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Volumn 8, Issue , 2009, Pages

Export of recombinant proteins in Escherichia coli using ABC transporter with an attached lipase ABC transporter recognition domain (LARD)

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BLOOD CLOTTING FACTOR 10A; EPIDERMAL GROWTH FACTOR; GLYCINE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LIPASE ABC TRANSPORTER; LIPASE ABC TRANSPORTER 0; LIPASE ABC TRANSPORTER 1; RECOMBINANT PROTEIN; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 60949100697     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-8-11     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 0642345085 scopus 로고    scopus 로고
    • Channel-tunnels: Outer membrane components of type I secretion systems and multidrug efflux pumps of Gram-negative bacteria
    • 12783268
    • Andersen C Channel-tunnels: Outer membrane components of type I secretion systems and multidrug efflux pumps of Gram-negative bacteria Reviews of physiology, biochemistry and pharmacology 2003, 147:122-165 12783268
    • (2003) Reviews of Physiology, Biochemistry and Pharmacology , vol.147 , pp. 122-165
    • Andersen, C.1
  • 2
    • 33845512921 scopus 로고    scopus 로고
    • Family I.3 lipase: Bacterial lipases secreted by the type I secretion system
    • 17103114
    • Angkawidjaja C Kanaya S Family I.3 lipase: Bacterial lipases secreted by the type I secretion system Cell Mol Life Sci 2006, 63(23):2804-2817 17103114
    • (2006) Cell Mol Life Sci , vol.63 , Issue.23 , pp. 2804-2817
    • Angkawidjaja, C.1    Kanaya, S.2
  • 3
    • 0028915106 scopus 로고
    • Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB
    • 7651140
    • Koronakis E Hughes C Milisav I Koronakis V Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB Mol Microbiol 1995, 16(1):87-96 7651140
    • (1995) Mol Microbiol , vol.16 , Issue.1 , pp. 87-96
    • Koronakis, E.1    Hughes, C.2    Milisav, I.3    Koronakis, V.4
  • 4
    • 0028051797 scopus 로고
    • PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signal-regulated ATPase activity
    • 7961727
    • Delepelaire P PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signal-regulated ATPase activity J Biol Chem 1994, 269(45):27952-27957 7961727
    • (1994) J Biol Chem , vol.269 , Issue.45 , pp. 27952-27957
    • Delepelaire, P.1
  • 5
    • 0026766441 scopus 로고
    • A topological model for the haemolysin translocator protein HlyD
    • 1495479
    • Schulein R Gentschev I Mollenkopf HJ Goebel W A topological model for the haemolysin translocator protein HlyD Mol Gen Genet 1992, 234(1):155-163 1495479
    • (1992) Mol Gen Genet , vol.234 , Issue.1 , pp. 155-163
    • Schulein, R.1    Gentschev, I.2    Mollenkopf, H.J.3    Goebel, W.4
  • 6
    • 0033912430 scopus 로고    scopus 로고
    • Multidrug resistance mechanisms: Drug efflux across two membranes
    • 10931319
    • Zgurskaya HI Nikaido H Multidrug resistance mechanisms: Drug efflux across two membranes Mol Microbiol 2000, 37(2):219-225 10931319
    • (2000) Mol Microbiol , vol.37 , Issue.2 , pp. 219-225
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 7
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps
    • 10092468
    • Johnson JM Church GM Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps J Mol Biol 1999, 287(3):695-715 10092468
    • (1999) J Mol Biol , vol.287 , Issue.3 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 8
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • 10879525
    • Koronakis V Sharff A Koronakis E Luisi B Hughes C Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export Nature 2000, 405(6789):914-919 10879525
    • (2000) Nature , vol.405 , Issue.6789 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 9
    • 0036202210 scopus 로고    scopus 로고
    • Role of repetitive nine-residue sequence motifs in secretion, enzymatic activity, and protein conformation of a family I.3 lipase
    • 16233181
    • Kwon HJ Haruki M Morikawa M Omori K Kanaya S Role of repetitive nine-residue sequence motifs in secretion, enzymatic activity, and protein conformation of a family I.3 lipase J Biosci Bioeng 2002, 93(2):157-164 16233181
    • (2002) J Biosci Bioeng , vol.93 , Issue.2 , pp. 157-164
    • Kwon, H.J.1    Haruki, M.2    Morikawa, M.3    Omori, K.4    Kanaya, S.5
  • 10
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin biology
    • 11417123
    • Welch RA RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin biology Curr Top Microbiol Immunol 2001, 257:85-111 11417123
    • (2001) Curr Top Microbiol Immunol , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 11
    • 0242478028 scopus 로고    scopus 로고
    • Protein secretion by Gram-negative bacterial ABC exporters - A review
    • 9224868
    • Binet R Letoffe S Ghigo JM Delepelaire P Wandersman C Protein secretion by Gram-negative bacterial ABC exporters - a review Gene 1997, 192(1):7-11 9224868
    • (1997) Gene , vol.192 , Issue.1 , pp. 7-11
    • Binet, R.1    Letoffe, S.2    Ghigo, J.M.3    Delepelaire, P.4    Wandersman, C.5
  • 12
    • 0000589822 scopus 로고    scopus 로고
    • Identification of the tliDEF ABC transporter specific for lipase in Pseudomonas fluorescens SIK W1
    • 93584 10074078
    • Ahn JH Pan JG Rhee JS Identification of the tliDEF ABC transporter specific for lipase in Pseudomonas fluorescens SIK W1 J Bacteriol 1999, 181(6):1847-1852 93584 10074078
    • (1999) J Bacteriol , vol.181 , Issue.6 , pp. 1847-1852
    • Ahn, J.H.1    Pan, J.G.2    Rhee, J.S.3
  • 13
    • 0035650931 scopus 로고    scopus 로고
    • Homologous expression of the lipase and ABC transporter gene cluster, tliDEFA, enhances lipase secretion in Pseudomonas spp
    • 93336 11722899
    • Ahn JH Pan JG Rhee JS Homologous expression of the lipase and ABC transporter gene cluster, tliDEFA, enhances lipase secretion in Pseudomonas spp Appl Environ Microbiol 2001, 67(12):5506-5511 93336 11722899
    • (2001) Appl Environ Microbiol , vol.67 , Issue.12 , pp. 5506-5511
    • Ahn, J.H.1    Pan, J.G.2    Rhee, J.S.3
  • 14
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • 9631087
    • Yang F Moss LG Phillips GN Jr The molecular structure of green fluorescent protein Nat Biotechnol 1996, 14(10):1246-1251 9631087
    • (1996) Nat Biotechnol , vol.14 , Issue.10 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 15
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • 8703075
    • Ormo M Cubitt AB Kallio K Gross LA Tsien RY Remington SJ Crystal structure of the Aequorea victoria green fluorescent protein Science 1996, 273(5280):1392-1395 8703075
    • (1996) Science , vol.273 , Issue.5280 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 16
    • 0037226702 scopus 로고    scopus 로고
    • A cka-gfp transcriptional fusion reveals that the colicin K activity gene is induced in only 3 percent of the population
    • 145340 12511512
    • Mulec J Podlesek Z Mrak P Kopitar A Ihan A Zgur-Bertok D A cka-gfp transcriptional fusion reveals that the colicin K activity gene is induced in only 3 percent of the population J Bacteriol 2003, 185(2):654-659 145340 12511512
    • (2003) J Bacteriol , vol.185 , Issue.2 , pp. 654-659
    • Mulec, J.1    Podlesek, Z.2    Mrak, P.3    Kopitar, A.4    Ihan, A.5    Zgur-Bertok, D.6
  • 17
    • 0033940002 scopus 로고    scopus 로고
    • Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli
    • 101937 10894736
    • Zgurskaya HI Nikaido H Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli J Bacteriol 2000, 182(15):4264-4267 101937 10894736
    • (2000) J Bacteriol , vol.182 , Issue.15 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 18
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • 2186024
    • Carpenter G Cohen S Epidermal growth factor J Biol Chem 1990, 265(14):7709-7712 2186024
    • (1990) J Biol Chem , vol.265 , Issue.14 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 19
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • 2849510
    • Frankel AD Pabo CO Cellular uptake of the tat protein from human immunodeficiency virus Cell 1988, 55(6):1189-1193 2849510
    • (1988) Cell , vol.55 , Issue.6 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 20
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • 2849509
    • Green M Loewenstein PM Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein Cell 1988, 55(6):1179-1188 2849509
    • (1988) Cell , vol.55 , Issue.6 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 21
    • 33646489207 scopus 로고    scopus 로고
    • Cytoplasmic transduction peptide (CTP): New approach for the delivery of biomolecules into cytoplasm in vitro and in vivo
    • 16466653
    • Kim D Jeon C Kim JH Kim MS Yoon CH Choi IS Kim SH Bae YS Cytoplasmic transduction peptide (CTP): New approach for the delivery of biomolecules into cytoplasm in vitro and in vivo Exp Cell Res 2006, 312(8):1277-1288 16466653
    • (2006) Exp Cell Res , vol.312 , Issue.8 , pp. 1277-1288
    • Kim, D.1    Jeon, C.2    Kim, J.H.3    Kim, M.S.4    Yoon, C.H.5    Choi, I.S.6    Kim, S.H.7    Bae, Y.S.8
  • 22
    • 0026088819 scopus 로고
    • The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin
    • 1904127
    • Guzzo J Duong F Wandersman C Murgier M Lazdunski A The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin Mol Microbiol 1991, 5(2):447-453 1904127
    • (1991) Mol Microbiol , vol.5 , Issue.2 , pp. 447-453
    • Guzzo, J.1    Duong, F.2    Wandersman, C.3    Murgier, M.4    Lazdunski, A.5
  • 23
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • 413609 8253063
    • Baumann U Wu S Flaherty KM McKay DB Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif Embo J 1993, 12(9):3357-3364 413609 8253063
    • (1993) Embo J , vol.12 , Issue.9 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 24
    • 0028027226 scopus 로고
    • Crystal structure of the 50 kDa metallo protease from Serratia marcescens
    • 8089845
    • Baumann U Crystal structure of the 50 kDa metallo protease from Serratia marcescens J Mol Biol 1994, 242(3):244-251 8089845
    • (1994) J Mol Biol , vol.242 , Issue.3 , pp. 244-251
    • Baumann, U.1
  • 25
    • 0035941112 scopus 로고    scopus 로고
    • Protease C of Erwinia chrysanthemi: The crystal structure and role of amino acids Y228 and E189
    • 11718553
    • Hege T Baumann U Protease C of Erwinia chrysanthemi: The crystal structure and role of amino acids Y228 and E189 J Mol Biol 2001, 314(2):187-193 11718553
    • (2001) J Mol Biol , vol.314 , Issue.2 , pp. 187-193
    • Hege, T.1    Baumann, U.2
  • 26
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • 11579220
    • Arai R Ueda H Kitayama A Kamiya N Nagamune T Design of the linkers which effectively separate domains of a bifunctional fusion protein Protein Eng 2001, 14(8):529-532 11579220
    • (2001) Protein Eng , vol.14 , Issue.8 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 27
    • 0033543597 scopus 로고    scopus 로고
    • The length of polypeptide linker affects the stability of green fluorescent protein fusion proteins
    • 10469502
    • Prescott M Nowakowski S Nagley P Devenish RJ The length of polypeptide linker affects the stability of green fluorescent protein fusion proteins Anal Biochem 1999, 273(2):305-307 10469502
    • (1999) Anal Biochem , vol.273 , Issue.2 , pp. 305-307
    • Prescott, M.1    Nowakowski, S.2    Nagley, P.3    Devenish, R.J.4
  • 29
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coli hemolysin: A unique protein lipidation mechanism underlying toxin function
    • 98917 9618444
    • Stanley P Koronakis V Hughes C Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function Microbiol Mol Biol Rev 1998, 62(2):309-333 98917 9618444
    • (1998) Microbiol Mol Biol Rev , vol.62 , Issue.2 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 30
    • 0024041944 scopus 로고
    • Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion
    • 281731 2839840
    • Felmlee T Welch RA Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion Proc Natl Acad Sci USA 1988, 85(14):5269-5273 281731 2839840
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.14 , pp. 5269-5273
    • Felmlee, T.1    Welch, R.A.2
  • 31
    • 0024116495 scopus 로고
    • The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytes
    • 3063951
    • Ludwig A Jarchau T Benz R Goebel W The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytes Mol Gen Genet 1988, 214(3):553-561 3063951
    • (1988) Mol Gen Genet , vol.214 , Issue.3 , pp. 553-561
    • Ludwig, A.1    Jarchau, T.2    Benz, R.3    Goebel, W.4
  • 32
    • 0028292373 scopus 로고
    • A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway
    • 8132636
    • Ghigo JM Wandersman C A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway J Biol Chem 1994, 269(12):8979-8985 8132636
    • (1994) J Biol Chem , vol.269 , Issue.12 , pp. 8979-8985
    • Ghigo, J.M.1    Wandersman, C.2
  • 33
    • 0030060225 scopus 로고    scopus 로고
    • Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin
    • 177793 8576066
    • Chervaux C Holland IB Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin J Bacteriol 1996, 178(4):1232-1236 177793 8576066
    • (1996) J Bacteriol , vol.178 , Issue.4 , pp. 1232-1236
    • Chervaux, C.1    Holland, I.B.2
  • 35
    • 0028936779 scopus 로고
    • Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA
    • 7703231
    • Zhang F Yin Y Arrowsmith CH Ling V Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA Biochemistry 1995, 34(13):4193-4201 7703231
    • (1995) Biochemistry , vol.34 , Issue.13 , pp. 4193-4201
    • Zhang, F.1    Yin, Y.2    Arrowsmith, C.H.3    Ling, V.4
  • 37
    • 0028285221 scopus 로고
    • C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: Proton NMR and CD conformational studies in membrane-mimetic environments
    • 8204613
    • Wolff N Ghigo JM Delepelaire P Wandersman C Delepierre M C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: Proton NMR and CD conformational studies in membrane-mimetic environments Biochemistry 1994, 33(22):6792-6801 8204613
    • (1994) Biochemistry , vol.33 , Issue.22 , pp. 6792-6801
    • Wolff, N.1    Ghigo, J.M.2    Delepelaire, P.3    Wandersman, C.4    Delepierre, M.5
  • 38
    • 0028877021 scopus 로고
    • Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes
    • 7592850
    • Rose T Sebo P Bellalou J Ladant D Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes J Biol Chem 1995, 270(44):26370-26376 7592850
    • (1995) J Biol Chem , vol.270 , Issue.44 , pp. 26370-26376
    • Rose, T.1    Sebo, P.2    Bellalou, J.3    Ladant, D.4
  • 39
    • 0028819525 scopus 로고
    • The binding of divalent cations to Escherichia coli alpha-haemolysin
    • 7883008
    • Ostolaza H Soloaga A Goni FM The binding of divalent cations to Escherichia coli alpha-haemolysin Eur J Biochem 1995, 228(1):39-44 7883008
    • (1995) Eur J Biochem , vol.228 , Issue.1 , pp. 39-44
    • Ostolaza, H.1    Soloaga, A.2    Goni, F.M.3
  • 40
    • 0034708415 scopus 로고    scopus 로고
    • Folding of a synthetic parallel beta-roll protein
    • 10734229
    • Lilie H Haehnel W Rudolph R Baumann U Folding of a synthetic parallel beta-roll protein FEBS Lett 2000, 470(2):173-177 10734229
    • (2000) FEBS Lett , vol.470 , Issue.2 , pp. 173-177
    • Lilie, H.1    Haehnel, W.2    Rudolph, R.3    Baumann, U.4
  • 41
    • 35348909085 scopus 로고    scopus 로고
    • Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation
    • 17923123
    • Angkawidjaja C You DJ Matsumura H Kuwahara K Koga Y Takano K Kanaya S Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation FEBS Lett 2007, 581(26):5060-5064 17923123
    • (2007) FEBS Lett , vol.581 , Issue.26 , pp. 5060-5064
    • Angkawidjaja, C.1    You, D.J.2    Matsumura, H.3    Kuwahara, K.4    Koga, Y.5    Takano, K.6    Kanaya, S.7
  • 42
    • 35748968219 scopus 로고    scopus 로고
    • A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens
    • 17728256
    • Meier R Drepper T Svensson V Jaeger KE Baumann U A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens J Biol Chem 2007, 282(43):31477-31483 17728256
    • (2007) J Biol Chem , vol.282 , Issue.43 , pp. 31477-31483
    • Meier, R.1    Drepper, T.2    Svensson, V.3    Jaeger, K.E.4    Baumann, U.5
  • 43
    • 0035920232 scopus 로고    scopus 로고
    • Serratia ATP-binding cassette protein exporter, Lip, recognizes a protein region upstream of the C terminus for specific secretion
    • 11335719
    • Omori K Idei A Akatsuka H Serratia ATP-binding cassette protein exporter, Lip, recognizes a protein region upstream of the C terminus for specific secretion J Biol Chem 2001, 276(29):27111-27119 11335719
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 27111-27119
    • Omori, K.1    Idei, A.2    Akatsuka, H.3
  • 44
    • 0035142648 scopus 로고    scopus 로고
    • Subset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi
    • 95009 11157948
    • Palacios JL Zaror I Martinez P Uribe F Opazo P Socias T Gidekel M Venegas A Subset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi J Bacteriol 2001, 183(4):1346-1358 95009 11157948
    • (2001) J Bacteriol , vol.183 , Issue.4 , pp. 1346-1358
    • Palacios, J.L.1    Zaror, I.2    Martinez, P.3    Uribe, F.4    Opazo, P.5    Socias, T.6    Gidekel, M.7    Venegas, A.8
  • 46
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • 168927 12824332
    • Schwede T Kopp J Guex N Peitsch MC SWISS-MODEL: An automated protein homology-modeling server Nucleic Acids Res 2003, 31(13):3381-3385 168927 12824332
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 47
    • 0019773726 scopus 로고
    • Novel preparation method of immunogen for hydrophobic hapten, enzyme immunoassay for daunomycin and adriamycin
    • 7026686
    • Fujiwara K Yasuno M Kitagawa T Novel preparation method of immunogen for hydrophobic hapten, enzyme immunoassay for daunomycin and adriamycin Journal of immunological methods 1981, 45(2):195-203 7026686
    • (1981) Journal of Immunological Methods , vol.45 , Issue.2 , pp. 195-203
    • Fujiwara, K.1    Yasuno, M.2    Kitagawa, T.3
  • 48
    • 0001030631 scopus 로고
    • Regulation of ribosomal RNA promoters with a synthetic lac operator
    • 392049 6390428
    • Brosius J Holy A Regulation of ribosomal RNA promoters with a synthetic lac operator Proc Natl Acad Sci USA 1984, 81(22):6929-6933 392049 6390428
    • (1984) Proc Natl Acad Sci USA , vol.81 , Issue.22 , pp. 6929-6933
    • Brosius, J.1    Holy, A.2
  • 49
    • 0025184938 scopus 로고
    • Protein secretion in gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin
    • 2211614
    • Delepelaire P Wandersman C Protein secretion in gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin J Biol Chem 1990, 265(28):17118-17125 2211614
    • (1990) J Biol Chem , vol.265 , Issue.28 , pp. 17118-17125
    • Delepelaire, P.1    Wandersman, C.2


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