism of DNA transfection: efficient gene transfer without viruses. Gene Therapy 1997; 4: 1313-1321.
    • (1997) Gene Therapy , vol.4 , pp. 1313-1321
    • Coonrod, A.1    Li, F.-Q.2    Horwitz, M.3
  • 5
    • 0029020950 scopus 로고
    • Plasmid DNA entry into post-mitotic nuclei of primary rat myotubes
    • Dowty M, Williams P, Zhang G, Wolff J. Plasmid DNA entry into post-mitotic nuclei of primary rat myotubes. Proc Natl Acad Sci USA 1995; 92: 4572-4576.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4572-4576
    • Dowty, M.1    Williams, P.2    Zhang, G.3    Wolff, J.4
  • 6
    • 0029067792 scopus 로고
    • The role of dioleoyl phosphatidylethanolamine in cationic liposome mediated gene transfer
    • Farhood H, Serbina N, Huang L. The role of dioleoyl phosphatidylethanolamine in cationic liposome mediated gene transfer. Biochim Biophys Acta 1995; 1235: 289-295.
    • (1995) Biochim Biophys Acta , vol.1235 , pp. 289-295
    • Farhood, H.1    Serbina, N.2    Huang, L.3
  • 7
    • 0029964866 scopus 로고    scopus 로고
    • Mechanism of oligonucleotide release from cationic liposomes
    • Zelphati O, Szoka FC. Mechanism of oligonucleotide release from cationic liposomes. Proc Natl Acad Sci USA 1996; 93: 11493-11498.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11493-11498
    • Zelphati, O.1    Szoka, F.C.2
  • 8
    • 0029856329 scopus 로고    scopus 로고
    • Intracellular distribution and mechanism of delivery of oligonucleotides mediated by cationic lipids
    • Zelphati O, Szoka FC. Intracellular distribution and mechanism of delivery of oligonucleotides mediated by cationic lipids. Pharm Res 1996; 13: 1367-1372.
    • (1996) Pharm Res , vol.13 , pp. 1367-1372
    • Zelphati, O.1    Szoka, F.C.2
  • 9
    • 0027290777 scopus 로고
    • Cytoplasmic expression of a reporter gene by co-delivery of T7 RNNa polymerase and T7 promoter sequence with cationic liposomes
    • Gao X, Huang L. Cytoplasmic expression of a reporter gene by co-delivery of T7 RNNA polymerase and T7 promoter sequence with cationic liposomes. Nucleic Acids Res 1993; 21: 2867-2872.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2867-2872
    • Gao, X.1    Huang, L.2
  • 10
    • 0030794696 scopus 로고    scopus 로고
    • Effect of co-lipids in enhancing cationic lipid-mediated gene transfer in vitro and in vivo
    • Fasbender A et al. Effect of co-lipids in enhancing cationic lipid-mediated gene transfer in vitro and in vivo. Gene Therapy 1997; 4: 716-725.
    • (1997) Gene Therapy , vol.4 , pp. 716-725
    • Fasbender, A.1
  • 11
    • 0029908918 scopus 로고    scopus 로고
    • Nuclear localization signal of SV40 T antigen directs import of plasmid DNA into sea urchin male pronuclei in vitro
    • Collas P, Alestrom P. Nuclear localization signal of SV40 T antigen directs import of plasmid DNA into sea urchin male pronuclei in vitro. Mol Reprod Develop 1996; 45: 431-438.
    • (1996) Mol Reprod Develop , vol.45 , pp. 431-438
    • Collas, P.1    Alestrom, P.2
  • 12
    • 0030864266 scopus 로고    scopus 로고
    • A low rate of cell proliferation and reduced DNA limit cationic lipid-mediated gene transfer to primary cultures of ciliated human airway epithelia
    • Fasbender A, Zabner J, Zeiher BG, Welsh MJ. A low rate of cell proliferation and reduced DNA limit cationic lipid-mediated gene transfer to primary cultures of ciliated human airway epithelia. Gene Therapy 1997; 4: 1173-1180.
    • (1997) Gene Therapy , vol.4 , pp. 1173-1180
    • Fasbender, A.1    Zabner, J.2    Zeiher, B.G.3    Welsh, M.J.4
  • 13
    • 0030458784 scopus 로고    scopus 로고
    • Efficacy of a peptide-based gene delivery system depends on mitotic activity
    • Wilke M et al. Efficacy of a peptide-based gene delivery system depends on mitotic activity. Gene Theapy 1996; 3: 1133-1142.
    • (1996) Gene Theapy , vol.3 , pp. 1133-1142
    • Wilke, M.1
  • 14
    • 0031974554 scopus 로고    scopus 로고
    • DNA vector chemistry: The covalent attachment of signal peptides to plasmid DNA
    • Sebestyen MG eta l. DNA vector chemistry: the covalent attachment of signal peptides to plasmid DNA. Nature Biotechnol 1998; 16: 80-85.
    • (1998) Nature Biotechnol , vol.16 , pp. 80-85
    • Sebestyen, M.G.1
  • 15
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome-mediated protein degradation
    • Dunn WA. Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol 1994; 4: 139-143.
    • (1994) Trends Cell Biol , vol.4 , pp. 139-143
    • Dunn, W.A.1
  • 16
    • 0030768810 scopus 로고    scopus 로고
    • Nuclear import of DNA in digitonin-permeabilized cells
    • Hagstrom JE et al. Nuclear import of DNA in digitonin-permeabilized cells. J Cell Sci 1997; 110: 2323-2331.
    • (1997) J Cell Sci , vol.110 , pp. 2323-2331
    • Hagstrom, J.E.1
  • 17
    • 0024576873 scopus 로고
    • Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates
    • Liao T-H, Liao W-C, Chang H-C, Lu K-S. Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates. Biochim Biophys Acta 1989; 1007: 15-22.
    • (1989) Biochim Biophys Acta , vol.1007 , pp. 15-22
    • Liao, T.-H.1    Liao, W.-C.2    Chang, H.-C.3    Lu, K.-S.4
  • 18
    • 0021100710 scopus 로고
    • High efficiency polyoma DNA transfection of chloroquine treated cells
    • Luthman H, Magnusson G. High efficiency polyoma DNA transfection of chloroquine treated cells. Nucleic Acids Res 1983; 11: 1295-1308.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1295-1308
    • Luthman, H.1    Magnusson, G.2
  • 19
    • 0020042010 scopus 로고
    • Inhibition of Semliki forest virus penetration by lysomotropic weak bases
    • Helenius A, Marsh M, White J. Inhibition of Semliki forest virus penetration by lysomotropic weak bases. J Gen Virol 1982; 58: 47-61.
    • (1982) J Gen Virol , vol.58 , pp. 47-61
    • Helenius, A.1    Marsh, M.2    White, J.3
  • 20
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (ΔF508) occurs in the endoplasmic reticulum and requires ATP
    • Lukacs GL et al. Conformational maturation of CFTR but not its mutant counterpart (ΔF508) occurs in the endoplasmic reticulum and requires ATP. EMBO J 1994; 13: 6076-6086.
    • (1994) EMBO J , vol.13 , pp. 6076-6086
    • Lukacs, G.L.1
  • 21
    • 0025083331 scopus 로고
    • Nuclear import in permeabilized cells requires soluble cytoplasmic factors
    • Adam SA, Sterne Marr R, Gerace L. Nuclear import in permeabilized cells requires soluble cytoplasmic factors. J Cell Biol 1990; 111: 807-816.
    • (1990) J Cell Biol , vol.111 , pp. 807-816
    • Adam, S.A.1    Sterne Marr, R.2    Gerace, L.3
  • 22
    • 0023706703 scopus 로고
    • Effect of tetanus toxin on catecholamine release from intact and digitonin permeabilized chromaffin cells
    • Bittner MA, Holz RW. Effect of tetanus toxin on catecholamine release from intact and digitonin permeabilized chromaffin cells. J Neurochem 1988; 51: 451-456.
    • (1988) J Neurochem , vol.51 , pp. 451-456
    • Bittner, M.A.1    Holz, R.W.2
  • 23
    • 0027730470 scopus 로고
    • Cationic lipids improve antisense oligonucleotide uptake and prevent degradation in cultured cells and in human serum
    • Cappaccioli S et al. Cationic lipids improve antisense oligonucleotide uptake and prevent degradation in cultured cells and in human serum. Biochem Biophys Res Com 1993; 197: 818-825.
    • (1993) Biochem Biophys Res Com , vol.197 , pp. 818-825
    • Cappaccioli, S.1
  • 24
    • 0028618172 scopus 로고
    • Enhanced resistance to nuclease degradation of nucleic acids complexed to asialoglycoprotein-polylysine carriers
    • Chiou HC et al. Enhanced resistance to nuclease degradation of nucleic acids complexed to asialoglycoprotein-polylysine carriers. Nucleic Acids Res 1994; 22: 5439-5446.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5439-5446
    • Chiou, H.C.1
  • 25
    • 0032991616 scopus 로고    scopus 로고
    • Stabilized plasmid-lipid particles: Construction and characterization
    • in press
    • Wheeler JJ et al. Stabilized plasmid-lipid particles: construction and characterization. Gene Therapy 1999 (in press).
    • (1999) Gene Therapy
    • Wheeler, J.J.1
  • 26
    • 0031684352 scopus 로고    scopus 로고
    • Liposome-mediated transfection of fetal lung epithelial cells: DNA degradation and enhanced superoxide toxicity
    • Tanswell AK et al. Liposome-mediated transfection of fetal lung epithelial cells: DNA degradation and enhanced superoxide toxicity. Am J Physiol 1998; 275: L452-L460.
    • (1998) Am J Physiol , vol.275
    • Tanswell, A.K.1
  • 27
    • 0021846763 scopus 로고
    • Identification of two lysosomal membrane glycoproteins
    • Chen JW et al. Identification of two lysosomal membrane glycoproteins. J Cell Biol 1985; 101: 85-95.
    • (1985) J Cell Biol , vol.101 , pp. 85-95
    • Chen, J.W.1
  • 28
    • 0029585288 scopus 로고
    • Vesicle accumulation and exocytosis at sites of plasma membrane disruption
    • Miyake K, McNeil PL. Vesicle accumulation and exocytosis at sites of plasma membrane disruption. J Cell Biol 1995; 131: 1737-1745.
    • (1995) J Cell Biol , vol.131 , pp. 1737-1745
    • Miyake, K.1    McNeil, P.L.2
  • 29
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt RA, Bi G, Alderton JM. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science 1994; 263: 390-393.
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 30
    • 0027745784 scopus 로고
    • Overexpression of deoxyribuonuclease I (DNase I) transfected into COS-cells: Its distribution during apoptotic cell death
    • Polzar B et al. Overexpression of deoxyribuonuclease I (DNase I) transfected into COS-cells: its distribution during apoptotic cell death. Eur J Cell Biol 1993; 62: 397-105.
    • (1993) Eur J Cell Biol , vol.62 , pp. 397-1105
    • Polzar, B.1
  • 31
    • 0028342410 scopus 로고
    • Distribution of DNase I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death)
    • Polzar B et al. Distribution of DNase I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death). Eur J Cell Biol 1994; 64: 200-210.
    • (1994) Eur J Cell Biol , vol.64 , pp. 200-210
    • Polzar, B.1
  • 32
    • 0028057478 scopus 로고
    • The apoptotic endonucleases: Cleaning up after cell death?
    • Peitsch MC, Mannherz HG, Tschopp J. The apoptotic endonucleases: cleaning up after cell death? Trends Cell Biol 1994; 4: 37-41.
    • (1994) Trends Cell Biol , vol.4 , pp. 37-41
    • Peitsch, M.C.1    Mannherz, H.G.2    Tschopp, J.3
  • 33
    • 0029791228 scopus 로고    scopus 로고
    • An apoptotic endonuclease activated either by decreasing the pH or by increasing calcium
    • Collins MKL et al. An apoptotic endonuclease activated either by decreasing the pH or by increasing calcium. J Cell Sci 1996; 109: 2393-2399.
    • (1996) J Cell Sci , vol.109 , pp. 2393-2399
    • Collins, M.K.L.1
  • 34
    • 0029042310 scopus 로고
    • Association of high molecular weight DNA fragmentation with apoptotic or non-apoptotic cell death induced by calcium ionophore
    • Kataoka A et al. Association of high molecular weight DNA fragmentation with apoptotic or non-apoptotic cell death induced by calcium ionophore. FEBS Lett 1995; 364: 264-267.
    • (1995) FEBS Lett , vol.364 , pp. 264-267
    • Kataoka, A.1
  • 35
    • 0028839839 scopus 로고
    • Ionic regulation of endonuclease activity in PC12 cells
    • Villalba M et al. Ionic regulation of endonuclease activity in PC12 cells. Biochem J 1995; 311: 1033-1038.
    • (1995) Biochem J , vol.311 , pp. 1033-1038
    • Villalba, M.1
  • 36
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H, Enari M, Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 1998; 391: 96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 37
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 1998; 391: 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1
  • 38
    • 0024375930 scopus 로고
    • Affinity purified tetanus toxin binds to isolated chromaffin granules and inhibits catecholamine release in digitonin-permeabilized chromaffin cells
    • Lazarovici P et al. Affinity purified tetanus toxin binds to isolated chromaffin granules and inhibits catecholamine release in digitonin-permeabilized chromaffin cells. FEBS Lett 1989; 253: 121-128.
    • (1989) FEBS Lett , vol.253 , pp. 121-128
    • Lazarovici, P.1
  • 39
    • 0027260453 scopus 로고
    • Internucleosomal DNA cleavage and neuronal cell death/survival
    • Batistatou A, Green LA. Internucleosomal DNA cleavage and neuronal cell death/survival. J Cell Biol 1993; 122: 523-532.
    • (1993) J Cell Biol , vol.122 , pp. 523-532
    • Batistatou, A.1    Green, L.A.2
  • 40
    • 0028896030 scopus 로고
    • Aurintricarboxilic acid, a putative inhibitor of apoptosis, is a potent inhibitor of DNA topoisomerase II in vitro and in Chinese hamster fibrosarcoma cells
    • Benchokroun Y, Couprie J, Larsen AK. Aurintricarboxilic acid, a putative inhibitor of apoptosis, is a potent inhibitor of DNA topoisomerase II in vitro and in Chinese hamster fibrosarcoma cells. Biochem Pharmacol 1995; 49: 305-313.
    • (1995) Biochem Pharmacol , vol.49 , pp. 305-313
    • Benchokroun, Y.1    Couprie, J.2    Larsen, A.K.3
  • 41
    • 0026100907 scopus 로고
    • Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway
    • Wittels M, Spear PG. Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway. Virus Res 1991; 18: 271-290.
    • (1991) Virus Res , vol.18 , pp. 271-290
    • Wittels, M.1    Spear, P.G.2
  • 42
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber UF, Willetts M, Webster P, Helenius A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell 1993; 75: 477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 44
    • 0031562675 scopus 로고    scopus 로고
    • Glycerol and polylysine synergise in their ability to rupture vesicular membranes: A mechanism for increase transferrin-polylysine-mediated gene transfer
    • Zauner W. Glycerol and polylysine synergise in their ability to rupture vesicular membranes: a mechanism for increase transferrin-polylysine-mediated gene transfer. Exp Cell Res 1997; 232: 137-145.
    • (1997) Exp Cell Res , vol.232 , pp. 137-145
    • Zauner, W.1
  • 45
    • 0028199067 scopus 로고
    • The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems
    • Plank C et al. The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems. J Biol Chem 1994; 269: 12918-12924.
    • (1994) J Biol Chem , vol.269 , pp. 12918-12924
    • Plank, C.1
  • 46
    • 0030053585 scopus 로고    scopus 로고
    • Association with capsid protein promotes nuclear targeting of simian virus 40 DNA
    • Nakanishi A et al. Association with capsid protein promotes nuclear targeting of simian virus 40 DNA. Proc Natl Acad Sci USA 1996; 93: 96-100.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 96-100
    • Nakanishi, A.1
  • 47
    • 0031017060 scopus 로고    scopus 로고
    • In vitro model for the nuclear transport of the hepadnavirus genome
    • Kann M, Bischof A, Gerlich WH. In vitro model for the nuclear transport of the hepadnavirus genome. J Virol 1997; 71: 1310-1316.
    • (1997) J Virol , vol.71 , pp. 1310-1316
    • Kann, M.1    Bischof, A.2    Gerlich, W.H.3
  • 48
    • 0345730460 scopus 로고    scopus 로고
    • The cytosol constitutes a metabolic barrier against transgene delivery to the nucleus
    • Lechardeur D et al. The cytosol constitutes a metabolic barrier against transgene delivery to the nucleus. Ped Pulm 1997; S14: 255.
    • (1997) Ped Pulm , vol.S14 , pp. 255
    • Lechardeur, D.1
  • 49
    • 0019191911 scopus 로고
    • High efficiency transformation by direct microinjection of DNA into cultured mammalian cells
    • Capecchi MR. High efficiency transformation by direct microinjection of DNA into cultured mammalian cells. Cell 1980; 22: 479-488.
    • (1980) Cell , vol.22 , pp. 479-488
    • Capecchi, M.R.1
  • 50
    • 0023375957 scopus 로고
    • Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells
    • Luby-Phelps K, Castle PE, Taylor DL, Lanni F. Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells. Proc Natl Acad Sci USA 1987; 84: 4910-4913.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4910-4913
    • Luby-Phelps, K.1    Castle, P.E.2    Taylor, D.L.3    Lanni, F.4
  • 51
    • 0028078889 scopus 로고
    • Physical properties of cytoplasm
    • Luby-Phelps K. Physical properties of cytoplasm. Curr Opin Cell Biol 1994; 6: 3-9.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 3-9
    • Luby-Phelps, K.1
  • 52
    • 0030742748 scopus 로고    scopus 로고
    • Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus
    • Seksek O, Biwersi J, Verkman AS. Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus. J Cell Biol 1997; 138: 131-142.
    • (1997) J Cell Biol , vol.138 , pp. 131-142
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 53
    • 0032571392 scopus 로고    scopus 로고
    • Polyethylenimine but not the cationic lipids promotes transgene delivery to the nucleus in mammalian cells
    • Pollard H et al. Polyethylenimine but not the cationic lipids promotes transgene delivery to the nucleus in mammalian cells. J Biol Chem 1998; 273: 7507-7511.
    • (1998) J Biol Chem , vol.273 , pp. 7507-7511
    • Pollard, H.1
  • 55
    • 0023654014 scopus 로고
    • Purification and characterization of a potent endonuclease in extracts of bovine heart mitochondria
    • Cummings OW, King TC, Holden JA, Low RL. Purification and characterization of a potent endonuclease in extracts of bovine heart mitochondria. J Biol Chem 1987; 262: 2005-2015.
    • (1987) J Biol Chem , vol.262 , pp. 2005-2015
    • Cummings, O.W.1    King, T.C.2    Holden, J.A.3    Low, R.L.4
  • 56
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activity
    • Wyllie AH. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activity. Nature 1980; 284: 555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 57
    • 0028851733 scopus 로고
    • Involvement of DNase II in nuclear degeneration during lens cell differentiation
    • Torriglia A et al. Involvement of DNase II in nuclear degeneration during lens cell differentiation. J Biol Chem 1995; 270: 28579-28585.
    • (1995) J Biol Chem , vol.270 , pp. 28579-28585
    • Torriglia, A.1
  • 58
    • 0030926327 scopus 로고    scopus 로고
    • Androgen ablation leads to an upregulation and intranuclear accumulation of DNase I in rat prostate epithelial cells paralleling their apoptotic elimination
    • Rauch F et al. Androgen ablation leads to an upregulation and intranuclear accumulation of DNase I in rat prostate epithelial cells paralleling their apoptotic elimination. J Cell Biol 1997; 137: 909-923.
    • (1997) J Cell Biol , vol.137 , pp. 909-923
    • Rauch, F.1
  • 59
    • 0027164993 scopus 로고
    • Identification of deoxyribonuclease II as an endonuclease involved in apoptosis
    • Barry MA, Eastman A. Identification of deoxyribonuclease II as an endonuclease involved in apoptosis. Arch Biochem Biophys 1993; 300: 440-450.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 440-450
    • Barry, M.A.1    Eastman, A.2
  • 60
    • 0030972976 scopus 로고    scopus 로고
    • Native recombinant cyclophilins A, B, and C degrade DNA independently of pepridylprolyl cis-trans-isomerase activity
    • Montague JW, Hughes FM, Cidlowski JA. Native recombinant cyclophilins A, B, and C degrade DNA independently of pepridylprolyl cis-trans-isomerase activity. J Cell Biol 1997; 272: 6677-6684.
    • (1997) J Cell Biol , vol.272 , pp. 6677-6684
    • Montague, J.W.1    Hughes, F.M.2    Cidlowski, J.A.3
  • 61
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik B, Ebersold MW, Helenius A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J Cell Biol 1997; 136: 1007-1021.
    • (1997) J Cell Biol , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 62
    • 0014089362 scopus 로고
    • A dye-buoyant-density method for the detection and isolation of closed circular duplex DNA: The closed circular DNA in HeLa cells
    • Radloff R, Bauer W, Vinograd J. A dye-buoyant-density method for the detection and isolation of closed circular duplex DNA: the closed circular DNA in HeLa cells. Proc Natl Acad Sci USA 1967; 57: 1514-1521.
    • (1967) Proc Natl Acad Sci USA , vol.57 , pp. 1514-1521
    • Radloff, R.1    Bauer, W.2    Vinograd, J.3
  • 63
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira J, Messing J. Production of single-stranded plasmid DNA. Meth Enzymol 1987; 153: 3-11.
    • (1987) Meth Enzymol , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 64
    • 0026298348 scopus 로고
    • DNA localization in metaphase and interphase cells by fluorescence in situ hybridization
    • Trask BJ. DNA localization in metaphase and interphase cells by fluorescence in situ hybridization. Meth Cell Biol 1991; 35: 3-35.
    • (1991) Meth Cell Biol , vol.35 , pp. 3-35
    • Trask, B.J.1
  • 65
    • 0027458860 scopus 로고
    • Technique for in situ measurements of calcium in intracellular inositol 1,4,5-trisphosphate-sensitive stores using the fluorescent indicator mag-fura-2
    • Hofer AM, Machen TE. Technique for in situ measurements of calcium in intracellular inositol 1,4,5-trisphosphate-sensitive stores using the fluorescent indicator mag-fura-2. Proc Natl Acad Sci USA 1993; 90: 2598-2602.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2598-2602
    • Hofer, A.M.1    Machen, T.E.2
  • 66
    • 0026015996 scopus 로고
    • Mutagenesis of the human transferrin receptor: Two cytoplasmic phenylalanines are required for efficient internalization and a second-site mutation is capable of reverting an internalization-defective phenotype
    • McGraw TE, Pytowski B, Arzt J, Ferrone C. Mutagenesis of the human transferrin receptor: two cytoplasmic phenylalanines are required for efficient internalization and a second-site mutation is capable of reverting an internalization-defective phenotype. J Cell Biol 1991; 112: 853-861.
    • (1991) J Cell Biol , vol.112 , pp. 853-861
    • McGraw, T.E.1    Pytowski, B.2    Arzt, J.3    Ferrone, C.4
  • 67
    • 0025239273 scopus 로고
    • Isolation of subcellular organelles
    • Storrie B, Madden EA. Isolation of subcellular organelles. Meth Enzymol 1990; 182: 203-227.
    • (1990) Meth Enzymol , vol.182 , pp. 203-227
    • Storrie, B.1    Madden, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.