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Volumn 106, Issue 9, 2009, Pages 3000-3005

Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag

Author keywords

Antibody engineering; Bioorthogonal reaction

Indexed keywords

CELL SURFACE PROTEIN; RECOMBINANT PROTEIN;

EID: 62549121136     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0807820106     Document Type: Article
Times cited : (203)

References (27)
  • 1
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: A summary and pharmacological classification
    • Leader B, Baca QJ, Golan DE (2008) Protein therapeutics: A summary and pharmacological classification. Nat Rev Drug Discovery 7:21-39.
    • (2008) Nat Rev Drug Discovery , vol.7 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 2
    • 0037350545 scopus 로고    scopus 로고
    • Immunotherapy: Past, present and future
    • Waldmann TA (2003) Immunotherapy: Past, present and future. Nat Med 9:269-277.
    • (2003) Nat Med , vol.9 , pp. 269-277
    • Waldmann, T.A.1
  • 3
    • 27744530542 scopus 로고    scopus 로고
    • Site-specific polymer modification of therapeutic proteins
    • Kochendoerfer GG (2005) Site-specific polymer modification of therapeutic proteins. Curr Opin Chem Biol 9:555-560.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 555-560
    • Kochendoerfer, G.G.1
  • 4
  • 5
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • Wu AM, Senter PD (2005) Arming antibodies: Prospects and challenges for immunoconjugates. Nat Biotechnol 23:1137-1146.
    • (2005) Nat Biotechnol , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 6
    • 49449087300 scopus 로고    scopus 로고
    • Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index
    • Junutula JR, et al. (2008) Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nat Biotechnol 26:925-932.
    • (2008) Nat Biotechnol , vol.26 , pp. 925-932
    • Junutula, J.R.1
  • 7
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin BA, Adams SR, Tsien RY (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science 281:269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 11
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
    • Chen I, Howarth M, Lin W, Ting AY (2005) Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat Meth 2:99-104.
    • (2005) Nat Meth , vol.2 , pp. 99-104
    • Chen, I.1    Howarth, M.2    Lin, W.3    Ting, A.Y.4
  • 12
    • 27644508250 scopus 로고    scopus 로고
    • Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase
    • Yin J, et al. (2005) Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase. Proc Natl Acad Sci USA 102:15815-15820.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15815-15820
    • Yin, J.1
  • 13
    • 36849084059 scopus 로고    scopus 로고
    • Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes
    • Fernandez-Suarez M, et al. (2007) Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes. Nat Biotechnol 25:1483-1487.
    • (2007) Nat Biotechnol , vol.25 , pp. 1483-1487
    • Fernandez-Suarez, M.1
  • 14
    • 0037847425 scopus 로고    scopus 로고
    • Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C-alpha-formylglycine generating enzyme
    • Dierks T, et al. (2003) Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C-alpha-formylglycine generating enzyme. Cell 113:435-444.
    • (2003) Cell , vol.113 , pp. 435-444
    • Dierks, T.1
  • 15
    • 8844275956 scopus 로고    scopus 로고
    • Sulfatases: Structure, mechanism, biological activity, inhibition, and synthetic utility
    • Hanson SR, Best MD, Wong CH (2004) Sulfatases: Structure, mechanism, biological activity, inhibition, and synthetic utility. Angew Chem Int Ed 43:5736-5763.
    • (2004) Angew Chem Int Ed , vol.43 , pp. 5736-5763
    • Hanson, S.R.1    Best, M.D.2    Wong, C.H.3
  • 16
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • Carrico IS, Carlson BL, Bertozzi CR (2007) Introducing genetically encoded aldehydes into proteins. Nat Chem Biol 3:321-322.
    • (2007) Nat Chem Biol , vol.3 , pp. 321-322
    • Carrico, I.S.1    Carlson, B.L.2    Bertozzi, C.R.3
  • 17
    • 46349085153 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant proteins: Significance for Biopharmaceuticals
    • Jenkins N, Murphy L, Tyther R (2008) Post-translational modifications of recombinant proteins: Significance for Biopharmaceuticals. Mol Biotechnol 39:113-118.
    • (2008) Mol Biotechnol , vol.39 , pp. 113-118
    • Jenkins, N.1    Murphy, L.2    Tyther, R.3
  • 18
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F,(2006) Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313:670-673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2
  • 19
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • Anthony RM, et al. (2008) Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320:373-376.
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1
  • 20
    • 33744937065 scopus 로고    scopus 로고
    • Monomeric Fc fusions: Impact on pharmacokinetic and biological activity of protein therapeutics
    • Dumont JA, Low SC, Peters RT, Bitonti AJ (2006) Monomeric Fc fusions: Impact on pharmacokinetic and biological activity of protein therapeutics. BioDrugs 20:151-160.
    • (2006) BioDrugs , vol.20 , pp. 151-160
    • Dumont, J.A.1    Low, S.C.2    Peters, R.T.3    Bitonti, A.J.4
  • 21
    • 0034662190 scopus 로고    scopus 로고
    • Detection and quantification of neurotensin in human brain tissue by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Gobom J, et al. (2000) Detection and quantification of neurotensin in human brain tissue by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Chem 72:3320-3326.
    • (2000) Anal Chem , vol.72 , pp. 3320-3326
    • Gobom, J.1
  • 22
    • 33845881958 scopus 로고    scopus 로고
    • Chimeric rabbit/human Fab and IgG specific for members of the Nogo-66 receptor family selected for species cross-reactivity with an improved phage display vector
    • Hofer T, et al. (2007) Chimeric rabbit/human Fab and IgG specific for members of the Nogo-66 receptor family selected for species cross-reactivity with an improved phage display vector. J Immunol Meth 318:75-87.
    • (2007) J Immunol Meth , vol.318 , pp. 75-87
    • Hofer, T.1
  • 23
    • 0036884547 scopus 로고    scopus 로고
    • Integrin alpha(v) beta3 targeted therapy for Kaposi's sarcoma with an in vitro evolved antibody
    • Rader C, Popkov M, Neves JA, Barbas CF, III (2002) Integrin alpha(v) beta3 targeted therapy for Kaposi's sarcoma with an in vitro evolved antibody. FASEB J 16:2000-2002.
    • (2002) FASEB J , vol.16 , pp. 2000-2002
    • Rader, C.1    Popkov, M.2    Neves, J.A.3    Barbas III, C.F.4
  • 24
    • 0027497193 scopus 로고
    • T-cell subsets in autoimmunity
    • O'Garra A, Murphy K (1993) T-cell subsets in autoimmunity. Curr Opin Immunol 5:880-886.
    • (1993) Curr Opin Immunol , vol.5 , pp. 880-886
    • O'Garra, A.1    Murphy, K.2
  • 25
    • 50649087540 scopus 로고    scopus 로고
    • Function and structure of a prokaryotic formylglycine-generating enzyme
    • Carlson BL, et al. (2008) Function and structure of a prokaryotic formylglycine-generating enzyme. J Biol Chem 283:20117-20125.
    • (2008) J Biol Chem , vol.283 , pp. 20117-20125
    • Carlson, B.L.1
  • 26
    • 0141922853 scopus 로고    scopus 로고
    • The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes
    • Landgrebe J, Dierks T, Schmidt B, Von Figura K (2003) The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes. Gene 316:47-56.
    • (2003) Gene , vol.316 , pp. 47-56
    • Landgrebe, J.1    Dierks, T.2    Schmidt, B.3    Von Figura, K.4
  • 27
    • 0037039298 scopus 로고    scopus 로고
    • Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
    • Kiick KL, Saxon E, Tirrell DA, Bertozzi CR (2002) Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc Natl Acad Sci USA 99:19-24.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 19-24
    • Kiick, K.L.1    Saxon, E.2    Tirrell, D.A.3    Bertozzi, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.