메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Taking down the FLAG! how insect cell expression challenges an established tag-system

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROPEPTIDASE; EPITOPE; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN; TYROSINE; ANTIBODY; FLAG PEPTIDE; PEPTIDE; PROTEIN TYROSINE SULFOTRANSFERASE; PROTEIN-TYROSINE SULFOTRANSFERASE; SIALIDASE; SULFOTRANSFERASE;

EID: 84862001696     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037779     Document Type: Article
Times cited : (28)

References (34)
  • 1
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh DS, (2005) Making the most of affinity tags. Trends Biotechnol 23: 316-320.
    • (2005) Trends Biotechnol , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 2
    • 0023714467 scopus 로고
    • A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification
    • Hopp TP, Prickett KS, Price VL, Libby RT, March CJ, et al. (1988) A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification. Bio-Technology 6: 1204-1210.
    • (1988) Bio-Technology , vol.6 , pp. 1204-1210
    • Hopp, T.P.1    Prickett, K.S.2    Price, V.L.3    Libby, R.T.4    March, C.J.5
  • 3
    • 0030152061 scopus 로고    scopus 로고
    • Metal-binding properties of a calcium-dependent monoclonal antibody
    • Hopp TP, Gallis B, Prickett KS, (1996) Metal-binding properties of a calcium-dependent monoclonal antibody. Mol Immunol 33: 601-608.
    • (1996) Mol Immunol , vol.33 , pp. 601-608
    • Hopp, T.P.1    Gallis, B.2    Prickett, K.S.3
  • 4
    • 0024675040 scopus 로고
    • A calcium-dependent antibody for identification and purification of recombinant proteins
    • Prickett KS, Amberg DC, Hopp TP, (1989) A calcium-dependent antibody for identification and purification of recombinant proteins. Biotechniques 7: 580-589.
    • (1989) Biotechniques , vol.7 , pp. 580-589
    • Prickett, K.S.1    Amberg, D.C.2    Hopp, T.P.3
  • 5
    • 0035968046 scopus 로고    scopus 로고
    • Affinity of the monoclonal antibody M1 directed against the FLAG peptide
    • Einhauer A, Jungbauer A, (2001) Affinity of the monoclonal antibody M1 directed against the FLAG peptide. J Chromatogr A 921: 25-30.
    • (2001) J Chromatogr A , vol.921 , pp. 25-30
    • Einhauer, A.1    Jungbauer, A.2
  • 6
    • 0035975859 scopus 로고    scopus 로고
    • The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins
    • Einhauer A, Jungbauer A, (2001) The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins. J Biochem Biophys Methods 49: 455-465.
    • (2001) J Biochem Biophys Methods , vol.49 , pp. 455-465
    • Einhauer, A.1    Jungbauer, A.2
  • 7
    • 33847659368 scopus 로고    scopus 로고
    • Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5
    • Slootstra JW, Kuperus D, Pluckthun A, Meloen RH, (1997) Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5. Mol Divers 2: 156-164.
    • (1997) Mol Divers , vol.2 , pp. 156-164
    • Slootstra, J.W.1    Kuperus, D.2    Pluckthun, A.3    Meloen, R.H.4
  • 8
    • 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 RM, DeGraaf ME, Fischer HD, (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
  • 9
    • 79951521237 scopus 로고    scopus 로고
    • A generic system for the expression and purification of soluble and stable influenza neuraminidase
    • Schmidt PM, Attwood RM, Mohr PG, Barrett SA, McKimm-Breschkin JL, (2011) A generic system for the expression and purification of soluble and stable influenza neuraminidase. PLoS One 6: e16284.
    • (2011) PLoS One , vol.6
    • Schmidt, P.M.1    Attwood, R.M.2    Mohr, P.G.3    Barrett, S.A.4    McKimm-Breschkin, J.L.5
  • 10
    • 77956313833 scopus 로고    scopus 로고
    • Structural and functional basis of resistance to neuraminidase inhibitors of influenza B viruses
    • Oakley AJ, Barrett S, Peat TS, Newman J, Streltsov VA, et al. (2010) Structural and functional basis of resistance to neuraminidase inhibitors of influenza B viruses. J Med Chem 53: 6421-6431.
    • (2010) J Med Chem , vol.53 , pp. 6421-6431
    • Oakley, A.J.1    Barrett, S.2    Peat, T.S.3    Newman, J.4    Streltsov, V.A.5
  • 11
    • 0028948876 scopus 로고
    • Tetrabrachion: a filamentous archaebacterial surface protein assembly of unusual structure and extreme stability
    • Peters J, Nitsch M, Kuhlmorgen B, Golbik R, Lupas A, et al. (1995) Tetrabrachion: a filamentous archaebacterial surface protein assembly of unusual structure and extreme stability. J Mol Biol 245: 385-401.
    • (1995) J Mol Biol , vol.245 , pp. 385-401
    • Peters, J.1    Nitsch, M.2    Kuhlmorgen, B.3    Golbik, R.4    Lupas, A.5
  • 12
    • 0033818702 scopus 로고    scopus 로고
    • Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer
    • Stetefeld J, Jenny M, Schulthess T, Landwehr R, Engel J, et al. (2000) Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer. Nat Struct Biol 7: 772-776.
    • (2000) Nat Struct Biol , vol.7 , pp. 772-776
    • Stetefeld, J.1    Jenny, M.2    Schulthess, T.3    Landwehr, R.4    Engel, J.5
  • 13
    • 0034014055 scopus 로고    scopus 로고
    • Tyrosine sulfation: a modulator of extracellular protein-protein interactions
    • Kehoe JW, Bertozzi CR, (2000) Tyrosine sulfation: a modulator of extracellular protein-protein interactions. Chem Biol 7: R57-61.
    • (2000) Chem Biol , vol.7
    • Kehoe, J.W.1    Bertozzi, C.R.2
  • 14
    • 67349111690 scopus 로고    scopus 로고
    • Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins
    • Stone MJ, Chuang S, Hou X, Shoham M, Zhu JZ, (2009) Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins. N Biotechnol 25: 299-317.
    • (2009) N Biotechnol , vol.25 , pp. 299-317
    • Stone, M.J.1    Chuang, S.2    Hou, X.3    Shoham, M.4    Zhu, J.Z.5
  • 16
    • 0024284753 scopus 로고
    • Inhibition of phosphatase and sulfatase by transition-state analogues
    • Stankiewicz PJ, Gresser MJ, (1988) Inhibition of phosphatase and sulfatase by transition-state analogues. Biochemistry 27: 206-212.
    • (1988) Biochemistry , vol.27 , pp. 206-212
    • Stankiewicz, P.J.1    Gresser, M.J.2
  • 17
    • 70549091167 scopus 로고    scopus 로고
    • Improved detection of intact tyrosine sulfate-containing peptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in linear negative ion mode
    • Drake SK, Hortin GL, (2010) Improved detection of intact tyrosine sulfate-containing peptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in linear negative ion mode. Int J Biochem Cell Biol 42: 174-179.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 174-179
    • Drake, S.K.1    Hortin, G.L.2
  • 18
    • 0032992904 scopus 로고    scopus 로고
    • Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis
    • Severs JC, Carnine M, Eguizabal H, Mock KK, (1999) Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis. Rapid Commun Mass Spectrom 13: 1016-1023.
    • (1999) Rapid Commun Mass Spectrom , vol.13 , pp. 1016-1023
    • Severs, J.C.1    Carnine, M.2    Eguizabal, H.3    Mock, K.K.4
  • 19
    • 0029175429 scopus 로고
    • Liquid secondary-ion mass spectrometry of peptides containing multiple tyrosine-O-sulfates
    • Yagami T, Kitagawa K, Futaki S, (1995) Liquid secondary-ion mass spectrometry of peptides containing multiple tyrosine-O-sulfates. Rapid Commun Mass Spectrom 9: 1335-1341.
    • (1995) Rapid Commun Mass Spectrom , vol.9 , pp. 1335-1341
    • Yagami, T.1    Kitagawa, K.2    Futaki, S.3
  • 20
    • 84862001828 scopus 로고    scopus 로고
    • Novel mini-dystrophin gene dual AAV vectors restore nNOS expression at the sarcolemma
    • Zhang Y, Dongsheng D, (2011) Novel mini-dystrophin gene dual AAV vectors restore nNOS expression at the sarcolemma. Hum Gene Ther.
    • (2011) Hum Gene Ther
    • Zhang, Y.1    Dongsheng, D.2
  • 21
    • 0033080755 scopus 로고    scopus 로고
    • Spontaneous alpha-N-6-phosphogluconoylation of a "His tag" in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins
    • Geoghegan KF, Dixon HB, Rosner PJ, Hoth LR, Lanzetti AJ, et al. (1999) Spontaneous alpha-N-6-phosphogluconoylation of a "His tag" in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal Biochem 267: 169-184.
    • (1999) Anal Biochem , vol.267 , pp. 169-184
    • Geoghegan, K.F.1    Dixon, H.B.2    Rosner, P.J.3    Hoth, L.R.4    Lanzetti, A.J.5
  • 22
    • 33845998556 scopus 로고    scopus 로고
    • Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody
    • Hoffhines AJ, Damoc E, Bridges KG, Leary JA, Moore KL, (2006) Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody. J Biol Chem 281: 37877-37887.
    • (2006) J Biol Chem , vol.281 , pp. 37877-37887
    • Hoffhines, A.J.1    Damoc, E.2    Bridges, K.G.3    Leary, J.A.4    Moore, K.L.5
  • 23
    • 0033772552 scopus 로고    scopus 로고
    • Stabilization of a tyrosine O-sulfate residue by a cationic functional group: formation of a conjugate acid-base pair
    • Yagami T, Kitagawa K, Aida C, Fujiwara H, Futaki S, (2000) Stabilization of a tyrosine O-sulfate residue by a cationic functional group: formation of a conjugate acid-base pair. J Pept Res 56: 239-249.
    • (2000) J Pept Res , vol.56 , pp. 239-249
    • Yagami, T.1    Kitagawa, K.2    Aida, C.3    Fujiwara, H.4    Futaki, S.5
  • 24
    • 0036088377 scopus 로고    scopus 로고
    • The Sulfinator: predicting tyrosine sulfation sites in protein sequences
    • Monigatti F, Gasteiger E, Bairoch A, Jung E, (2002) The Sulfinator: predicting tyrosine sulfation sites in protein sequences. Bioinformatics 18: 769-770.
    • (2002) Bioinformatics , vol.18 , pp. 769-770
    • Monigatti, F.1    Gasteiger, E.2    Bairoch, A.3    Jung, E.4
  • 25
    • 46749128220 scopus 로고    scopus 로고
    • Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine-containing peptides
    • Seibert C, Sakmar TP, (2008) Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine-containing peptides. Biopolymers 90: 459-477.
    • (2008) Biopolymers , vol.90 , pp. 459-477
    • Seibert, C.1    Sakmar, T.P.2
  • 26
    • 0000799431 scopus 로고
    • Interaction of vanadate with phenol and tyrosine: implications for the effects of vanadate on systems regulated by tyrosine phosphorylation
    • Tracey AS, Gresser MJ, (1986) Interaction of vanadate with phenol and tyrosine: implications for the effects of vanadate on systems regulated by tyrosine phosphorylation. Proc Natl Acad Sci U S A 83: 609-613.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 609-613
    • Tracey, A.S.1    Gresser, M.J.2
  • 27
    • 0023720322 scopus 로고
    • Change in binding affinities of 3Y1 secreted fibronectin upon desulfation of tyrosine-O-sulfate
    • Suiko M, Liu MC, (1988) Change in binding affinities of 3Y1 secreted fibronectin upon desulfation of tyrosine-O-sulfate. Biochem Biophys Res Commun 154: 1094-1098.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 1094-1098
    • Suiko, M.1    Liu, M.C.2
  • 28
    • 33845971497 scopus 로고    scopus 로고
    • Using phage display to select antibodies recognizing post-translational modifications independently of sequence context
    • Kehoe JW, Velappan N, Walbolt M, Rasmussen J, King D, et al. (2006) Using phage display to select antibodies recognizing post-translational modifications independently of sequence context. Mol Cell Proteomics 5: 2350-2363.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2350-2363
    • Kehoe, J.W.1    Velappan, N.2    Walbolt, M.3    Rasmussen, J.4    King, D.5
  • 29
    • 33745635392 scopus 로고    scopus 로고
    • Detection of influenza viruses resistant to neuraminidase inhibitors in global surveillance during the first 3 years of their use
    • Monto AS, McKimm-Breschkin JL, Macken C, Hampson AW, Hay A, et al. (2006) Detection of influenza viruses resistant to neuraminidase inhibitors in global surveillance during the first 3 years of their use. Antimicrob Agents Chemother 50: 2395-2402.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2395-2402
    • Monto, A.S.1    McKimm-Breschkin, J.L.2    Macken, C.3    Hampson, A.W.4    Hay, A.5
  • 30
    • 0029063045 scopus 로고
    • Rapid expression of an anti-human C5 chimeric Fab utilizing a vector that replicates in COS and 293 cells
    • Evans MJ, Hartman SL, Wolff DW, Rollins SA, Squinto SP, (1995) Rapid expression of an anti-human C5 chimeric Fab utilizing a vector that replicates in COS and 293 cells. J Immunol Methods 184: 123-138.
    • (1995) J Immunol Methods , vol.184 , pp. 123-138
    • Evans, M.J.1    Hartman, S.L.2    Wolff, D.W.3    Rollins, S.A.4    Squinto, S.P.5
  • 31
    • 27844460147 scopus 로고    scopus 로고
    • Characterization of cathepsin L secreted by Sf21 insect cells
    • Johnson GD, Jiang W, (2005) Characterization of cathepsin L secreted by Sf21 insect cells. Arch Biochem Biophys 444: 7-14.
    • (2005) Arch Biochem Biophys , vol.444 , pp. 7-14
    • Johnson, G.D.1    Jiang, W.2
  • 32
    • 0025678690 scopus 로고
    • The use of tetramethylbenzidine for solid phase immunoassays
    • McKimm-Breschkin JL, (1990) The use of tetramethylbenzidine for solid phase immunoassays. J Immunol Methods 135: 277-280.
    • (1990) J Immunol Methods , vol.135 , pp. 277-280
    • McKimm-Breschkin, J.L.1
  • 33
    • 0030053758 scopus 로고    scopus 로고
    • Generation and characterization of variants of NWS/G70C influenza virus after in vitro passage in 4-amino-Neu5Ac2en and 4-guanidino-Neu5Ac2en
    • McKimm-Breschkin JL, Blick TJ, Sahasrabudhe A, Tiong T, Marshall D, et al. (1996) Generation and characterization of variants of NWS/G70C influenza virus after in vitro passage in 4-amino-Neu5Ac2en and 4-guanidino-Neu5Ac2en. Antimicrob Agents Chemother 40: 40-46.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 40-46
    • McKimm-Breschkin, J.L.1    Blick, T.J.2    Sahasrabudhe, A.3    Tiong, T.4    Marshall, D.5
  • 34
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate
    • Potier M, Mameli L, Belisle M, Dallaire L, Melancon SB, (1979) Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate. Anal Biochem 94: 287-296.
    • (1979) Anal Biochem , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.