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Volumn 41, Issue 5, 2011, Pages 1013-1036

Protein-based tumor molecular imaging probes

Author keywords

Antibody; Human epidermal growth factor receptor (HER); Tumor targeting; Vascular endothelial growth factor (VEGF)

Indexed keywords

6 O ALKYLGUANINE DNA ALKYLTRANSFERASE; ALVESPIMYCIN; CANCER ANTIBODY; CARCINOEMBRYONIC ANTIGEN; CD20 ANTIGEN; CD33 ANTIGEN; CD4 ANTIGEN; CD52 ANTIGEN; CETUXIMAB; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; EPITHELIAL CELL ADHESION MOLECULE; ETARACIZUMAB; FATTY ACID BINDING PROTEIN; FIBRONECTIN; IMMUNOGLOBULIN G ANTIBODY; LIPOCORTIN 5; PROSTATE SPECIFIC MEMBRANE ANTIGEN; SCAFFOLD PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; SOMATOMEDIN C RECEPTOR; TENASCIN; TRASTUZUMAB; TUMOR MARKER; UNINDEXED DRUG; VASCULOTROPIN RECEPTOR 2; VITRONECTIN RECEPTOR;

EID: 84855221646     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-010-0545-z     Document Type: Review
Times cited : (11)

References (217)
  • 1
    • 0037208969 scopus 로고    scopus 로고
    • Use of inteins for the in vivo production of stable cyclic peptide libraries in e coli
    • Abel-Santos E, Scott CP, Benkovic SJ (2003) Use of inteins for the in vivo production of stable cyclic peptide libraries in E coli. Methods Mol Biol 205:281-294
    • (2003) Methods Mol Biol , vol.205 , pp. 281-294
    • Abel-Santos, E.1    Scott, C.P.2    Benkovic, S.J.3
  • 2
    • 0033506131 scopus 로고    scopus 로고
    • Generating improved single-chain Fv molecules for tumor targeting
    • DOI 10.1016/S0022-1759(99)00161-1, PII S0022175999001611
    • Adams GP, Schier R (1999) Generating improved single-chain Fv molecules for tumor targeting. J Immunol Methods 231(1-2):249-260 (Pubitemid 30394738)
    • (1999) Journal of Immunological Methods , vol.231 , Issue.1-2 , pp. 249-260
    • Adams, G.P.1    Schier, R.2
  • 5
    • 0028690586 scopus 로고
    • Clinical radioimmunolocalization with a rat monoclonal antibody directed against c-erbB-2
    • Allan SM, Dean CJ, Eccles S, Sacks NP (1994) Clinical radioimmunolocalization with a rat monoclonal antibody directed against c-erbB-2. Cell Biophys 24-25:93-98
    • (1994) Cell Biophys , vol.24-25 , pp. 93-98
    • Allan, S.M.1    Dean, C.J.2    Eccles, S.3    Sacks, N.P.4
  • 7
    • 0037667420 scopus 로고    scopus 로고
    • Targeting HER1/EGFR: A molecular approach to cancer therapy
    • Arteaga C (2003) Targeting HER1/EGFR: a molecular approach to cancer therapy. Semin Oncol 30(3 Suppl 7):3-14 (Pubitemid 36828623)
    • (2003) Seminars in Oncology , vol.30 , Issue.3 SUPPL. 7 , pp. 3-14
    • Arteaga, C.L.1
  • 10
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D, Kovaleva E, Schatz PJ (1999) A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci 8(4):921-929 (Pubitemid 29165423)
    • (1999) Protein Science , vol.8 , Issue.4 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 11
    • 33846215917 scopus 로고    scopus 로고
    • Antibody constructs in cancer therapy: Protein engineering strategies to improve exposure in solid tumors
    • DOI 10.1002/cncr.22402
    • Beckman RA, Weiner LM, Davis HM (2007) Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors. Cancer 109(2):170-179 (Pubitemid 46106231)
    • (2007) Cancer , vol.109 , Issue.2 , pp. 170-179
    • Beckman, R.A.1    Weiner, L.M.2    Davis, H.M.3
  • 12
    • 0031911476 scopus 로고    scopus 로고
    • Reducing the renal uptake of radiolabeled antibody fragments and peptides for diagnosis and therapy: Present status, future prospects and limitations
    • DOI 10.1007/s002590050216
    • Behr TM, Goldenberg DM, Becker W (1998) Reducing the renal uptake of radiolabeled antibody fragments and peptides for diagnosis and therapy: present status, future prospects and limitations. Eur J Nucl Med 25(2):201-212 (Pubitemid 28130048)
    • (1998) European Journal of Nuclear Medicine , vol.25 , Issue.2 , pp. 201-212
    • Behr, T.M.1    Goldenberg, D.M.2    Becker, W.3
  • 13
    • 0036533489 scopus 로고    scopus 로고
    • Cytokines as a link between innate and adaptive antitumor immunity
    • DOI 10.1016/S1471-4906(02)02195-6, PII S1471490602021956
    • Belardelli F, Ferrantini M (2002) Cytokines as a link between innate and adaptive antitumor immunity. Trends Immunol 23(4):201-208 (Pubitemid 34260936)
    • (2002) Trends in Immunology , vol.23 , Issue.4 , pp. 201-208
    • Belardelli, F.1    Ferrantini, M.2
  • 14
    • 0037967272 scopus 로고    scopus 로고
    • Tumorigenesis and the angiogenic switch
    • DOI 10.1038/nrc1093
    • Bergers G, Benjamin LE (2003) Tumorigenesis and the angiogenic switch. Nat Rev Cancer 3(6):401-410 (Pubitemid 37328844)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.6 , pp. 401-410
    • Bergers, G.1    Benjamin, L.E.2
  • 16
    • 33747330135 scopus 로고    scopus 로고
    • A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes
    • Berteau O, Guillot A, Benjdia A, Rabot S (2006) A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes. J Biol Chem 281(32):22464-22470
    • (2006) J Biol Chem , vol.281 , Issue.32 , pp. 22464-22470
    • Berteau, O.1    Guillot, A.2    Benjdia, A.3    Rabot, S.4
  • 18
    • 0021713342 scopus 로고
    • Production of functional chimaeric mouse/human antibody
    • DOI 10.1038/312643a0
    • Boulianne GL, Hozumi N, Shulman MJ (1984) Production of functional chimaeric mouse/human antibody. Nature 312(5995):643-646 (Pubitemid 15218335)
    • (1984) Nature , vol.312 , Issue.5995 , pp. 643-646
    • Boulianne, G.L.1    Hozumi, N.2    Shulman, M.J.3
  • 19
    • 58849110330 scopus 로고    scopus 로고
    • A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer
    • Brustad EM, Lemke EA, Schultz PG, Deniz AA (2008) A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer. J Am Chem Soc 130(52):17664-17665
    • (2008) J Am Chem Soc , vol.130 , Issue.52 , pp. 17664-17665
    • Brustad, E.M.1    Lemke, E.A.2    Schultz, P.G.3    Deniz, A.A.4
  • 21
    • 33750377517 scopus 로고    scopus 로고
    • 3
    • DOI 10.1158/0008-5472.CAN-06-1480
    • Cai W, Wu Y, Chen K, Cao Q, Tice DA, Chen X (2006a) In vitro and in vivo characterization of 64Cu-labeled Abegrin, a humanized monoclonal antibody against integrin alpha v beta 3. Cancer Res 66(19):9673-9681 (Pubitemid 44623667)
    • (2006) Cancer Research , vol.66 , Issue.19 , pp. 9673-9681
    • Cai, W.1    Wu, Y.2    Chen, K.3    Cao, Q.4    Tice, D.A.5    Chen, X.6
  • 26
    • 30744479430 scopus 로고    scopus 로고
    • Angiogenesis in life, disease and medicine
    • DOI 10.1038/nature04478, PII NATURE04478
    • Carmeliet P (2005) Angiogenesis in life, disease and medicine. Nature 438(7070):932-936 (Pubitemid 43093958)
    • (2005) Nature , vol.438 , Issue.7070 , pp. 932-936
    • Carmeliet, P.1
  • 27
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • DOI 10.1038/nchembio878, PII NCHEMBIO878
    • Carrico IS, Carlson BL, Bertozzi CR (2007) Introducing genetically encoded aldehydes into proteins. Nat Chem Biol 3(6):321-322 (Pubitemid 46789266)
    • (2007) Nature Chemical Biology , vol.3 , Issue.6 , pp. 321-322
    • Carrico, I.S.1    Carlson, B.L.2    Bertozzi, C.R.3
  • 28
    • 3442890204 scopus 로고    scopus 로고
    • Role of HER receptors family in development and differentiation
    • DOI 10.1002/jcp.20007
    • Casalini P, Iorio MV, Galmozzi E, Menard S (2004) Role of HER receptors family in development and differentiation. J Cell Physiol 200(3):343-350 (Pubitemid 39006925)
    • (2004) Journal of Cellular Physiology , vol.200 , Issue.3 , pp. 343-350
    • Casalini, P.1    Iorio, M.V.2    Galmozzi, E.3    Menard, S.4
  • 31
    • 0034256057 scopus 로고    scopus 로고
    • Antibody engineering and its applications in tumor targeting and intracellular immunization
    • DOI 10.1016/S0378-1097(00)00251-2, PII S0378109700002512
    • Chames P, Baty D (2000) Antibody engineering and its applications in tumor targeting and intracellular immunization. FEMS Microbiol Lett 189(1):1-8 (Pubitemid 30456238)
    • (2000) FEMS Microbiology Letters , vol.189 , Issue.1 , pp. 1-8
    • Chames, P.1    Baty, D.2
  • 32
    • 0027474492 scopus 로고
    • Contribution of platelet microparticle formation and granule secretion to the transmembrane migration of phosphatidylserine
    • Chang CP, Zhao J, Wiedmer T, Sims PJ (1993) Contribution of platelet microparticle formation and granule secretion to the transmembrane migration of phosphatidylserine. J Biol Chem 268(10):7171-7178 (Pubitemid 23105607)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.10 , pp. 7171-7178
    • Chang, C.-P.1    Zhao, J.2    Wiedmer, T.3    Sims, P.J.4
  • 33
    • 74549213819 scopus 로고    scopus 로고
    • Intein-mediated site-specific conjugation of quantum dots to proteins in vivo
    • Charalambous A, Andreou M, Skourides PA (2009) Intein-mediated site-specific conjugation of quantum dots to proteins in vivo. J Nanobiotechnol 7:9
    • (2009) J Nanobiotechnol , vol.7 , pp. 9
    • Charalambous, A.1    Andreou, M.2    Skourides, P.A.3
  • 34
    • 0036701613 scopus 로고    scopus 로고
    • 111In-DTPA-hEGF, chemotherapeutic agents and γ-radiation on EGFR-positive breast cancer cells
    • DOI 10.1016/S0969-8051(02)00325-6, PII S0969805102003256
    • Chen P, Mrkobrada M, Vallis KA et al (2002) Comparative antiproliferative effects of (111)In-DTPA-hEGF, chemotherapeutic agents and gamma-radiation on EGFR-positive breast cancer cells. Nucl Med Biol 29(6):693-699 (Pubitemid 35266670)
    • (2002) Nuclear Medicine and Biology , vol.29 , Issue.6 , pp. 693-699
    • Chen, P.1    Mrkobrada, M.2    Vallis, K.A.3    Cameron, R.4    Sandhu, J.5    Hendler, A.6    Reilly, R.M.7
  • 35
    • 0020583891 scopus 로고
    • The epidermal growth factor (EGF)
    • Cohen S (1983) The epidermal growth factor (EGF). Cancer 51(10):1787-1791 (Pubitemid 13093942)
    • (1983) Cancer , vol.51 , Issue.10 , pp. 1787-1791
    • Cohen, S.1
  • 39
    • 0027978049 scopus 로고
    • Assembly of the prothrombinase complex on lipid vesicles depends on the stereochemical configuration of the polar headgroup of phosphatidylserine
    • Comfurius P, Smeets EF, Willems GM, Bevers EM, Zwaal RF (1994) Assembly of the prothrombinase complex on lipid vesicles depends on the stereochemical configuration of the polar headgroup of phosphatidylserine. Biochemistry 33(34):10319-10324 (Pubitemid 24281797)
    • (1994) Biochemistry , vol.33 , Issue.34 , pp. 10319-10324
    • Comfurius, P.1    Smeets, E.F.2    Willems, G.M.3    Bevers, E.M.4    Zwaal, R.F.A.5
  • 41
    • 0026522680 scopus 로고
    • Factors that govern the specificity of transglutaminase-catalysed modification of proteins and peptides
    • Coussons PJ, Price NC, Kelly SM, Smith B, Sawyer L (1992) Factors that govern the specificity of transglutaminase-catalysed modification of proteins and peptides. Biochem J 282(Pt 3):929-930
    • (1992) Biochem J , vol.282 , Issue.PART 3 , pp. 929-930
    • Coussons, P.J.1    Price, N.C.2    Kelly, S.M.3    Smith, B.4    Sawyer, L.5
  • 43
    • 0033819031 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo and in vitro using small peptide tags
    • Cull MG, Schatz PJ (2000) Biotinylation of proteins in vivo and in vitro using small peptide tags. Methods Enzymol 326:430-440
    • (2000) Methods Enzymol , vol.326 , pp. 430-440
    • Cull, M.G.1    Schatz, P.J.2
  • 44
    • 0028050352 scopus 로고
    • Clinical screening of monoclonal antibodies 323/A3, cSF-25 and K928 for suitability of targetting tumours in the upper aerodigestive and respiratory tract
    • De Bree R, Roos JC, Quak JJ, Den Hollander W, Snow GB, Van Dongen GA (1994) Clinical screening of monoclonal antibodies 323/A3, cSF-25 and K928 for suitability of targeting tumours in the upper aerodigestive and respiratory tract. Nucl Med Commun 15(8):613-627 (Pubitemid 24259775)
    • (1994) Nuclear Medicine Communications , vol.15 , Issue.8 , pp. 613-627
    • De Bree, R.1    Roos, J.C.2    Quak, J.J.3    Den Hollander, W.4    Snow, G.B.5    Van Dongen, G.A.M.S.6
  • 45
    • 0027538924 scopus 로고
    • Rat MAbs to the product of the c-erbB-2 proto-oncogene for diagnosis and therapy in breast cancer
    • Dean CJ, Eccles SA, Valeri M et al (1993) Rat MAbs to the product of the c-erbB-2 proto-oncogene for diagnosis and therapy in breast cancer. Cell Biophys 22(1-3):111-127
    • (1993) Cell Biophys , vol.22 , Issue.1-3 , pp. 111-127
    • Dean, C.J.1    Eccles, S.A.2    Valeri, M.3
  • 46
    • 66649121433 scopus 로고    scopus 로고
    • Development and characterization of clinical-grade 89Zr-trastuzumab for HER2/neu immunoPET imaging
    • Dijkers EC, Kosterink JG, Rademaker AP et al (2009) Development and characterization of clinical-grade 89Zr-trastuzumab for HER2/neu immunoPET imaging. J Nucl Med 50(6):974-981
    • (2009) J Nucl Med , vol.50 , Issue.6 , pp. 974-981
    • Dijkers, E.C.1    Kosterink, J.G.2    Rademaker, A.P.3
  • 47
    • 0021281324 scopus 로고
    • Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
    • Downward J, Yarden Y, Mayes E et al (1984) Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences. Nature 307(5951):521-527 (Pubitemid 14135812)
    • (1984) Nature , vol.307 , Issue.5951 , pp. 521-527
    • Downward, J.1    Yarden, Y.2    Mayes, E.3
  • 49
    • 20444507608 scopus 로고    scopus 로고
    • Chemical synthesis of triple-labelled three-helix bundle binding proteins for specific fluorescent detection of unlabelled protein
    • DOI 10.1002/cbic.200400388
    • Engfeldt T, Renberg B, Brumer H, Nygren PA, Karlstrom AE (2005) Chemical synthesis of triple-labelled three-helix bundle binding proteins for specific fluorescent detection of unlabelled protein. Chembiochem 6(6):1043-1050 (Pubitemid 40825345)
    • (2005) ChemBioChem , vol.6 , Issue.6 , pp. 1043-1050
    • Engfeldt, T.1    Renberg, B.2    Brumer, H.3    Nygren, P.A.4    Karlstrom, A.E.5
  • 51
    • 0039374819 scopus 로고    scopus 로고
    • The in vitro ligation of bacterially expressed proteins using an intein from Methanobacterium thermoautotrophicum
    • Evans TC Jr, Benner J, Xu MQ (1999) The in vitro ligation of bacterially expressed proteins using an intein from Methanobacterium thermoautotrophicum. J Biol Chem 274(7):3923-3926
    • (1999) J Biol Chem , vol.274 , Issue.7 , pp. 3923-3926
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.Q.3
  • 52
    • 0026767229 scopus 로고
    • A new monoclonal antibody for detection of EGF-receptors in western blots and paraffin-embedded tissue sections
    • Fernandez A, Spitzer E, Perez R et al (1992) A new monoclonal antibody for detection of EGF-receptors in western blots and paraffin-embedded tissue sections. J Cell Biochem 49(2):157-165
    • (1992) J Cell Biochem , vol.49 , Issue.2 , pp. 157-165
    • Fernandez, A.1    Spitzer, E.2    Perez, R.3
  • 53
    • 0036782278 scopus 로고    scopus 로고
    • VEGF and the quest for tumour angiogenesis factors
    • DOI 10.1038/nrc909
    • Ferrara N (2002) VEGF and the quest for tumour angiogenesis factors. Nat Rev Cancer 2(10):795-803 (Pubitemid 37328914)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.10 , pp. 795-803
    • Ferrara, N.1
  • 54
    • 4143136640 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Basic science and clinical progress
    • DOI 10.1210/er.2003-0027
    • Ferrara N (2004) Vascular endothelial growth factor: basic science and clinical progress. Endocr Rev 25(4):581-611 (Pubitemid 39099316)
    • (2004) Endocrine Reviews , vol.25 , Issue.4 , pp. 581-611
    • Ferrara, N.1
  • 55
    • 16644395747 scopus 로고    scopus 로고
    • The role of VEGF in the regulation of physiological and pathological angiogenesis
    • Ferrara N (2005) The role of VEGF in the regulation of physiological and pathological angiogenesis. EXS (94):209-231
    • (2005) EXS , vol.94 , pp. 209-231
    • Ferrara, N.1
  • 58
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase- catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • Folk JE (1983) Mechanism and basis for specificity of transglutaminase- catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv Enzymol Relat Areas Mol Biol 54:1-56
    • (1983) Adv Enzymol Relat Areas Mol Biol , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 59
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman J (1995) Angiogenesis in cancer, vascular, rheumatoid and other disease. Nat Med 1(1):27-31
    • (1995) Nat Med , vol.1 , Issue.1 , pp. 27-31
    • Folkman, J.1
  • 60
    • 36549039553 scopus 로고    scopus 로고
    • Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase
    • DOI 10.1016/j.addr.2007.06.015, PII S0169409X07001354, Peptide and Protein PEGylation III: Advances in Chemistry and Clinical Applications
    • Fontana A, Spolaore B, Mero A, Veronese FM (2008) Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase. Adv Drug Deliv Rev 60(1):13-28 (Pubitemid 350181164)
    • (2008) Advanced Drug Delivery Reviews , vol.60 , Issue.1 , pp. 13-28
    • Fontana, A.1    Spolaore, B.2    Mero, A.3    Veronese, F.M.4
  • 61
    • 18544390790 scopus 로고    scopus 로고
    • A phase i trial of antibody directed enzyme prodrug therapy (ADEPT) in patients with advanced colorectal carcinoma or other CEA producing tumours
    • Francis RJ, Sharma SK, Springer C et al (2002) A phase I trial of antibody directed enzyme prodrug therapy (ADEPT) in patients with advanced colorectal carcinoma or other CEA producing tumours. Br J Cancer 87(6):600-607
    • (2002) Br J Cancer , vol.87 , Issue.6 , pp. 600-607
    • Francis, R.J.1    Sharma, S.K.2    Springer, C.3
  • 62
    • 65649127261 scopus 로고    scopus 로고
    • Engineered affinity proteins for tumour-targeting applications
    • Friedman M, Stahl S (2009) Engineered affinity proteins for tumour-targeting applications. Biotechnol Appl Biochem 53(Pt 1):1-29
    • (2009) Biotechnol Appl Biochem , vol.53 , Issue.PART 1 , pp. 1-29
    • Friedman, M.1    Stahl, S.2
  • 64
    • 39149087035 scopus 로고    scopus 로고
    • Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule
    • Friedman M, Orlova A, Johansson E et al (2008) Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule. J Mol Biol 376(5):1388-1402
    • (2008) J Mol Biol , vol.376 , Issue.5 , pp. 1388-1402
    • Friedman, M.1    Orlova, A.2    Johansson, E.3
  • 66
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V, Moss SE (2002) Annexins: from structure to function. Physiol Rev 82(2):331-371 (Pubitemid 34654456)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 68
    • 0037048525 scopus 로고    scopus 로고
    • A novel affinity gene fusion system allowing protein A-based recovery of non-immunoglobulin gene products
    • DOI 10.1016/S0168-1656(02)00158-X, PII S016816560200158X
    • Graslund S, Eklund M, Falk R, Uhlen M, Nygren PA, Stahl S (2002) A novel affinity gene fusion system allowing protein A-based recovery of non-immunoglobulin gene products. J Biotechnol 99(1):41-50 (Pubitemid 35229982)
    • (2002) Journal of Biotechnology , vol.99 , Issue.1 , pp. 41-50
    • Graslund, S.1    Eklund, M.2    Falk, R.3    Uhlen, M.4    Nygren, P.-A.5    Stahl, S.6
  • 69
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg CS, Birckbichler PJ, Rice RH (1991) Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J 5(15):3071-3077 (Pubitemid 21892867)
    • (1991) FASEB Journal , vol.5 , Issue.15 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 71
    • 33845665382 scopus 로고    scopus 로고
    • Selection and characterization of Affibody ligands binding to Alzheimer amyloid β peptides
    • DOI 10.1016/j.jbiotec.2006.09.013, PII S0168165606007826
    • Gronwall C, Jonsson A, Lindstrom S, Gunneriusson E, Stahl S, Herne N (2007a) Selection and characterization of Affibody ligands binding to Alzheimer amyloid beta peptides. J Biotechnol 128(1):162-183 (Pubitemid 44960520)
    • (2007) Journal of Biotechnology , vol.128 , Issue.1 , pp. 162-183
    • Gronwall, C.1    Jonsson, A.2    Lindstrom, S.3    Gunneriusson, E.4    Stahl, S.5    Herne, N.6
  • 74
    • 2142700147 scopus 로고    scopus 로고
    • Targeting the HER-kinase axis in cancer
    • Gross ME, Shazer RL, Agus DB (2004) Targeting the HER-kinase axis in cancer. Semin Oncol 31(1 Suppl 3):9-20 (Pubitemid 38543936)
    • (2004) Seminars in Oncology , vol.31 , Issue.1 SUPPL. 3 , pp. 9-20
    • Gross, M.E.1    Shazer, R.L.2    Agus, D.B.3
  • 75
    • 0032717780 scopus 로고    scopus 로고
    • Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling
    • Gunneriusson E, Nord K, Uhlen M, Nygren P (1999) Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling. Protein Eng 12(10):873-878 (Pubitemid 29533112)
    • (1999) Protein Engineering , vol.12 , Issue.10 , pp. 873-878
    • Gunneriusson, E.1    Nord, K.2    Uhlen, M.3    Nygren, P.-A.4
  • 76
    • 78651309159 scopus 로고    scopus 로고
    • 99mTc-HYNIC-annexin v imaging of early tumor apoptosis in mice after single dose irradiation
    • 99mTc-HYNIC-annexin V imaging of early tumor apoptosis in mice after single dose irradiation. J Exp Clin Cancer Res 28:136
    • (2009) J Exp Clin Cancer Res , vol.28 , pp. 136
    • Guo, M.F.1    Zhao, Y.2    Tian, R.3
  • 77
    • 0036381953 scopus 로고    scopus 로고
    • Genetic modification of adenovirus 5 tropism by a novel class of ligands based on a three-helix bundle scaffold derived from staphylococcal protein A
    • Henning P, Magnusson MK, Gunneriusson E et al (2002) Genetic modification of adenovirus 5 tropism by a novel class of ligands based on a three-helix bundle scaffold derived from staphylococcal protein A. Hum Gene Ther 13(12):1427-1439
    • (2002) Hum Gene Ther , vol.13 , Issue.12 , pp. 1427-1439
    • Henning, P.1    Magnusson, M.K.2    Gunneriusson, E.3
  • 78
    • 0036275534 scopus 로고    scopus 로고
    • Cancer immunotherapy with natural killer cells
    • Herberman RB (2002) Cancer immunotherapy with natural killer cells. Semin Oncol 29(3 Suppl 7):27-30 (Pubitemid 34620432)
    • (2002) Seminars in Oncology , vol.29 , Issue.3 SUPPL. 7 , pp. 27-30
    • Herberman, R.B.1
  • 79
    • 14644440555 scopus 로고    scopus 로고
    • Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis
    • DOI 10.1200/JCO.2005.06.081
    • Hicklin DJ, Ellis LM (2005) Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis. J Clin Oncol 23(5):1011-1027 (Pubitemid 46202320)
    • (2005) Journal of Clinical Oncology , vol.23 , Issue.5 , pp. 1011-1027
    • Hicklin, D.J.1    Ellis, L.M.2
  • 80
  • 82
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • DOI 10.1038/nbt1142, PII N1142
    • Holliger P, Hudson PJ (2005) Engineered antibody fragments and the rise of single domains. Nat Biotechnol 23(9):1126-1136 (Pubitemid 41486394)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 83
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood JD, Cheresh DA (2002) Role of integrins in cell invasion and migration. Nat Rev Cancer 2(2):91-100 (Pubitemid 37328796)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 85
    • 0029890636 scopus 로고    scopus 로고
    • Minibody: A novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts
    • Hu S, Shively L, Raubitschek A et al (1996) Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts. Cancer Res 56(13):3055-3061
    • (1996) Cancer Res , vol.56 , Issue.13 , pp. 3055-3061
    • Hu, S.1    Shively, L.2    Raubitschek, A.3
  • 86
    • 0032822839 scopus 로고    scopus 로고
    • Recombinant antibody constructs in cancer therapy
    • DOI 10.1016/S0952-7915(99)00013-8
    • Hudson PJ (1999) Recombinant antibody constructs in cancer therapy. Curr Opin Immunol 11(5):548-557 (Pubitemid 29462131)
    • (1999) Current Opinion in Immunology , vol.11 , Issue.5 , pp. 548-557
    • Hudson, P.J.1
  • 87
    • 0034077520 scopus 로고    scopus 로고
    • Recombinant antibodies: A novel approach to cancer diagnosis and therapy
    • Hudson PJ (2000) Recombinant antibodies: a novel approach to cancer diagnosis and therapy. Expert Opin Invest Drugs 9(6):1231-1242 (Pubitemid 30342611)
    • (2000) Expert Opinion on Investigational Drugs , vol.9 , Issue.6 , pp. 1231-1242
    • Hudson, P.J.1
  • 88
    • 0033506366 scopus 로고    scopus 로고
    • High avidity scFv multimers; diabodies and triabodies
    • DOI 10.1016/S0022-1759(99)00157-X, PII S002217599900157X
    • Hudson PJ, Kortt AA (1999) High avidity scFv multimers; diabodies and triabodies. J Immunol Methods 231(1-2):177-189 (Pubitemid 30394733)
    • (1999) Journal of Immunological Methods , vol.231 , Issue.1-2 , pp. 177-189
    • Hudson, P.J.1    Kortt, A.A.2
  • 89
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes RO (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110(6):673-687 (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 90
    • 0035844128 scopus 로고    scopus 로고
    • Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus
    • Iwai H, Lingel A, Pluckthun A (2001) Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus. J Biol Chem 276(19):16548-16554
    • (2001) J Biol Chem , vol.276 , Issue.19 , pp. 16548-16554
    • Iwai, H.1    Lingel, A.2    Pluckthun, A.3
  • 92
    • 0022558297 scopus 로고
    • Replacing the complementary determining regions in a human antibody with those from a mouse
    • Jones PT, Dear PH, Foote J, Neuberger MS, Winter G (1986) Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321(6069): 522-525 (Pubitemid 16052256)
    • (1986) Nature , vol.321 , Issue.6069 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3
  • 93
    • 77649180964 scopus 로고    scopus 로고
    • Site-specific labeling of proteins with NMR-active unnatural amino acids
    • Jones DH, Cellitti SE, Hao X et al (2010) Site-specific labeling of proteins with NMR-active unnatural amino acids. J Biomol NMR 46(1):89-100
    • (2010) J Biomol NMR , vol.46 , Issue.1 , pp. 89-100
    • Jones, D.H.1    Cellitti, S.E.2    Hao, X.3
  • 94
    • 0037399074 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo
    • DOI 10.1016/S1074-5521(03)00068-1
    • Juillerat A, Gronemeyer T, Keppler A et al (2003) Directed evolution of O6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo. Chem Biol 10(4):313-317 (Pubitemid 36516649)
    • (2003) Chemistry and Biology , vol.10 , Issue.4 , pp. 313-317
    • Juillerat, A.1    Gronemeyer, T.2    Keppler, A.3    Gendreizig, S.4    Pick, H.5    Vogel, H.6    Johnsson, K.7
  • 95
    • 70349283056 scopus 로고    scopus 로고
    • Fluorescent substrates for covalent protein labeling catalyzed by microbial transglutaminase
    • Kamiya N, Abe H, Goto M, Tsuji Y, Jikuya H (2009) Fluorescent substrates for covalent protein labeling catalyzed by microbial transglutaminase. Org Biomol Chem 7(17):3407-3412
    • (2009) Org Biomol Chem , vol.7 , Issue.17 , pp. 3407-3412
    • Kamiya, N.1    Abe, H.2    Goto, M.3    Tsuji, Y.4    Jikuya, H.5
  • 96
    • 66149167323 scopus 로고    scopus 로고
    • Site-specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase
    • Kampmeier F, Ribbert M, Nachreiner T et al (2009) Site-specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase. Bioconjug Chem 20(5):1010-1015
    • (2009) Bioconjug Chem , vol.20 , Issue.5 , pp. 1010-1015
    • Kampmeier, F.1    Ribbert, M.2    Nachreiner, T.3
  • 97
    • 0035423772 scopus 로고    scopus 로고
    • Dual labeling of a binding protein allows for specific fluorescence detection of native protein
    • DOI 10.1006/abio.2001.5186
    • Karlstrom A, Nygren PA (2001) Dual labeling of a binding protein allows for specific fluorescence detection of native protein. Anal Biochem 295(1):22-30 (Pubitemid 32725022)
    • (2001) Analytical Biochemistry , vol.295 , Issue.1 , pp. 22-30
    • Karlstrom, A.1    Nygren, P.-A.2
  • 98
    • 0029920944 scopus 로고    scopus 로고
    • Identification of vascular endothelial growth factor determinants for binding KDR and FLT-1 receptors Generation of receptor-selective VEGF variants by site-directed mutagenesis
    • Keyt BA, Nguyen HV, Berleau LT et al (1996) Identification of vascular endothelial growth factor determinants for binding KDR and FLT-1 receptors Generation of receptor-selective VEGF variants by site-directed mutagenesis. J Biol Chem 271(10):5638-5646
    • (1996) J Biol Chem , vol.271 , Issue.10 , pp. 5638-5646
    • Keyt, B.A.1    Nguyen, H.V.2    Berleau, L.T.3
  • 99
    • 37149038059 scopus 로고    scopus 로고
    • In vivo molecular imaging to diagnose and subtype tumors through receptor-targeted optically labeled monoclonal antibodies
    • DOI 10.1593/neo.07787
    • Koyama Y, Barrett T, Hama Y, Ravizzini G, Choyke PL, Kobayashi H (2007) In vivo molecular imaging to diagnose and subtype tumors through receptor-targeted optically labeled monoclonal antibodies. Neoplasia 9(12):1021-1029 (Pubitemid 350255349)
    • (2007) Neoplasia , vol.9 , Issue.12 , pp. 1021-1029
    • Koyama, Y.1    Barrett, T.2    Hama, Y.3    Ravizzini, G.4    Choyke, P.L.5    Kobayashi, H.6
  • 100
    • 67650091425 scopus 로고    scopus 로고
    • Changes in HER2 expression in breast cancer xenografts after therapy can be quantified using PET and (18)F-labeled affibody molecules
    • Kramer-Marek G, Kiesewetter DO, Capala J (2009) Changes in HER2 expression in breast cancer xenografts after therapy can be quantified using PET and (18)F-labeled affibody molecules. J Nucl Med 50(7):1131-1139
    • (2009) J Nucl Med , vol.50 , Issue.7 , pp. 1131-1139
    • Kramer-Marek, G.1    Kiesewetter, D.O.2    Capala, J.3
  • 101
    • 41149172339 scopus 로고    scopus 로고
    • A novel affinity protein selection system based on staphylococcal cell surface display and flow cytometry
    • DOI 10.1093/protein/gzm090
    • Kronqvist N, Lofblom J, Jonsson A, Wernerus H, Stahl S (2008) A novel affinity protein selection system based on staphylococcal cell surface display and flow cytometry. Protein Eng Des Sel 21(4):247-255 (Pubitemid 351431053)
    • (2008) Protein Engineering, Design and Selection , vol.21 , Issue.4 , pp. 247-255
    • Kronqvist, N.1    Lofblom, J.2    Jonsson, A.3    Wernerus, H.4    Stahl, S.5
  • 102
    • 0020011459 scopus 로고
    • Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci
    • Langone JJ (1982) Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci. Adv Immunol 32:157-252
    • (1982) Adv Immunol , vol.32 , pp. 157-252
    • Langone, J.J.1
  • 103
    • 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 Discov 7(1):21-39
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.1 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 104
    • 56149088445 scopus 로고    scopus 로고
    • In vivo photoacoustic molecular imaging with simultaneous multiple selective targeting using antibody-conjugated gold nanorods
    • Li PC, Wang CR, Shieh DB et al (2008) In vivo photoacoustic molecular imaging with simultaneous multiple selective targeting using antibody-conjugated gold nanorods. Opt Express 16(23):18605-18615
    • (2008) Opt Express , vol.16 , Issue.23 , pp. 18605-18615
    • Li, P.C.1    Wang, C.R.2    Shieh, D.B.3
  • 105
    • 33646038598 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells
    • Lin CW, Ting AY (2006) Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J Am Chem Soc 128(14):4542-4543
    • (2006) J Am Chem Soc , vol.128 , Issue.14 , pp. 4542-4543
    • Lin, C.W.1    Ting, A.Y.2
  • 106
    • 0021257637 scopus 로고
    • Expression cloning of human EGF receptor complementary DNA: Gene amplification and three related messenger RNA products in A431 cells
    • Lin CR, Chen WS, Kruiger W et al (1984) Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells. Science 224(4651):843-848 (Pubitemid 14102458)
    • (1984) Science , vol.224 , Issue.4651 , pp. 843-848
    • Lin, C.R.1    Chen, W.S.2    Kruiger, W.3
  • 107
    • 0023919219 scopus 로고
    • Regulation and expression of the adaptive response to alkylating agents
    • Lindahl T, Sedgwick B, Sekiguchi M, Nakabeppu Y (1988) Regulation and expression of the adaptive response to alkylating agents. Annu Rev Biochem 57:133-157
    • (1988) Annu Rev Biochem , vol.57 , pp. 133-157
    • Lindahl, T.1    Sedgwick, B.2    Sekiguchi, M.3    Nakabeppu, Y.4
  • 108
    • 3242707674 scopus 로고    scopus 로고
    • Intracellular antibodies as specific reagents for functional ablation: Future therapeutic molecules
    • DOI 10.2174/1566524043360384
    • Lobato MN, Rabbitts TH (2004) Intracellular antibodies as specific reagents for functional ablation: future therapeutic molecules. Curr Mol Med 4(5):519-528 (Pubitemid 38961195)
    • (2004) Current Molecular Medicine , vol.4 , Issue.5 , pp. 519-528
    • Lobato, M.N.1    Rabbitts, T.H.2
  • 110
    • 33846244218 scopus 로고    scopus 로고
    • Site-specifically conjugated anti-HER2 Affibody molecules as one-step reagents for target expression analyses on cells and xenograft samples
    • DOI 10.1016/j.jim.2006.10.013, PII S0022175906003073
    • Lundberg E, Hoiden-Guthenberg I, Larsson B, Uhlen M, Graslund T (2007) Site-specifically conjugated anti-HER2 Affibody molecules as one-step reagents for target expression analyses on cells and xenograft samples. J Immunol Methods 319(1-2):53-63 (Pubitemid 46107467)
    • (2007) Journal of Immunological Methods , vol.319 , Issue.1-2 , pp. 53-63
    • Lundberg, E.1    Hoiden-Guthenberg, I.2    Larsson, B.3    Uhlen, M.4    Graslund, T.5
  • 111
    • 76649094603 scopus 로고    scopus 로고
    • HER2- and EGFRspecific affiprobes: Novel recombinant optical probes for cell imaging
    • Lyakhov I, Zielinski R, Kuban M et al (2010) HER2- and EGFRspecific affiprobes: novel recombinant optical probes for cell imaging. Chembiochem 11(3):345-350
    • (2010) Chembiochem , vol.11 , Issue.3 , pp. 345-350
    • Lyakhov, I.1    Zielinski, R.2    Kuban, M.3
  • 112
    • 1142269594 scopus 로고    scopus 로고
    • Application of Vortex Flow Adsorption Technology to Intein-Mediated Recovery of Recombinant Human α1-Antitrypsin
    • DOI 10.1021/bp0341803
    • Ma J, Cooney CL (2004) Application of vortex flow adsorption technology to intein-mediated recovery of recombinant human alpha1-antitrypsin. Biotechnol Prog 20(1):269-276 (Pubitemid 38204198)
    • (2004) Biotechnology Progress , vol.20 , Issue.1 , pp. 269-276
    • Ma, J.1    Cooney, C.L.2
  • 113
    • 34547439889 scopus 로고    scopus 로고
    • A definition of molecular imaging
    • Mankoff DA (2007) A definition of molecular imaging. J Nucl Med 48(6):18N-21N
    • (2007) J Nucl Med , vol.48 , Issue.6
    • Mankoff, D.A.1
  • 114
    • 0036839143 scopus 로고    scopus 로고
    • Macrophage polarization: Tumor-associated macrophages as a paradigm for polarized M2 mononuclear phagocytes
    • DOI 10.1016/S1471-4906(02)02302-5, PII S1471490602023025
    • Mantovani A, Sozzani S, Locati M, Allavena P, Sica A (2002) Macrophage polarization: tumor-associated macrophages as a paradigm for polarized M2 mononuclear phagocytes. Trends Immunol 23(11):549-555 (Pubitemid 35223554)
    • (2002) Trends in Immunology , vol.23 , Issue.11 , pp. 549-555
    • Mantovani, A.1    Sozzani, S.2    Locati, M.3    Allavena, P.4    Sica, A.5
  • 115
    • 0036006173 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Role in carcinogenesis and chemotherapy
    • DOI 10.1002/bies.10063
    • Margison GP, Santibanez-Koref MF (2002) O6-alkylguanine-DNA alkyltransferase: role in carcinogenesis and chemotherapy. Bioessays 24(3):255-266 (Pubitemid 34248691)
    • (2002) BioEssays , vol.24 , Issue.3 , pp. 255-266
    • Margison, G.P.1    Santibanez-Koref, M.F.2
  • 116
    • 1242338152 scopus 로고    scopus 로고
    • The HER receptor family: A rich target for therapeutic development
    • DOI 10.1016/j.ijrobp.2003.09.093
    • Mass RD (2004) The HER receptor family: a rich target for therapeutic development. Int J Radiat Oncol Biol Phys 58(3):932-940 (Pubitemid 38221153)
    • (2004) International Journal of Radiation Oncology Biology Physics , vol.58 , Issue.3 , pp. 932-940
    • Mass, R.D.1
  • 118
    • 0034753262 scopus 로고    scopus 로고
    • Newer methods of labeling diagnostic agents with Tc-99m
    • Mease RC, Lambert C (2001) Newer methods of labeling diagnostic agents with Tc-99m. Semin Nucl Med 31(4):278-285 (Pubitemid 33027506)
    • (2001) Seminars in Nuclear Medicine , vol.31 , Issue.4 , pp. 278-285
    • Mease, R.C.1    Lambert, C.2
  • 119
    • 0027365034 scopus 로고
    • Calcium-dependent annexin V binding to phospholipids: Stoichiometry, specificity, and the role of negative charge
    • DOI 10.1021/bi00094a030
    • Meers P, Mealy T (1993) Calcium-dependent annexin V binding to phospholipids: stoichiometry, specificity, and the role of negative charge. Biochemistry 32(43):11711-11721 (Pubitemid 23341451)
    • (1993) Biochemistry , vol.32 , Issue.43 , pp. 11711-11721
    • Meers, P.1    Mealy, T.2
  • 120
    • 67649588679 scopus 로고    scopus 로고
    • Probing protein folding using site-specifically encoded unnatural amino acids as FRET donors with tryptophan
    • Miyake-Stoner SJ, Miller AM, Hammill JT et al (2009) Probing protein folding using site-specifically encoded unnatural amino acids as FRET donors with tryptophan. Biochemistry 48(25):5953-5962
    • (2009) Biochemistry , vol.48 , Issue.25 , pp. 5953-5962
    • Miyake-Stoner, S.J.1    Miller, A.M.2    Hammill, J.T.3
  • 121
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • DOI 10.1146/annurev.biochem.72.121801.161900
    • Muir TW (2003) Semisynthesis of proteins by expressed protein ligation. Annu Rev Biochem 72:249-289 (Pubitemid 36930447)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 123
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • DOI 10.1038/nmeth886, PII N886
    • Muralidharan V, Muir TW (2006) Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat Methods 3(6):429-438 (Pubitemid 43811554)
    • (2006) Nature Methods , vol.3 , Issue.6 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 128
    • 68949197399 scopus 로고    scopus 로고
    • Monitoring therapeutic response of human ovarian cancer to 17-DMAG by noninvasive PET imaging with (64)Cu-DOTA-trastuzumab
    • Niu G, Li Z, Cao Q, Chen X (2009) Monitoring therapeutic response of human ovarian cancer to 17-DMAG by noninvasive PET imaging with (64)Cu-DOTA-trastuzumab. Eur J Nucl Med Mol Imaging 36(9):1510-1519
    • (2009) Eur J Nucl Med Mol Imaging , vol.36 , Issue.9 , pp. 1510-1519
    • Niu, G.1    Li, Z.2    Cao, Q.3    Chen, X.4
  • 129
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain
    • Nord K, Gunneriusson E, Ringdahl J, Stahl S, Uhlen M, Nygren PA (1997) Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nat Biotechnol 15(8):772-777 (Pubitemid 27329481)
    • (1997) Nature Biotechnology , vol.15 , Issue.8 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Stahl, S.4    Uhlen, M.5    Nygren, P.-A.6
  • 130
    • 0034625656 scopus 로고    scopus 로고
    • Ligands selected from combinatorial libraries of protein A for use in affinity capture of apolipoprotein A-1(M) and Taq DNA polymerase
    • DOI 10.1016/S0168-1656(00)00232-7, PII S0168165600002327
    • Nord K, Gunneriusson E, Uhlen M, Nygren PA (2000) Ligands selected from combinatorial libraries of protein A for use in affinity capture of apolipoprotein A-1M and taq DNA polymerase. J Biotechnol 80(1):45-54 (Pubitemid 30336349)
    • (2000) Journal of Biotechnology , vol.80 , Issue.1 , pp. 45-54
    • Nord, K.1    Gunneriusson, E.2    Uhlen, M.3    Nygren, P.-A.4
  • 131
    • 0034832744 scopus 로고    scopus 로고
    • Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A
    • DOI 10.1046/j.1432-1327.2001.02344.x
    • Nord K, Nord O, Uhlen M, Kelley B, Ljungqvist C, Nygren PA (2001) Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A. Eur J Biochem 268(15):4269-4277 (Pubitemid 32867311)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.15 , pp. 4269-4277
    • Nord, K.1    Nord, O.2    Uhlen, M.3    Kelley, B.4    Ljungqvist, C.5    Nygren, P.-A.6
  • 132
    • 11144312470 scopus 로고    scopus 로고
    • Fluorescent detection of β-lactamase activity in living Escherichia coli cells via esterase supplementation
    • DOI 10.1016/j.femsle.2004.10.047, PII S0378109704007931
    • Nord O, Gustrin A, Nygren PA (2005) Fluorescent detection of betalactamase activity in living Escherichia coli cells via esterase supplementation. FEMS Microbiol Lett 242(1):73-79 (Pubitemid 40038422)
    • (2005) FEMS Microbiology Letters , vol.242 , Issue.1 , pp. 73-79
    • Nord, O.1    Gustrin, A.2    Nygren, P.-A.3
  • 134
    • 64649090835 scopus 로고    scopus 로고
    • Fluorophore-quencher based activatable targeted optical probes for detecting in vivo cancer metastases
    • Ogawa M, Kosaka N, Longmire MR, Urano Y, Choyke PL, Kobayashi H (2009) Fluorophore-quencher based activatable targeted optical probes for detecting in vivo cancer metastases. Mol Pharm 6(2):386-395
    • (2009) Mol Pharm , vol.6 , Issue.2 , pp. 386-395
    • Ogawa, M.1    Kosaka, N.2    Longmire, M.R.3    Urano, Y.4    Choyke, P.L.5    Kobayashi, H.6
  • 135
    • 33645974332 scopus 로고    scopus 로고
    • Comparative in vivo evaluation of technetium and iodine labels on an anti-HER2 affibody for single-photon imaging of HER2 expression in tumors
    • Orlova A, Nilsson FY, Wikman M et al (2006a) Comparative in vivo evaluation of technetium and iodine labels on an anti-HER2 affibody for single-photon imaging of HER2 expression in tumors. J Nucl Med 47(3):512-519 (Pubitemid 46768494)
    • (2006) Journal of Nuclear Medicine , vol.47 , Issue.3 , pp. 512-519
    • Orlova, A.1    Nilsson, F.Y.2    Wikman, M.3    Widstrom, C.4    Stahl, S.5    Carlsson, J.6    Tolmachev, V.7
  • 136
    • 33646261864 scopus 로고    scopus 로고
    • Tumor imaging using a picomolar affinity HER2 binding affibody molecule
    • Orlova A, Magnusson M, Eriksson TL et al (2006b) Tumor imaging using a picomolar affinity HER2 binding affibody molecule. Cancer Res 66(8):4339-4348
    • (2006) Cancer Res , vol.66 , Issue.8 , pp. 4339-4348
    • Orlova, A.1    Magnusson, M.2    Eriksson, T.L.3
  • 138
    • 69249157205 scopus 로고    scopus 로고
    • SERS imaging of HER2- overexpressed MCF7 cells using antibody-conjugated gold nanorods
    • Park H, Lee S, Chen L et al (2009) SERS imaging of HER2- overexpressed MCF7 cells using antibody-conjugated gold nanorods. Phys Chem Chem Phys 11(34):7444-7449
    • (2009) Phys Chem Chem Phys , vol.11 , Issue.34 , pp. 7444-7449
    • Park, H.1    Lee, S.2    Chen, L.3
  • 139
    • 0026305962 scopus 로고
    • Lymphoscintigraphy using epidermal growth factor as tumour-seeking agent in uterine cervical cancer
    • Pateisky N, Schatten C, Vavra N et al (1991) Lymphoscintigraphy using epidermal growth factor as tumour-seeking agent in uterine cervical cancer. Wien Klin Wochenschr 103(21):654-656
    • (1991) Wien Klin Wochenschr , vol.103 , Issue.21 , pp. 654-656
    • Pateisky, N.1    Schatten, C.2    Vavra, N.3
  • 140
    • 0034028030 scopus 로고    scopus 로고
    • Repair of O(6)-alkylguanine by alkyltransferases
    • Pegg AE (2000) Repair of O(6)-alkylguanine by alkyltransferases. Mutat Res 462(2-3):83-100
    • (2000) Mutat Res , vol.462 , Issue.2-3 , pp. 83-100
    • Pegg, A.E.1
  • 141
    • 0028794564 scopus 로고
    • Structure, function, and inhibition of O6-alkylguanine-DNA alkyltransferase
    • Pegg AE, Dolan ME, Moschel RC (1995) Structure, function, and inhibition of O6-alkylguanine-DNA alkyltransferase. Prog Nucleic Acid Res Mol Biol 51:167-223
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.51 , pp. 167-223
    • Pegg, A.E.1    Dolan, M.E.2    Moschel, R.C.3
  • 142
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • DOI 10.1016/S1380-2933(97)00067-5, PII S1380293397000675
    • Pluckthun A, Pack P (1997) New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology 3(2):83-105 (Pubitemid 27356788)
    • (1997) Immunotechnology , vol.3 , Issue.2 , pp. 83-105
    • Pluckthun, A.1    Pack, P.2
  • 143
    • 67650676003 scopus 로고    scopus 로고
    • Multiple site-specific in vitro labeling of single-chain antibody
    • Ramakrishnan B, Boeggeman E, Manzoni M et al (2009) Multiple site-specific in vitro labeling of single-chain antibody. Bioconjug Chem 20(7):1383-1389
    • (2009) Bioconjug Chem , vol.20 , Issue.7 , pp. 1383-1389
    • Ramakrishnan, B.1    Boeggeman, E.2    Manzoni, M.3
  • 146
    • 69449083591 scopus 로고    scopus 로고
    • A 2-helix small protein labeled with 68Ga for PET imaging of HER2 expression
    • Ren G, Zhang R, Liu Z et al (2009) A 2-helix small protein labeled with 68Ga for PET imaging of HER2 expression. J Nucl Med 50(9):1492-1499
    • (2009) J Nucl Med , vol.50 , Issue.9 , pp. 1492-1499
    • Ren, G.1    Zhang, R.2    Liu, Z.3
  • 148
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • DOI 10.1038/nri2155, PII NRI2155
    • Roopenian DC, Akilesh S (2007) FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 7(9):715-725 (Pubitemid 47327396)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.9 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 150
    • 0026028190 scopus 로고
    • Scintigraphic detection of overexpressed c-erbB-2 protooncogene products by a classswitched murine anti-c-erbB-2 protein monoclonal antibody
    • Saga T, Endo K, Akiyama T et al (1991) Scintigraphic detection of overexpressed c-erbB-2 protooncogene products by a classswitched murine anti-c-erbB-2 protein monoclonal antibody. Cancer Res 51(3):990-994
    • (1991) Cancer Res , vol.51 , Issue.3 , pp. 990-994
    • Saga, T.1    Endo, K.2    Akiyama, T.3
  • 151
    • 34548567115 scopus 로고    scopus 로고
    • Dual-labeled trastuzumab-based imaging agent for the detection of human epidermal growth factor receptor 2 overexpression in breast cancer
    • DOI 10.2967/jnumed.107.042234
    • Sampath L, Kwon S, Ke S et al (2007) Dual-labeled trastuzumabbased imaging agent for the detection of human epidermal growth factor receptor 2 overexpression in breast cancer. J Nucl Med 48(9):1501-1510 (Pubitemid 47397400)
    • (2007) Journal of Nuclear Medicine , vol.48 , Issue.9 , pp. 1501-1510
    • Sampath, L.1    Kwon, S.2    Ke, S.3    Wang, W.4    Schiff, R.5    Mawad, M.E.6    Sevick-Muraca, E.M.7
  • 152
    • 0142184270 scopus 로고    scopus 로고
    • Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering
    • Sandstrom K, Xu Z, Forsberg G, Nygren PA (2003) Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering. Protein Eng 16(9):691-697 (Pubitemid 37314397)
    • (2003) Protein Engineering , vol.16 , Issue.9 , pp. 691-697
    • Sandstrom, K.1    Xu, Z.2    Forsberg, G.3    Nygren, P.-A.4
  • 153
    • 0029802270 scopus 로고    scopus 로고
    • Site-specific modification of interleukin-2 by the combined use of genetic engineering techniques and transglutaminase
    • DOI 10.1021/bi952616k
    • Sato H, Ikeda M, Suzuki K, Hirayama K (1996) Site-specific modification of interleukin-2 by the combined use of genetic engineering techniques and transglutaminase. Biochemistry 35(40):13072-13080 (Pubitemid 26349457)
    • (1996) Biochemistry , vol.35 , Issue.40 , pp. 13072-13080
    • Sato, H.1    Ikeda, M.2    Suzuki, K.3    Hirayama, K.4
  • 154
    • 0025924205 scopus 로고
    • Lymphoscintigraphy with 123I-labelled epidermal growth factor
    • Schatten C, Pateisky N, Vavra N et al (1991) Lymphoscintigraphy with 123I-labelled epidermal growth factor. Lancet 337(8738):395-396
    • (1991) Lancet , vol.337 , Issue.8738 , pp. 395-396
    • Schatten, C.1    Pateisky, N.2    Vavra, N.3
  • 156
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103(2):211-225
    • (2000) Cell , vol.103 , Issue.2 , pp. 211-225
    • Schlessinger, J.1
  • 159
    • 27744495195 scopus 로고    scopus 로고
    • Protein semisynthesis and expressed protein ligation: Chasing a protein's tail
    • DOI 10.1016/j.cbpa.2005.09.018, PII S1367593105001353, Biopolymers / Model Systems
    • Schwarzer D, Cole PA (2005) Protein semisynthesis and expressed protein ligation: chasing a protein's tail. Curr Opin Chem Biol 9(6):561-569 (Pubitemid 41612183)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.6 , pp. 561-569
    • Schwarzer, D.1    Cole, P.A.2
  • 162
    • 0032983924 scopus 로고    scopus 로고
    • In vivo biotinylated recombinant antibodies: High efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments
    • DOI 10.1016/S0022-1759(99)00016-2, PII S0022175999000162
    • Sibler AP, Kempf E, Glacet A, Orfanoudakis G, Bourel D, Weiss E (1999) In vivo biotinylated recombinant antibodies: high efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments. J Immunol Methods 224(1-2):129-140 (Pubitemid 29273987)
    • (1999) Journal of Immunological Methods , vol.224 , Issue.1-2 , pp. 129-140
    • Sibler, A.-P.1    Kempf, E.2    Glacet, A.3    Orfanoudakis, G.4    Bourel, D.5    Weiss, E.6
  • 163
    • 0036385845 scopus 로고    scopus 로고
    • Biological imaging for the diagnosis of inflammatory conditions
    • Signore A, Annovazzi A, Corsetti F et al (2002) Biological imaging for the diagnosis of inflammatory conditions. BioDrugs 16(4):241-259
    • (2002) BioDrugs , vol.16 , Issue.4 , pp. 241-259
    • Signore, A.1    Annovazzi, A.2    Corsetti, F.3
  • 165
    • 0038644077 scopus 로고    scopus 로고
    • Radiolabelled lymphokines and growth factors for in vivo imaging of inflammation, infection and cancer
    • DOI 10.1016/S1471-4906(03)00174-1
    • Signore A, Capriotti G, Scopinaro F, Bonanno E, Modesti A (2003b) Radiolabelled lymphokines and growth factors for in vivo imaging of inflammation, infection and cancer. Trends Immunol 24(7):395-402 (Pubitemid 36830967)
    • (2003) Trends in Immunology , vol.24 , Issue.7 , pp. 395-402
    • Signore, A.1    Capriotti, G.2    Scopinaro, F.3    Bonanno, E.4    Modesti, A.5
  • 166
    • 0345164367 scopus 로고    scopus 로고
    • Receptors of vascular endothelial growth factor/vascular permeability factor (VEGF/ VPF) in fetal and adult human kidney: Localization and [125I]VEGF binding sites
    • Simon M, Rockl W, Hornig C et al (1998) Receptors of vascular endothelial growth factor/vascular permeability factor (VEGF/ VPF) in fetal and adult human kidney: localization and [125I]VEGF binding sites. J Am Soc Nephrol 9(6):1032-1044
    • (1998) J Am Soc Nephrol , vol.9 , Issue.6 , pp. 1032-1044
    • Simon, M.1    Rockl, W.2    Hornig, C.3
  • 167
    • 58149085521 scopus 로고    scopus 로고
    • Site-specific, thiol-mediated conjugation of fluorescent probes to cysteinemodified diabodies targeting CD20 or HER2
    • Sirk SJ, Olafsen T, Barat B, Bauer KB, Wu AM (2008) Site-specific, thiol-mediated conjugation of fluorescent probes to cysteinemodified diabodies targeting CD20 or HER2. Bioconjug Chem 19(12):2527-2534
    • (2008) Bioconjug Chem , vol.19 , Issue.12 , pp. 2527-2534
    • Sirk, S.J.1    Olafsen, T.2    Barat, B.3    Bauer, K.B.4    Wu, A.M.5
  • 169
    • 0026660488 scopus 로고
    • A microtiter plate transglutaminase assay utilizing 5-(biotinamido) pentylamine as substrate
    • Slaughter TF, Achyuthan KE, Lai TS, Greenberg CS (1992) A microtiter plate transglutaminase assay utilizing 5-(biotinamido) pentylamine as substrate. Anal Biochem 205(1):166-171
    • (1992) Anal Biochem , vol.205 , Issue.1 , pp. 166-171
    • Slaughter, T.F.1    Achyuthan, K.E.2    Lai, T.S.3    Greenberg, C.S.4
  • 170
    • 0032520638 scopus 로고    scopus 로고
    • A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli
    • DOI 10.1093/nar/26.6.1414
    • Smith PA, Tripp BC, DiBlasio-Smith EA, Lu Z, LaVallie ER, McCoy JM (1998) A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res 26(6):1414-1420 (Pubitemid 28291615)
    • (1998) Nucleic Acids Research , vol.26 , Issue.6 , pp. 1414-1420
    • Smith, P.A.1    Tripp, B.C.2    DiBlasio-Smith, E.A.3    Lu, Z.4    LaVallie, E.R.5    McCoy, J.M.6
  • 172
    • 0025124471 scopus 로고
    • Rat monoclonal antibodies to the external domain of the product of the C-erbB-2 proto-oncogene
    • Styles JM, Harrison S, Gusterson BA, Dean CJ (1990) Rat monoclonal antibodies to the external domain of the product of the C-erbB-2 proto-oncogene. Int J Cancer 45(2):320-324 (Pubitemid 20061388)
    • (1990) International Journal of Cancer , vol.45 , Issue.2 , pp. 320-324
    • Styles, J.M.1    Harrison, S.2    Gusterson, B.A.3    Dean, C.J.4
  • 174
    • 70349266046 scopus 로고    scopus 로고
    • Site specific protein labeling by enzymatic posttranslational modification
    • Sunbul M, Yin J (2009) Site specific protein labeling by enzymatic posttranslational modification. Org Biomol Chem 7(17):3361-3371
    • (2009) Org Biomol Chem , vol.7 , Issue.17 , pp. 3361-3371
    • Sunbul, M.1    Yin, J.2
  • 177
    • 0028830713 scopus 로고
    • Inhibition of hepatic metastases of human colon cancer in nude mice by a chimeric SF-25 monoclonal antibody
    • Takahashi H, Nakada T, Nakaki M, Wands JR (1995) Inhibition of hepatic metastases of human colon cancer in nude mice by a chimeric SF-25 monoclonal antibody. Gastroenterology 108(1):172-182
    • (1995) Gastroenterology , vol.108 , Issue.1 , pp. 172-182
    • Takahashi, H.1    Nakada, T.2    Nakaki, M.3    Wands, J.R.4
  • 179
    • 1842815920 scopus 로고    scopus 로고
    • Transglutaminase-mediated N- and C-terminal fluorescein labeling of a protein can support the native activity of the modified protein
    • DOI 10.1093/protein/gzh015
    • Taki M, Shiota M, Taira K (2004) Transglutaminase-mediated N- and C-terminal fluorescein labeling of a protein can support the native activity of the modified protein. Protein Eng Des Sel 17(2):119-126 (Pubitemid 38477738)
    • (2004) Protein Engineering, Design and Selection , vol.17 , Issue.2 , pp. 119-126
    • Taki, M.1    Shiota, M.2    Taira, K.3
  • 181
    • 33746006525 scopus 로고    scopus 로고
    • Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins
    • DOI 10.1016/j.ijbiomac.2006.01.012, PII S0141813006000341
    • Tirat A, Freuler F, Stettler T, Mayr LM, Leder L (2006) Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Int J Biol Macromol 39(1-3):66-76 (Pubitemid 44066539)
    • (2006) International Journal of Biological Macromolecules , vol.39 , Issue.1-3 , pp. 66-76
    • Tirat, A.1    Freuler, F.2    Stettler, T.3    Mayr, L.M.4    Leder, L.5
  • 186
    • 0020602654 scopus 로고
    • Gene fusion vectors based on the gene for staphylococcal protein A
    • DOI 10.1016/0378-1119(83)90025-2
    • Uhlen M, Nilsson B, Guss B, Lindberg M, Gatenbeck S, Philipson L (1983) Gene fusion vectors based on the gene for staphylococcal protein A. Gene 23(3):369-378 (Pubitemid 13009986)
    • (1983) Gene , vol.23 , Issue.3 , pp. 369-378
    • Uhlen, M.1    Nillson, B.2    Guss, B.3
  • 187
    • 1642295074 scopus 로고    scopus 로고
    • Development of vascular endothelial growth factor receptor (VEGFR) kinase inhibitors as anti-angiogenic agents in cancer therapy
    • DOI 10.2174/0929867043455756
    • Underiner TL, Ruggeri B, Gingrich DE (2004) Development of vascular endothelial growth factor receptor (VEGFR) kinase inhibitors as anti-angiogenic agents in cancer therapy. Curr Med Chem 11(6):731-745 (Pubitemid 38380047)
    • (2004) Current Medicinal Chemistry , vol.11 , Issue.6 , pp. 731-745
    • Underiner, T.L.1    Ruggeri, B.2    Gingrich, D.E.3
  • 190
    • 0029945204 scopus 로고    scopus 로고
    • A novel assay to measure loss of plasma membrane asymmetry during apoptosis of adherent cells in culture
    • DOI 10.1002/(SICI)1097-0320(19960601)24:2<131::AID-CYTO5>3.0.CO;2-M
    • van Engeland M, Ramaekers FC, Schutte B, Reutelingsperger CP (1996) A novel assay to measure loss of plasma membrane asymmetry during apoptosis of adherent cells in culture. Cytometry 24(2):131-139 (Pubitemid 26202924)
    • (1996) Cytometry , vol.24 , Issue.2 , pp. 131-139
    • Van Engeland, M.1    Ramaekers, F.C.S.2    Schutte, B.3    Reutelingsperger, C.P.M.4
  • 192
    • 0033555628 scopus 로고    scopus 로고
    • Increased binding affinity and valence of recombinant antibody fragments lead to improved targeting of tumoral angiogenesis
    • Viti F, Tarli L, Giovannoni L, Zardi L, Neri D (1999) Increased binding affinity and valence of recombinant antibody fragments lead to improved targeting of tumoral angiogenesis. Cancer Res 59(2):347-352 (Pubitemid 29048866)
    • (1999) Cancer Research , vol.59 , Issue.2 , pp. 347-352
    • Viti, F.1    Tarli, L.2    Giovannoni, L.3    Zardi, L.4    Neri, D.5
  • 193
    • 77954058847 scopus 로고    scopus 로고
    • Protein C-terminal labeling and biotinylation using synthetic peptide and split-intein
    • Volkmann G, Liu XQ (2009) Protein C-terminal labeling and biotinylation using synthetic peptide and split-intein. PLoS One 4(12):e8381
    • (2009) PLoS One , vol.4 , Issue.12
    • Volkmann, G.1    Liu, X.Q.2
  • 194
    • 34248678476 scopus 로고    scopus 로고
    • Biochemical markers in oncology. Part I: Molecular basis. Part II: Clinical uses
    • DOI 10.1016/j.ctrv.2007.01.008, PII S0305737207000096
    • Voorzanger-Rousselot N, Garnero P (2007) Biochemical markers in oncology. Part I. Molecular basis. Part II. Clinical uses. Cancer Treat Rev 33(3):230-283 (Pubitemid 46767942)
    • (2007) Cancer Treatment Reviews , vol.33 , Issue.3 , pp. 230-283
    • Voorzanger-Rousselot, N.1    Garnero, P.2
  • 195
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • DOI 10.1002/anie.200501023
    • Walsh CT, Garneau-Tsodikova S, Gatto GJ Jr (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed Engl 44(45):7342-7372 (Pubitemid 41689988)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.45 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto Jr., G.J.3
  • 198
    • 62649089820 scopus 로고    scopus 로고
    • Site-specifically biotinylated VEGF121 for near-infrared fluorescence imaging of tumor angiogenesis
    • Wang H, Chen K, Niu G, Chen X (2008) Site-specifically biotinylated VEGF121 for near-infrared fluorescence imaging of tumor angiogenesis. Mol Pharm 6(1):285-294
    • (2008) Mol Pharm , vol.6 , Issue.1 , pp. 285-294
    • Wang, H.1    Chen, K.2    Niu, G.3    Chen, X.4
  • 199
    • 0029553186 scopus 로고
    • The effector functions of immunoglobulins: Implications for therapy
    • Ward ES, Ghetie V (1995) The effector functions of immunoglobulins: implications for therapy. Ther Immunol 2(2):77-94 (Pubitemid 26101857)
    • (1995) Therapeutic Immunology , vol.2 , Issue.2 , pp. 77-94
    • Ward, E.S.1    Ghetie, V.2
  • 201
    • 54549111498 scopus 로고    scopus 로고
    • Targeted tumor cell internalization and imaging of multifunctional quantum dot-conjugated immunoliposomes in vitro and in vivo
    • Weng KC, Noble CO, Papahadjopoulos-Sternberg B et al (2008) Targeted tumor cell internalization and imaging of multifunctional quantum dot-conjugated immunoliposomes in vitro and in vivo. Nano Lett 8(9):2851-2857
    • (2008) Nano Lett , vol.8 , Issue.9 , pp. 2851-2857
    • Weng, K.C.1    Noble, C.O.2    Papahadjopoulos-Sternberg, B.3
  • 204
    • 0024509749 scopus 로고
    • Preparation, characterization and application of interleukin-1β mutant proteins with surface-accessible cysteine residues
    • DOI 10.1111/j.1432-1033.1989.tb14584.x
    • Wingfield P, Graber P, Shaw AR, Gronenborn AM, Clore GM, MacDonald HR (1989) Preparation, characterization and application of interleukin-1 beta mutant proteins with surfaceaccessible cysteine residues. Eur J Biochem 179(3):565-571 (Pubitemid 19062331)
    • (1989) European Journal of Biochemistry , vol.179 , Issue.3 , pp. 565-571
    • Wingfield, P.1    Graber, P.2    Shaw, A.R.3    Gronenborn, A.M.4    Clore, G.M.5    MacDonald, H.R.6
  • 205
    • 0024276816 scopus 로고
    • Evidence that the two amino termini of plasma fibronectin are in close proximity: A fluorescence energy transfer study
    • Wolff C, Lai CS (1988) Evidence that the two amino termini of plasma fibronectin are in close proximity: a fluorescence energy transfer study. Biochemistry 27(9):3483-3487
    • (1988) Biochemistry , vol.27 , Issue.9 , pp. 3483-3487
    • Wolff, C.1    Lai, C.S.2
  • 209
    • 62549121136 scopus 로고    scopus 로고
    • Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag
    • Wu P, Shui W, Carlson BL et al (2009) Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proc Natl Acad Sci USA 106(9):3000-3005
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.9 , pp. 3000-3005
    • Wu, P.1    Shui, W.2    Carlson, B.L.3
  • 210
    • 70449512642 scopus 로고    scopus 로고
    • Anti-HER2 IgY antibodyfunctionalized single-walled carbon nanotubes for detection and selective destruction of breast cancer cells
    • Xiao Y, Gao X, Taratula O et al (2009) Anti-HER2 IgY antibodyfunctionalized single-walled carbon nanotubes for detection and selective destruction of breast cancer cells. BMC Cancer 9:351
    • (2009) BMC Cancer , vol.9 , pp. 351
    • Xiao, Y.1    Gao, X.2    Taratula, O.3
  • 211
    • 33749019097 scopus 로고    scopus 로고
    • A chemical toolkit for proteins - An expanded genetic code
    • DOI 10.1038/nrm2005, PII NRM2005
    • Xie J, Schultz PG (2006) A chemical toolkit for proteins-an expanded genetic code. Nat Rev Mol Cell Biol 7(10):775-782 (Pubitemid 44450461)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.10 , pp. 775-782
    • Xie, J.1    Schultz, P.G.2
  • 212
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • DOI 10.1126/science.1069040
    • Xiong JP, Stehle T, Zhang R et al (2002) Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 296(5565):151-155 (Pubitemid 34280076)
    • (2002) Science , vol.296 , Issue.5565 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 213
    • 23444457741 scopus 로고    scopus 로고
    • Recent advances in protein splicing: Manipulating proteins in vitro and in vivo
    • DOI 10.1016/j.copbio.2005.06.012, PII S0958166905001060, Protein Technologies and Commercial Enzymes
    • Xu MQ, Evans TC Jr (2005) Recent advances in protein splicing: manipulating proteins in vitro and in vivo. Curr Opin Biotechnol 16(4):440-446 (Pubitemid 41111531)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.4 , pp. 440-446
    • Xu, M.-Q.1    Evans Jr., T.C.2
  • 216
    • 0032549693 scopus 로고    scopus 로고
    • Level of expression of phospholipid scramblase regulates induced movement of phosphatidylserine to the cell surface
    • DOI 10.1074/jbc.273.12.6603
    • Zhao J, Zhou Q, Wiedmer T, Sims PJ (1998) Level of expression of phospholipid scramblase regulates induced movement of phosphatidylserine to the cell surface. J Biol Chem 273(12):6603-6606 (Pubitemid 28160315)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6603-6606
    • Zhao, J.1    Zhou, Q.2    Wiedmer, T.3    Sims, P.J.4
  • 217
    • 67650555677 scopus 로고    scopus 로고
    • Phosphopantetheinyl transferase catalyzed sitespecific protein labeling with ADP conjugated chemical probes
    • Zou Y, Yin J (2009) Phosphopantetheinyl transferase catalyzed sitespecific protein labeling with ADP conjugated chemical probes. J Am Chem Soc 131(22):7548-7549
    • (2009) J Am Chem Soc , vol.131 , Issue.22 , pp. 7548-7549
    • Zou, Y.1    Yin, J.2


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