메뉴 건너뛰기




Volumn 17, Issue 2, 1998, Pages 615-625

Modulation of the intracellular stability and toxicity of diphtheria toxin through degradation by the N-end rule pathway

Author keywords

Diphtheria toxin; FLAG epitope; N end rule; Protein degradation; Vero cells

Indexed keywords

BETA GALACTOSIDASE; DIPHTHERIA TOXIN; ELONGATION FACTOR 2;

EID: 0032518925     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.2.615     Document Type: Article
Times cited : (31)

References (59)
  • 1
    • 0023754392 scopus 로고
    • Cotranslational processing and protein turnover in eukaryotic cells
    • Arfin, S.M. and Bradshaw, R.A. (1988) Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry, 27, 7979-7984.
    • (1988) Biochemistry , vol.27 , pp. 7979-7984
    • Arfin, S.M.1    Bradshaw, R.A.2
  • 3
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair, A. and Varshavsky, A. (1989) The degradation signal in a short-lived protein. Cell, 56, 1019-1032.
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 4
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. and Varshavsky, A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 5
    • 0026023373 scopus 로고
    • Inhibition of the N-end rule pathway in riving cells
    • Baker, R.T. and Varshavsky, A. (1991) Inhibition of the N-end rule pathway in riving cells. Proc. Natl Acad. Sci. USA, 88, 1090-1094.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1090-1094
    • Baker, R.T.1    Varshavsky, A.2
  • 6
    • 0029016564 scopus 로고
    • Yeast N-terminal amidase. a new enzyme and component of the N-end rule pathway
    • Baker, R.T. and Varshavsky, A. (1995) Yeast N-terminal amidase. A new enzyme and component of the N-end rule pathway. J. Biol Chem., 270, 12065-12074.
    • (1995) J. Biol Chem. , vol.270 , pp. 12065-12074
    • Baker, R.T.1    Varshavsky, A.2
  • 7
    • 0022397324 scopus 로고
    • Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration
    • Blewitt, M.G., Chung, L.A. and London, E. (1985) Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration. Biochemistry, 24, 5458-5464.
    • (1985) Biochemistry , vol.24 , pp. 5458-5464
    • Blewitt, M.G.1    Chung, L.A.2    London, E.3
  • 8
    • 0023899659 scopus 로고
    • Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin
    • Boissel, J.P., Kasper, T.J. and Bunn, H.F. (1988) Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin. J. Biol. Chem., 263, 8443-8449.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8443-8449
    • Boissel, J.P.1    Kasper, T.J.2    Bunn, H.F.3
  • 9
    • 0024467357 scopus 로고
    • Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis
    • Bragg, T.S. and Robertson, D.L. (1989) Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis. Gene, 81, 45-54.
    • (1989) Gene , vol.81 , pp. 45-54
    • Bragg, T.S.1    Robertson, D.L.2
  • 11
    • 0015217337 scopus 로고
    • Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments
    • Collier, R.J. and Kandel, J. (1971) Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments. J. Biol. Chem., 246, 1496-1503.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1496-1503
    • Collier, R.J.1    Kandel, J.2
  • 12
    • 0018292139 scopus 로고
    • The amino acid sequence of fragment A, an enzymically active fragment of diphtheria toxin. III. The chymotryptic peptides, the peptides derived by cleavage at tryptophan residues, and the complete sequence of the protein
    • DeLange, R.J., Williams, L.C., Drazin, R.E. and Collier, R.J. (1979) The amino acid sequence of fragment A, an enzymically active fragment of diphtheria toxin. III. The chymotryptic peptides, the peptides derived by cleavage at tryptophan residues, and the complete sequence of the protein. J. Biol. Chem., 254, 5838-5842.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5838-5842
    • DeLange, R.J.1    Williams, L.C.2    Drazin, R.E.3    Collier, R.J.4
  • 13
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement
    • Draper, R.K. and Simon, M.I. (1980) The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement. J. Cell Biol., 87, 849-854.
    • (1980) J. Cell Biol. , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 14
    • 0015217329 scopus 로고
    • Structure and activity of diphtheria toxin. II. Attack by trypsin at a specific site within the intact toxin molecule
    • Drazin, R., Kandel, J. and Collier, R.J. (1971) Structure and activity of diphtheria toxin. II. Attack by trypsin at a specific site within the intact toxin molecule. J. Biol. Chem., 246, 1504-1510.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1504-1510
    • Drazin, R.1    Kandel, J.2    Collier, R.J.3
  • 15
    • 0024262750 scopus 로고
    • Structural homology between virulence-associated bacterial adenylate cvclases
    • Escuyer, V., Duflot, E., Sezer, O., Danchin, A. and Mock, M. (1988) Structural homology between virulence-associated bacterial adenylate cvclases. Gene. 71, 293-298.
    • (1988) Gene , vol.71 , pp. 293-298
    • Escuyer, V.1    Duflot, E.2    Sezer, O.3    Danchin, A.4    Mock, M.5
  • 16
    • 0029166706 scopus 로고
    • Farnesylation of CaaX-tagged diphtheria toxin A-fragment as a measure of transfer to the cytosol
    • Falnes, P.O., Wiedlocha, A., Rapak, A. and Olsnes, S. (1995) Farnesylation of CaaX-tagged diphtheria toxin A-fragment as a measure of transfer to the cytosol. Biochemistry, 34, 11152-11159.
    • (1995) Biochemistry , vol.34 , pp. 11152-11159
    • Falnes, P.O.1    Wiedlocha, A.2    Rapak, A.3    Olsnes, S.4
  • 17
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.E., Lane, W.S., Choi, S., Corey, E.J. and Schreiber, S.L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science, 268, 726-721.
    • (1995) Science , vol.268 , pp. 726-1721
    • Fenteany, G.1    Standaert, R.E.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 18
    • 0023145912 scopus 로고
    • Role of arginine-tRNA in protein degradation by the ubiquitin pathway
    • Ferber, S. and Ciechanover, A. (1987) Role of arginine-tRNA in protein degradation by the ubiquitin pathway. Nature, 326, 808-811.
    • (1987) Nature , vol.326 , pp. 808-811
    • Ferber, S.1    Ciechanover, A.2
  • 19
    • 0015935156 scopus 로고
    • The elongation factor 2 content of mammalian cells. Assay method and relation to ribosome number
    • Gill, D.M. and Dinius, L.L. (1973) The elongation factor 2 content of mammalian cells. Assay method and relation to ribosome number. J. Biol. Chem., 248, 654-658.
    • (1973) J. Biol. Chem. , vol.248 , pp. 654-658
    • Gill, D.M.1    Dinius, L.L.2
  • 22
    • 0015218131 scopus 로고
    • Adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis by diphtheria toxin
    • Honjo, T., Nishizuka, Y., Kato, I. and Hayaishi, O. (1971) Adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis by diphtheria toxin. J. Biol. Chem., 246, 4251-4260.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4251-4260
    • Honjo, T.1    Nishizuka, Y.2    Kato, I.3    Hayaishi, O.4
  • 24
    • 0023657282 scopus 로고
    • Specificity of cotranslational amino-terminal processing of proteins in yeast
    • Huang, S. et al. (1987) Specificity of cotranslational amino-terminal processing of proteins in yeast. Biochemistry. 26, 8242-8246.
    • (1987) Biochemistry , vol.26 , pp. 8242-8246
    • Huang, S.1
  • 25
    • 0021988228 scopus 로고
    • Quantal entry of diphtheria toxin to the cytosol
    • Hudson, T.H. and Neville, D.M.,Jr (1985) Quantal entry of diphtheria toxin to the cytosol. J. Biol. Chem., 260, 2675-2680.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2675-2680
    • Hudson, T.H.1    Neville Jr., D.M.2
  • 27
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S. and Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell, 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 28
    • 0025992494 scopus 로고
    • Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites
    • Krieglstein, K.G., Henschen, A.H., Weller, U. and Habermann, E. (1991) Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites. Eur. J. Biochem., 202, 41-51.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 41-51
    • Krieglstein, K.G.1    Henschen, A.H.2    Weller, U.3    Habermann, E.4
  • 29
    • 0026769405 scopus 로고
    • Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A
    • Kurazono, H. et al. (1992) Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A. J. Biol. Chem., 267, 14721-14729.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14721-14729
    • Kurazono, H.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0022425912 scopus 로고
    • Nucleotide sequence of cloned cDNA coding for preproricin
    • Lamb, F.I., Roberts, L.M. and Lord, J.M. (1985) Nucleotide sequence of cloned cDNA coding for preproricin. Eur. J. Biochem., 148, 265-270.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 265-270
    • Lamb, F.I.1    Roberts, L.M.2    Lord, J.M.3
  • 33
    • 0019273844 scopus 로고
    • Ligand interactions of diphtheria toxin. II. Relationships between the NAD site and the P site
    • Lory, S., Carroll, S.F. and Collier, R.J. (1980) Ligand interactions of diphtheria toxin. II. Relationships between the NAD site and the P site. J. Biol. Chem., 255, 12016-12019.
    • (1980) J. Biol. Chem. , vol.255 , pp. 12016-12019
    • Lory, S.1    Carroll, S.F.2    Collier, R.J.3
  • 34
    • 0024394164 scopus 로고
    • Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants
    • McGill, S., Stenmark, H., Sandvig, K. and Olsnes, S. (1989) Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants. EMBO J., 8, 2843-2848.
    • (1989) EMBO J. , vol.8 , pp. 2843-2848
    • McGill, S.1    Stenmark, H.2    Sandvig, K.3    Olsnes, S.4
  • 35
    • 0028084802 scopus 로고
    • Two-stage selection of sequences from a random phage display library delineates both core residues and permitted structural range within an epitope
    • Miceli, R.M., DeGraaf, M.E. and Fischer, H.D. (1994) Two-stage selection of sequences from a random phage display library delineates both core residues and permitted structural range within an epitope. J. Immunol. Methods, 167, 279-287.
    • (1994) J. Immunol. Methods , vol.167 , pp. 279-287
    • Miceli, R.M.1    DeGraaf, M.E.2    Fischer, H.D.3
  • 36
    • 0023866565 scopus 로고
    • Low pH-induced release of diphtheria toxin A-fragment in Vero cells. Biochemical evidence for transfer to the cytosol
    • Moskaug, J.O., Sandvig, K. and Olsnes, S. (1988) Low pH-induced release of diphtheria toxin A-fragment in Vero cells. Biochemical evidence for transfer to the cytosol. J. Biol. Chem., 263, 2518-2525.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2518-2525
    • Moskaug, J.O.1    Sandvig, K.2    Olsnes, S.3
  • 37
    • 0019497198 scopus 로고
    • Kinetics of adenosinediphosphoribosylation of elongation factor 2 in cells exposed to diphtheria toxin
    • Moynihan, M.R. and Pappenheimer, A.M.,Jr (1981) Kinetics of adenosinediphosphoribosylation of elongation factor 2 in cells exposed to diphtheria toxin. Infect. Immun., 32, 575-582.
    • (1981) Infect. Immun. , vol.32 , pp. 575-582
    • Moynihan, M.R.1    Pappenheimer Jr., A.M.2
  • 38
    • 0345197348 scopus 로고
    • Cloning and sequencing of the pertussis toxin genes: Operon structure and gene duplication
    • Nicosia, A. et al. (1986) Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication. Proc. Natl Acad. Sci. USA, 83, 4631-4635.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4631-4635
    • Nicosia, A.1
  • 39
    • 0025243542 scopus 로고
    • Processing of Pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the cytosol
    • Ogata, M., Chaudhary, V.K., Pastan, I. and FitzGerald, D.J. (1990) Processing of Pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the cytosol. J. Biol. Chem., 265, 20678-20685.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20678-20685
    • Ogata, M.1    Chaudhary, V.K.2    Pastan, I.3    Fitzgerald, D.J.4
  • 40
    • 0023818260 scopus 로고
    • Specificity of binding of NH2-terminal residue of proteins to ubiquitin-protein ligase. Use of amino acid derivatives to characterize specific binding sites
    • Reiss, Y., Kaim, D. and Hershko, A. (1988) Specificity of binding of NH2-terminal residue of proteins to ubiquitin-protein ligase. Use of amino acid derivatives to characterize specific binding sites. J. Biol. Chem., 263, 2693-2698.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2693-2698
    • Reiss, Y.1    Kaim, D.2    Hershko, A.3
  • 41
    • 0022982251 scopus 로고
    • Degradation of proteins microinjected into HeLa cells. The role of substrate flexibility
    • Rote, K.V. and Rechsteiner, M. (1986) Degradation of proteins microinjected into HeLa cells. The role of substrate flexibility. J. Biol. Chem., 261, 15430-15436.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15430-15436
    • Rote, K.V.1    Rechsteiner, M.2
  • 42
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig, K. and Olsnes, S. (1980) Diphtheria toxin entry into cells is facilitated by low pH. J. Cell Biol., 87, 828-832.
    • (1980) J. Cell Biol. , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 43
    • 0021334088 scopus 로고
    • Evidence that diphtheria toxin and modeccin enter the cytosol from different vesicular compartments
    • Sandvig, K., Sundan, A. and Olsnes.S. (1984) Evidence that diphtheria toxin and modeccin enter the cytosol from different vesicular compartments. J. Cell Biol., 98, 963-970.
    • (1984) J. Cell Biol. , vol.98 , pp. 963-970
    • Sandvig, K.1    Sundan, A.2    OlsnesS3
  • 44
    • 0026708316 scopus 로고
    • In vivo function of the proteasome in the ubiquitin pathway
    • Seufert, W. and Jentsch, S. (1992) In vivo function of the proteasome in the ubiquitin pathway. EMBO J., 11, 3077-3080.
    • (1992) EMBO J. , vol.11 , pp. 3077-3080
    • Seufert, W.1    Jentsch, S.2
  • 45
    • 0026597357 scopus 로고
    • Association between diphtheria toxin A- and B-fragment and their fusion proteins
    • Stenmark, H., Afanasiev, B.N., Ariansen, S. and Olsnes, S. (1992) Association between diphtheria toxin A-and B-fragment and their fusion proteins. Biochem. J., 281, 619-625.
    • (1992) Biochem. J. , vol.281 , pp. 619-625
    • Stenmark, H.1    Afanasiev, B.N.2    Ariansen, S.3    Olsnes, S.4
  • 46
    • 0023840545 scopus 로고
    • Cloning and sequencing of the genes for Shiga toxin from Shigella dysenteriae type 1
    • Strockbine, N.A., Jackson, M.P., Sung, L.M., Holmes, R.K. and O'Brien, A.D. (1988) Cloning and sequencing of the genes for Shiga toxin from Shigella dysenteriae type 1. J. Bacteriol., 170, 1116-1122.
    • (1988) J. Bacteriol. , vol.170 , pp. 1116-1122
    • Strockbine, N.A.1    Jackson, M.P.2    Sung, L.M.3    Holmes, R.K.4    O'Brien, A.D.5
  • 47
    • 0020361446 scopus 로고
    • Preparation and properties of chimeric toxins prepared from the constituent polypeptides of diphtheria toxin and ricin. Evidence for entry of ricin A-chain via the diphtheria toxin pathway
    • Sundan, A., Olsnes, S., Sandvig, K. and Pihl, A. (1982) Preparation and properties of chimeric toxins prepared from the constituent polypeptides of diphtheria toxin and ricin. Evidence for entry of ricin A-chain via the diphtheria toxin pathway. J. Biol. Chem., 257, 9733-9739.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9733-9739
    • Sundan, A.1    Olsnes, S.2    Sandvig, K.3    Pihl, A.4
  • 49
    • 0015522546 scopus 로고
    • Reconstitution of diphtheria toxin from two nontoxic cross-reacting mutant proteins
    • Uchida, T., Pappenheimer, A.M.,Jr and Harper, A.A. (1972) Reconstitution of diphtheria toxin from two nontoxic cross-reacting mutant proteins. Science, 175, 901-903.
    • (1972) Science , vol.175 , pp. 901-903
    • Uchida, T.1    Pappenheimer Jr., A.M.2    Harper, A.A.3
  • 51
    • 0029060153 scopus 로고
    • Codominance and toxins: A path to drugs of nearly unlimited selectivity
    • Varshavsky, A. (1995b) Codominance and toxins: a path to drugs of nearly unlimited selectivity. Proc. Natl Acad. Sci. USA, 92, 3663-3667.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3663-3667
    • Varshavsky, A.1
  • 52
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Sci. USA, 93, 12142-12149.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 53
    • 0028328846 scopus 로고
    • Dual mode of signal transduction by externally added acidic fibroblast growth factor
    • Wiedlocha, A., Falnes, P.Ø., Madshus, I.H., Sandvig, K. and Olsnes, S. (1994) Dual mode of signal transduction by externally added acidic fibroblast growth factor. Cell, 76, 1039-1051.
    • (1994) Cell , vol.76 , pp. 1039-1051
    • Wiedlocha, A.1    Falnes, P.Ø.2    Madshus, I.H.3    Sandvig, K.4    Olsnes, S.5
  • 54
    • 0025076421 scopus 로고
    • Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine
    • Wilson, B.A., Reich, K.A., Weinstein, B.R. and Collier, R.J. (1990) Active-site mutations of diphtheria toxin: effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine. Biochemistry, 29, 8643-8651.
    • (1990) Biochemistry , vol.29 , pp. 8643-8651
    • Wilson, B.A.1    Reich, K.A.2    Weinstein, B.R.3    Collier, R.J.4
  • 55
    • 0025730340 scopus 로고
    • Preproabrin: Genomic cloning, characterisation and the expression of the A-chain in Escherichia coli
    • Wood, K.A., Lord, J.M., Wawrzynczak, E.J. and Piatak, M. (1991) Preproabrin: genomic cloning, characterisation and the expression of the A-chain in Escherichia coli. Eur. J. Biochem., 198, 723-732.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 723-732
    • Wood, K.A.1    Lord, J.M.2    Wawrzynczak, E.J.3    Piatak, M.4
  • 56
    • 0018167496 scopus 로고
    • One molecule of diphtheria toxin fragment a introduced into a cell can kill the cell
    • Yamaizumi, M., Mekada, E., Uchida, T. and Okada, Y. (1978) One molecule of diphtheria toxin fragment A introduced into a cell can kill the cell. Cell. 15, 245-250.
    • (1978) Cell , vol.15 , pp. 245-250
    • Yamaizumi, M.1    Mekada, E.2    Uchida, T.3    Okada, Y.4
  • 57
    • 0020047987 scopus 로고
    • Intracellular stability of diphtheria toxin fragment A in the presence and absence of anti-fragment A antibody
    • Yamaizumi, M., Uchida, T., Takamatsu, K. and Okada, Y. (1982) Intracellular stability of diphtheria toxin fragment A in the presence and absence of anti-fragment A antibody. Proc. Natl Acad. Sci. USA, 79, 461-465.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 461-465
    • Yamaizumi, M.1    Uchida, T.2    Takamatsu, K.3    Okada, Y.4
  • 58
    • 0023144350 scopus 로고
    • Evolutionary origin of pathogenic determinants in enterotoxigenic Escherichia coli and Vibrio cholerae O1
    • Yamamoto, T., Gojobori, T. and Yokota, T. (1987) Evolutionary origin of pathogenic determinants in enterotoxigenic Escherichia coli and Vibrio cholerae O1. J. Bacteriol., 169, 1352-1357.
    • (1987) J. Bacteriol. , vol.169 , pp. 1352-1357
    • Yamamoto, T.1    Gojobori, T.2    Yokota, T.3
  • 59
    • 8944250216 scopus 로고    scopus 로고
    • cDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p
    • Yokota, K. et al. (1996) cDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p. Mol. Biol. Cell, 7, 853-870.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 853-870
    • Yokota, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.