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Volumn 21, Issue 3, 2015, Pages 261-268

In Silico Evaluation of Different Signal Peptides for the Secretory Production of Human Growth Hormone in E. coli

Author keywords

Bioinformatics; E. coli; Human growth hormone; Signal peptide

Indexed keywords

DSBA PROTEIN; FIMBRIA PROTEIN; HUMAN GROWTH HORMONE; OUTER MEMBRANE PROTEIN C; OUTER MEMBRANE PROTEIN F; PROTEIN SFMC; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 84937980732     PISSN: 15733149     EISSN: 15733904     Source Type: Journal    
DOI: 10.1007/s10989-015-9454-z     Document Type: Article
Times cited : (47)

References (54)
  • 1
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
    • 1:CAS:528:DyaK2sXptlWisg%3D%3D 9084211
    • Arora D, Khanna N (1996) Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J Biotechnol 52(2):127-133
    • (1996) J Biotechnol , vol.52 , Issue.2 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 2
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • 1:CAS:528:DC%2BD2cXptlSlsL4%3D 15529165
    • Baneyx F, Mujacic M (2004) Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22(11):1399-1408
    • (2004) Nat Biotechnol , vol.22 , Issue.11 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 3
    • 84872803348 scopus 로고    scopus 로고
    • Cloning and in silico characterization of two signal peptides from Pediococcus pentosaceus and their function for the secretion of heterologous protein in Lactococcus lactis
    • 1:CAS:528:DC%2BC3sXhsVOhu70%3D 23076361
    • Baradaran A, Sieo CC, Foo HL, Illias RM, Yusoff K, Rahim RA (2013) Cloning and in silico characterization of two signal peptides from Pediococcus pentosaceus and their function for the secretion of heterologous protein in Lactococcus lactis. Biotechnol Lett 35(2):233-238
    • (2013) Biotechnol Lett , vol.35 , Issue.2 , pp. 233-238
    • Baradaran, A.1    Sieo, C.C.2    Foo, H.L.3    Illias, R.M.4    Yusoff, K.5    Rahim, R.A.6
  • 4
    • 0022473255 scopus 로고
    • Expression, secretion and folding of human growth hormone in Escherichia coli: Purification and characterization
    • 1:CAS:528:DyaL28Xls1Khtrk%3D 3527743
    • Becker GW, Hsiung HM (1986) Expression, secretion and folding of human growth hormone in Escherichia coli: purification and characterization. FEBS Lett 204(1):145-150
    • (1986) FEBS Lett , vol.204 , Issue.1 , pp. 145-150
    • Becker, G.W.1    Hsiung, H.M.2
  • 5
    • 0022475473 scopus 로고
    • Conformations of signal peptides induced by lipids suggest initial steps in protein export
    • 1:CAS:528:DyaL28Xls1OisL0%3D 2941862
    • Briggs MS, Cornell DG, Dluhy RA, Gierasch LM (1986) Conformations of signal peptides induced by lipids suggest initial steps in protein export. Science 233(4760):206-208
    • (1986) Science , vol.233 , Issue.4760 , pp. 206-208
    • Briggs, M.S.1    Cornell, D.G.2    Dluhy, R.A.3    Gierasch, L.M.4
  • 6
    • 0023270946 scopus 로고
    • High-level secretion of human growth hormone by Escherichia coli
    • 1:CAS:528:DyaL2sXlvFahsbw%3D 3311882
    • Chang CN, Key M, Bochner B, Heyneker H, Gray G (1987) High-level secretion of human growth hormone by Escherichia coli. Gene 55(2):189-196
    • (1987) Gene , vol.55 , Issue.2 , pp. 189-196
    • Chang, C.N.1    Key, M.2    Bochner, B.3    Heyneker, H.4    Gray, G.5
  • 7
    • 84913538021 scopus 로고    scopus 로고
    • Bioinformatics approaches for improved recombinant protein production in Escherichia coli: Protein solubility prediction
    • 23926206
    • Chang CCH, Song J, Tey BT, Ramanan RN (2014) Bioinformatics approaches for improved recombinant protein production in Escherichia coli: protein solubility prediction. Brief Bioinform 15(6):953-962
    • (2014) Brief Bioinform , vol.15 , Issue.6 , pp. 953-962
    • Chang, C.C.H.1    Song, J.2    Tey, B.T.3    Ramanan, R.N.4
  • 8
    • 0029830550 scopus 로고    scopus 로고
    • Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway
    • 1:CAS:528:DyaK28Xnt1ags7c%3D 178558 8955279
    • Chen H, Kim J, Kendall DA (1996) Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. J Bacteriol 178(23):6658-6664
    • (1996) J Bacteriol , vol.178 , Issue.23 , pp. 6658-6664
    • Chen, H.1    Kim, J.2    Kendall, D.A.3
  • 9
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • 1:CAS:528:DC%2BD2cXjs1eiu7Y%3D 14966662
    • Choi J, Lee S (2004) Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 64(5):625-635
    • (2004) Appl Microbiol Biotechnol , vol.64 , Issue.5 , pp. 625-635
    • Choi, J.1    Lee, S.2
  • 10
    • 0030715279 scopus 로고    scopus 로고
    • Analysis of recombinant human growth hormone directly in osmotic shock fluids
    • 1:CAS:528:DyaK2sXmtFKnu7w%3D 9368400
    • Dalmora S, de Oliveira JE, Affonso R, Gimbo E, Ribela MTC, Bartolini P (1997) Analysis of recombinant human growth hormone directly in osmotic shock fluids. J Chromatogr A 782(2):199-210
    • (1997) J Chromatogr A , vol.782 , Issue.2 , pp. 199-210
    • Dalmora, S.1    De Oliveira, J.E.2    Affonso, R.3    Gimbo, E.4    Ribela, M.T.C.5    Bartolini, P.6
  • 13
    • 84867692604 scopus 로고    scopus 로고
    • The possible role of HSPs on Behçet's disease: A bioinformatic approach
    • 1:CAS:528:DC%2BC38XhsVemtLvJ 23036375
    • Ghasemi Y, Dabbagh F, Rasoul-Amini S, Borhani Haghighi A, Morowvat MH (2012) The possible role of HSPs on Behçet's disease: a bioinformatic approach. Comput Biol Med 42(11):1079-1085
    • (2012) Comput Biol Med , vol.42 , Issue.11 , pp. 1079-1085
    • Ghasemi, Y.1    Dabbagh, F.2    Rasoul-Amini, S.3    Borhani Haghighi, A.4    Morowvat, M.H.5
  • 14
    • 0027222194 scopus 로고
    • Efficient processing and export of human growth hormone by heat labile enterotoxin chain B signal sequence
    • 1:CAS:528:DyaK3sXmt1Cgsbg%3D 8370461
    • Ghorpade A, Garg LC (1993) Efficient processing and export of human growth hormone by heat labile enterotoxin chain B signal sequence. FEBS Lett 330(1):61-65
    • (1993) FEBS Lett , vol.330 , Issue.1 , pp. 61-65
    • Ghorpade, A.1    Garg, L.C.2
  • 15
    • 0021334157 scopus 로고
    • Pseudomonas aeruginosa secretes and correctly processes human growth hormone
    • 1:CAS:528:DyaL2cXhsFWqsL0%3D
    • Gray GL, McKeown KA, Jones AJ, Seeburg PH, Heyneker HL (1984) Pseudomonas aeruginosa secretes and correctly processes human growth hormone. Nat Biotechnol 2(2):161-165
    • (1984) Nat Biotechnol , vol.2 , Issue.2 , pp. 161-165
    • Gray, G.L.1    McKeown, K.A.2    Jones, A.J.3    Seeburg, P.H.4    Heyneker, H.L.5
  • 16
    • 0022371052 scopus 로고
    • Periplasmic production of correctly processed human growth hormone in Escherichia coli: Natural and bacterial signal sequences are interchangeable
    • 1:CAS:528:DyaL28XotlSnsA%3D%3D 3912261
    • Gray GL, Baldridge JS, McKeown KS, Heyneker HL, Chang CN (1985) Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable. Gene 39(2):247-254
    • (1985) Gene , vol.39 , Issue.2 , pp. 247-254
    • Gray, G.L.1    Baldridge, J.S.2    McKeown, K.S.3    Heyneker, H.L.4    Chang, C.N.5
  • 17
    • 46849115458 scopus 로고    scopus 로고
    • Secretory expression of human growth hormone in Saccharomyces cerevisiae using three different leader sequences
    • 1:CAS:528:DC%2BD3MXmslSksbs%3D
    • Hahm MS, Chung BH (2001) Secretory expression of human growth hormone in Saccharomyces cerevisiae using three different leader sequences. Biotechnol Bioprocess Eng 6(4):306-309
    • (2001) Biotechnol Bioprocess Eng , vol.6 , Issue.4 , pp. 306-309
    • Hahm, M.S.1    Chung, B.H.2
  • 18
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • Heijne G (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133(1):17-21
    • (1983) Eur J Biochem , vol.133 , Issue.1 , pp. 17-21
    • Heijne, G.1
  • 19
    • 3242878999 scopus 로고    scopus 로고
    • PrediSi: Prediction of signal peptides and their cleavage positions
    • 1:CAS:528:DC%2BD2cXlvFKnur4%3D 441516 15215414
    • Hiller K, Grote A, Scheer M, Münch R, Jahn D (2004) PrediSi: prediction of signal peptides and their cleavage positions. Nucleic Acids Res 32(suppl 2):W375-W379
    • (2004) Nucleic Acids Res , vol.32 , pp. W375-W379
    • Hiller, K.1    Grote, A.2    Scheer, M.3    Münch, R.4    Jahn, D.5
  • 20
    • 0033727599 scopus 로고    scopus 로고
    • High-level periplasmic expression in Escherichia coli using a eukaryotic signal peptide: Importance of codon usage at the 5′ end of the coding sequence
    • 1:CAS:528:DC%2BD3cXnsFWhsbc%3D 11049749
    • Humphreys DP, Sehdev M, Chapman AP, Ganesh R, Smith BJ, King LM, Glover DJ, Reeks DG, Stephens PE (2000) High-level periplasmic expression in Escherichia coli using a eukaryotic signal peptide: importance of codon usage at the 5′ end of the coding sequence. Protein Expr Purif 20(2):252-264
    • (2000) Protein Expr Purif , vol.20 , Issue.2 , pp. 252-264
    • Humphreys, D.P.1    Sehdev, M.2    Chapman, A.P.3    Ganesh, R.4    Smith, B.J.5    King, L.M.6    Glover, D.J.7    Reeks, D.G.8    Stephens, P.E.9
  • 21
    • 0343573330 scopus 로고
    • Role of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane
    • 1:CAS:528:DyaL38XksFahtLs%3D 346435 7048305
    • Inouye S, Soberon X, Franceschini T, Nakamura K, Itakura K, Inouye M (1982) Role of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane. Proc Natl Acad Sci 79(11):3438-3441
    • (1982) Proc Natl Acad Sci , vol.79 , Issue.11 , pp. 3438-3441
    • Inouye, S.1    Soberon, X.2    Franceschini, T.3    Nakamura, K.4    Itakura, K.5    Inouye, M.6
  • 22
    • 0021894457 scopus 로고
    • Mode of action of pituitary growth hormone on target cells
    • 1:CAS:528:DyaL2MXktVSltL0%3D 3888078
    • Isaksson O, Eden S, Jansson J (1985) Mode of action of pituitary growth hormone on target cells. Annu Rev Physiol 47(1):483-499
    • (1985) Annu Rev Physiol , vol.47 , Issue.1 , pp. 483-499
    • Isaksson, O.1    Eden, S.2    Jansson, J.3
  • 23
    • 0023177768 scopus 로고
    • Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli
    • 1:CAS:528:DyaL2sXltFSgurw%3D 2820841
    • Kato C, Kobayashi T, Kudo T, Furusato T, Murakami Y, Tanaka T, Baba H, Oishi T, Ohtsuka E, Ikehara M (1987) Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli. Gene 54(2):197-202
    • (1987) Gene , vol.54 , Issue.2 , pp. 197-202
    • Kato, C.1    Kobayashi, T.2    Kudo, T.3    Furusato, T.4    Murakami, Y.5    Tanaka, T.6    Baba, H.7    Oishi, T.8    Ohtsuka, E.9    Ikehara, M.10
  • 24
    • 84885927117 scopus 로고    scopus 로고
    • Optimisation of signal peptide for recombinant protein secretion in bacterial hosts
    • 1:CAS:528:DC%2BC3sXlvV2htrw%3D 23529680
    • Low KO, Mahadi NM, Illias RM (2013) Optimisation of signal peptide for recombinant protein secretion in bacterial hosts. Appl Microbiol Biotechnol 97(9):3811-3826
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.9 , pp. 3811-3826
    • Low, K.O.1    Mahadi, N.M.2    Illias, R.M.3
  • 25
    • 69949162927 scopus 로고    scopus 로고
    • SOLpro: Accurate sequence-based prediction of protein solubility
    • 1:CAS:528:DC%2BD1MXhtVelu7fE 19549632
    • Magnan CN, Randall A, Baldi P (2009) SOLpro: accurate sequence-based prediction of protein solubility. Bioinformatics 25(17):2200-2207
    • (2009) Bioinformatics , vol.25 , Issue.17 , pp. 2200-2207
    • Magnan, C.N.1    Randall, A.2    Baldi, P.3
  • 26
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • 1:CAS:528:DyaK28XmtFWhtbo%3D 239455 8840785
    • Makrides SC (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 60(3):512-538
    • (1996) Microbiol Rev , vol.60 , Issue.3 , pp. 512-538
    • Makrides, S.C.1
  • 27
    • 0025825078 scopus 로고
    • Growth rate of Escherichia coli
    • 1:CAS:528:DyaK38XjslGnsw%3D%3D 372817 1886524
    • Marr AG (1991) Growth rate of Escherichia coli. Microbiol Rev 55(2):316-333
    • (1991) Microbiol Rev , vol.55 , Issue.2 , pp. 316-333
    • Marr, A.G.1
  • 28
    • 0031043413 scopus 로고    scopus 로고
    • Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids
    • 1:CAS:528:DyaK2sXht1KgtrY%3D 9042967
    • Nesmeyanova MA, Karamyshev AL, Karamysheva ZN, Kalinin AE, Ksenzenko VN, Kajava AV (1997) Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids. FEBS Lett 403(2):203-207
    • (1997) FEBS Lett , vol.403 , Issue.2 , pp. 203-207
    • Nesmeyanova, M.A.1    Karamyshev, A.L.2    Karamysheva, Z.N.3    Kalinin, A.E.4    Ksenzenko, V.N.5    Kajava, A.V.6
  • 29
    • 84896964486 scopus 로고    scopus 로고
    • A novel multi-epitope peptide vaccine against cancer: An in silico approach
    • 1:CAS:528:DC%2BC2cXltl2ntbo%3D 24512916
    • Nezafat N, Ghasemi Y, Javadi G, Khoshnoud MJ, Omidinia E (2014) A novel multi-epitope peptide vaccine against cancer: an in silico approach. J Theor Biol 349:121-134
    • (2014) J Theor Biol , vol.349 , pp. 121-134
    • Nezafat, N.1    Ghasemi, Y.2    Javadi, G.3    Khoshnoud, M.J.4    Omidinia, E.5
  • 30
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • Nielsen H, Krogh A (1998) Prediction of signal peptides and signal anchors by a hidden Markov model. In: Ismb, pp 122-130
    • (1998) Ismb , pp. 122-130
    • Nielsen, H.1    Krogh, A.2
  • 31
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • 1:CAS:528:DyaK2sXhsVersrs%3D 9051728
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10(1):1-6
    • (1997) Protein Eng , vol.10 , Issue.1 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 32
    • 64549120754 scopus 로고    scopus 로고
    • Expression system for recombinant human growth hormone production from Bacillus subtilis
    • 19224557
    • Özdamar TH, Şentürk B, Yilmaz ÖD, Çalik G, Çelik E, Çalik P (2009) Expression system for recombinant human growth hormone production from Bacillus subtilis. Biotechnol Prog 25(1):75-84
    • (2009) Biotechnol Prog , vol.25 , Issue.1 , pp. 75-84
    • Özdamar, T.H.1    Şentürk, B.2    Yilmaz, Ö.D.3    Çalik, G.4    Çelik, E.5    Çalik, P.6
  • 33
    • 84862501228 scopus 로고    scopus 로고
    • The twin-arginine translocation (Tat) protein export pathway
    • 1:CAS:528:DC%2BC38XotlCksL8%3D 22683878
    • Palmer T, Berks BC (2012) The twin-arginine translocation (Tat) protein export pathway. Nat Rev Microbiol 10(7):483-496
    • (2012) Nat Rev Microbiol , vol.10 , Issue.7 , pp. 483-496
    • Palmer, T.1    Berks, B.C.2
  • 34
    • 0020638192 scopus 로고
    • A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides
    • 1:CAS:528:DyaL3sXks1Kmtb4%3D 6345794
    • Perlman D, Halvorson HO (1983) A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol 167(2):391-409
    • (1983) J Mol Biol , vol.167 , Issue.2 , pp. 391-409
    • Perlman, D.1    Halvorson, H.O.2
  • 35
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • 1:CAS:528:DC%2BC3MXht1CrtrbL 21959131
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8(10):785-786
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 36
    • 0031841932 scopus 로고    scopus 로고
    • Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: Requirement for secondary structure at the cleavage junction
    • 1:CAS:528:DyaK1cXjvF2iu7c%3D 9648736
    • Pratap J, Dikshit K (1998) Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction. Mol Gen Genet MGG 258(4):326-333
    • (1998) Mol Gen Genet MGG , vol.258 , Issue.4 , pp. 326-333
    • Pratap, J.1    Dikshit, K.2
  • 37
    • 0026744155 scopus 로고
    • Alterations in the hydrophilic segment of the maltose-binding protein (MBP) signal peptide that affect either export or translation of MBP
    • 1:CAS:528:DyaK3sXjsFGmtA%3D%3D 207610 1400201
    • Puziss JW, Harvey R, Bassford P (1992) Alterations in the hydrophilic segment of the maltose-binding protein (MBP) signal peptide that affect either export or translation of MBP. J Bacteriol 174(20):6488-6497
    • (1992) J Bacteriol , vol.174 , Issue.20 , pp. 6488-6497
    • Puziss, J.W.1    Harvey, R.2    Bassford, P.3
  • 38
    • 77954557401 scopus 로고    scopus 로고
    • In silico analysis of antibody triggering biofilm associated protein in Acinetobacter baumannii
    • 1:CAS:528:DC%2BC3cXhtVansLrK 20600143
    • Rahbar MR, Rasooli I, Mousavi Gargari SL, Amani J, Fattahian Y (2010) In silico analysis of antibody triggering biofilm associated protein in Acinetobacter baumannii. J Theor Biol 266(2):275-290
    • (2010) J Theor Biol , vol.266 , Issue.2 , pp. 275-290
    • Rahbar, M.R.1    Rasooli, I.2    Mousavi Gargari, S.L.3    Amani, J.4    Fattahian, Y.5
  • 40
    • 0037412923 scopus 로고    scopus 로고
    • The many faces of human growth hormone
    • Roehr B (2002) The many faces of human growth hormone. BETA Bull Exp Treat AIDS 15(4):12-16
    • (2002) BETA Bull Exp Treat AIDS , vol.15 , Issue.4 , pp. 12-16
    • Roehr, B.1
  • 41
    • 34548206622 scopus 로고    scopus 로고
    • Interactions that drive Sec-dependent bacterial protein transport
    • 1:CAS:528:DC%2BD2sXosVOqt70%3D 2675607 17676771
    • Rusch SL, Kendall DA (2007) Interactions that drive Sec-dependent bacterial protein transport. Biochemistry 46(34):9665-9673
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9665-9673
    • Rusch, S.L.1    Kendall, D.A.2
  • 42
    • 77955428012 scopus 로고    scopus 로고
    • A software tool to accelerate design of protein constructs for recombinant expression
    • 1:CAS:528:DC%2BC3cXmtFChtLs%3D 20359538
    • Sagemark J, Kraulis P, Weigelt J (2010) A software tool to accelerate design of protein constructs for recombinant expression. Protein Expr Purif 72(2):175-178
    • (2010) Protein Expr Purif , vol.72 , Issue.2 , pp. 175-178
    • Sagemark, J.1    Kraulis, P.2    Weigelt, J.3
  • 43
    • 1442286042 scopus 로고    scopus 로고
    • Periplasmic expression of human growth hormone via plasmid vectors containing the λpL promoter: Use of HPLC for product quantification
    • 1:CAS:528:DC%2BD2cXivFamsb0%3D 14983096
    • Soares CR, Gomide FI, Ueda EK, Bartolini P (2003) Periplasmic expression of human growth hormone via plasmid vectors containing the λPL promoter: use of HPLC for product quantification. Protein Eng 16(12):1131-1138
    • (2003) Protein Eng , vol.16 , Issue.12 , pp. 1131-1138
    • Soares, C.R.1    Gomide, F.I.2    Ueda, E.K.3    Bartolini, P.4
  • 44
    • 33746161571 scopus 로고    scopus 로고
    • Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display
    • 1:CAS:528:DC%2BD28XmvFans7k%3D 16823375
    • Steiner D, Forrer P, Stumpp MT, Plückthun A (2006) Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display. Nat Biotechnol 24(7):823-831
    • (2006) Nat Biotechnol , vol.24 , Issue.7 , pp. 823-831
    • Steiner, D.1    Forrer, P.2    Stumpp, M.T.3    Plückthun, A.4
  • 45
    • 0028957251 scopus 로고
    • Effects of signal peptide mutations on processing of Bacillus stearothermophilus α-amylase in Escherichia coli
    • 1:CAS:528:DyaK2MXksVeisrc%3D 7711904
    • Suominen I, Meyer P, Tilgmann C, Glumoff T, Glumoff V, Käpylä J, Mäntsälä P (1995) Effects of signal peptide mutations on processing of Bacillus stearothermophilus α-amylase in Escherichia coli. Microbiology 141(3):649-654
    • (1995) Microbiology , vol.141 , Issue.3 , pp. 649-654
    • Suominen, I.1    Meyer, P.2    Tilgmann, C.3    Glumoff, T.4    Glumoff, V.5    Käpylä, J.6    Mäntsälä, P.7
  • 46
    • 0032125723 scopus 로고    scopus 로고
    • Recombinant human growth hormone: Old and novel uses
    • 1:CAS:528:DyaK1cXlt1alsbw%3D 9688021
    • Tritos NA, Mantzoros CS (1998) Recombinant human growth hormone: old and novel uses. Am J Med 105(1):44-57
    • (1998) Am J Med , vol.105 , Issue.1 , pp. 44-57
    • Tritos, N.A.1    Mantzoros, C.S.2
  • 47
    • 27244446613 scopus 로고    scopus 로고
    • Type I signal peptidase: An overview
    • 1:CAS:528:DC%2BD2MXpslarsbo%3D 16126156
    • Tuteja R (2005) Type I signal peptidase: an overview. Arch Biochem Biophys 441(2):107-111
    • (2005) Arch Biochem Biophys , vol.441 , Issue.2 , pp. 107-111
    • Tuteja, R.1
  • 48
    • 0343811713 scopus 로고    scopus 로고
    • Secretion of authentic 20-kDa human growth hormone (20 K hGH) in Escherichia coli and properties of the purified product
    • 1:CAS:528:DyaK2sXkslWgtL8%3D 9232032
    • Uchida H, Naito N, Asada N, Wada M, Ikeda M, Kobayashi H, Asanagi M, Mori K, Fujita Y, Konda K (1997) Secretion of authentic 20-kDa human growth hormone (20 K hGH) in Escherichia coli and properties of the purified product. J Biotechnol 55(2):101-112
    • (1997) J Biotechnol , vol.55 , Issue.2 , pp. 101-112
    • Uchida, H.1    Naito, N.2    Asada, N.3    Wada, M.4    Ikeda, M.5    Kobayashi, H.6    Asanagi, M.7    Mori, K.8    Fujita, Y.9    Konda, K.10
  • 49
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • 1:CAS:528:DC%2BD28XktVeiurk%3D 16503059
    • Ventura S, Villaverde A (2006) Protein quality in bacterial inclusion bodies. Trends Biotechnol 24(4):179-185
    • (2006) Trends Biotechnol , vol.24 , Issue.4 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 50
    • 0021099521 scopus 로고
    • Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli
    • 1:CAS:528:DyaL3sXktF2nu78%3D 6343386
    • Vlasuk GP, Inouye S, Ito H, Itakura K, Inouye M (1983) Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli. J Biol Chem 258(11):7141-7148
    • (1983) J Biol Chem , vol.258 , Issue.11 , pp. 7141-7148
    • Vlasuk, G.P.1    Inouye, S.2    Ito, H.3    Itakura, K.4    Inouye, M.5
  • 51
    • 0021856417 scopus 로고
    • Signal sequences: The limits of variation
    • Von Heijne G (1985) Signal sequences: the limits of variation. J Mol Biol 184(1):99-105
    • (1985) J Mol Biol , vol.184 , Issue.1 , pp. 99-105
    • Von Heijne, G.1
  • 52
    • 84923823670 scopus 로고    scopus 로고
    • Cloning, expression and purification of a synthetic human growth hormone in Escherichia coli: Response surface methodology approach
    • 10.1007/s12033-014-9818-1
    • Zamani M, Berenjian A, Hemmati S, Nezafat N, Ghoshoon MB, Dabbagh F, Mohkam M, Ghasemi Y (2014) Cloning, expression and purification of a synthetic human growth hormone in Escherichia coli: response surface methodology approach. Mol Biotechnol. doi: 10.1007/s12033-014-9818-1
    • (2014) Mol Biotechnol
    • Zamani, M.1    Berenjian, A.2    Hemmati, S.3    Nezafat, N.4    Ghoshoon, M.B.5    Dabbagh, F.6    Mohkam, M.7    Ghasemi, Y.8
  • 54
    • 70350638652 scopus 로고    scopus 로고
    • Construction of recombinant plasmids for periplasmic expression of human growth hormone in Escherichia coli under T7 and lac promoters
    • Zomorodipour A (2003) Construction of recombinant plasmids for periplasmic expression of human growth hormone in Escherichia coli under T7 and lac promoters. J Sci Islamic Repub Iran 14(4):311-316
    • (2003) J Sci Islamic Repub Iran , vol.14 , Issue.4 , pp. 311-316
    • Zomorodipour, A.1


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