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Volumn 9, Issue 1, 2018, Pages 33-46

Antibody-drug conjugates: recent advances in conjugation and linker chemistries

Author keywords

antibody drug conjugates; cancer; chemotherapy; conjugation; linker; site specific conjugation

Indexed keywords

ANTIBODY DRUG CONJUGATE; ANTIGEN; CATHEPSIN B; CYSTEINE; HYDRAZONE DERIVATIVE; MACROGOL; SORTASE; TUMOR ANTIGEN; VANDETANIB; AMINO ACID; ANTIBODY CONJUGATE; MONOCLONAL ANTIBODY;

EID: 84991081605     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-016-0323-0     Document Type: Review
Times cited : (538)

References (64)
  • 1
    • 79953230865 scopus 로고    scopus 로고
    • Monoclonal antibodies—a proven and rapidly expanding therapeutic modality for human diseases
    • PID: 21203944
    • An Z (2010) Monoclonal antibodies—a proven and rapidly expanding therapeutic modality for human diseases. Protein Cell 1:319–330
    • (2010) Protein Cell , vol.1 , pp. 319-330
    • An, Z.1
  • 3
    • 84940100072 scopus 로고    scopus 로고
    • Sortase enzyme-mediated generation of site-specifically conjugated antibody drug conjugates with high in vitro and in vivo potency
    • PID: 26132162
    • Beerli RR, Hell T, Merkel AS, Grawunder U (2015) Sortase enzyme-mediated generation of site-specifically conjugated antibody drug conjugates with high in vitro and in vivo potency. PLoS ONE 10:e0131177
    • (2015) PLoS ONE , vol.10
    • Beerli, R.R.1    Hell, T.2    Merkel, A.S.3    Grawunder, U.4
  • 4
    • 84946567523 scopus 로고    scopus 로고
    • Antibody-drug conjugates (ADCs) derived from interchain cysteine cross-linking demonstrate improved homogeneity and other pharmacological properties over conventional heterogeneous ADCs
    • COI: 1:CAS:528:DC%2BC2MXhsFejtLjE, PID: 26393951
    • Behrens CR, Ha EH, Chinn LL, Bowers S, Probst G, Fitch-Bruhns M, Monteon J, Valdiosera A, Bermudez A, Liao-Chan S et al (2015) Antibody-drug conjugates (ADCs) derived from interchain cysteine cross-linking demonstrate improved homogeneity and other pharmacological properties over conventional heterogeneous ADCs. Mol Pharm 12:3986–3998
    • (2015) Mol Pharm , vol.12 , pp. 3986-3998
    • Behrens, C.R.1    Ha, E.H.2    Chinn, L.L.3    Bowers, S.4    Probst, G.5    Fitch-Bruhns, M.6    Monteon, J.7    Valdiosera, A.8    Bermudez, A.9    Liao-Chan, S.10
  • 5
    • 84910122560 scopus 로고    scopus 로고
    • Antibody–drug conjugates—a new wave of cancer drugs
    • COI: 1:CAS:528:DC%2BC2cXhslOisr7L, PID: 25455482
    • Bouchard H, Viskov C, Garcia-Echeverria C (2014) Antibody–drug conjugates—a new wave of cancer drugs. Bioorg Med Chem Lett 24:5357–5363
    • (2014) Bioorg Med Chem Lett , vol.24 , pp. 5357-5363
    • Bouchard, H.1    Viskov, C.2    Garcia-Echeverria, C.3
  • 6
    • 84930652377 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of cysteine rebridged trastuzumab–MMAE antibody drug conjugates with defined drug-to-antibody ratios
    • COI: 1:CAS:528:DC%2BC2MXms1Onsbg%3D, PID: 25894424
    • Bryant P, Pabst M, Badescu G, Bird M, McDowell W, Jamieson E, Swierkosz J, Jurlewicz K, Tommasi R, Henseleit K et al (2015) In vitro and in vivo evaluation of cysteine rebridged trastuzumab–MMAE antibody drug conjugates with defined drug-to-antibody ratios. Mol Pharm 12:1872–1879
    • (2015) Mol Pharm , vol.12 , pp. 1872-1879
    • Bryant, P.1    Pabst, M.2    Badescu, G.3    Bird, M.4    McDowell, W.5    Jamieson, E.6    Swierkosz, J.7    Jurlewicz, K.8    Tommasi, R.9    Henseleit, K.10
  • 7
    • 84896500653 scopus 로고    scopus 로고
    • Regioselective and stoichiometrically controlled conjugation of photodynamic sensitizers to a HER2 targeting antibody fragment
    • COI: 1:CAS:528:DC%2BC2cXivFOgsb4%3D
    • Bryden F, Maruani A, Savoie H, Chudasama V, Smith MEB, Caddick S, Boyle RW (2014) Regioselective and stoichiometrically controlled conjugation of photodynamic sensitizers to a HER2 targeting antibody fragment. Bioconjugate Chem 25:611–617
    • (2014) Bioconjugate Chem , vol.25 , pp. 611-617
    • Bryden, F.1    Maruani, A.2    Savoie, H.3    Chudasama, V.4    Smith, M.E.B.5    Caddick, S.6    Boyle, R.W.7
  • 8
    • 38949192547 scopus 로고    scopus 로고
    • Targeted cancer therapy: conferring specificity to cytotoxic drugs
    • COI: 1:CAS:528:DC%2BD2sXpt12isLo%3D, PID: 17705444
    • Chari RVJ (2008) Targeted cancer therapy: conferring specificity to cytotoxic drugs. Acc Chem Res 41:98–107
    • (2008) Acc Chem Res , vol.41 , pp. 98-107
    • Chari, R.V.J.1
  • 9
    • 84898066972 scopus 로고    scopus 로고
    • Antibody-drug conjugates: an emerging concept in cancer therapy
    • COI: 1:CAS:528:DC%2BC2cXjtVGmsr0%3D, PID: 24677743
    • Chari RVJ, Miller ML, Widdison WC (2014) Antibody-drug conjugates: an emerging concept in cancer therapy. Angew Chem Int Ed Engl 53:3796–3827
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 3796-3827
    • Chari, R.V.J.1    Miller, M.L.2    Widdison, W.C.3
  • 10
    • 84955494300 scopus 로고    scopus 로고
    • Recent advances in the construction of antibody-drug conjugates
    • COI: 1:CAS:528:DC%2BC28Xjslartg%3D%3D, PID: 26791893
    • Chudasama V, Maruani A, Caddick S (2016) Recent advances in the construction of antibody-drug conjugates. Nat Chem 8:114–119
    • (2016) Nat Chem , vol.8 , pp. 114-119
    • Chudasama, V.1    Maruani, A.2    Caddick, S.3
  • 11
    • 84943581233 scopus 로고    scopus 로고
    • Evolving strategies for target selection for antibody-drug conjugates
    • COI: 1:CAS:528:DC%2BC2MXnvVSmtQ%3D%3D, PID: 25585957
    • Damelin M, Zhong W, Myers J, Sapra P (2015) Evolving strategies for target selection for antibody-drug conjugates. Pharm Res 32:3494–3507
    • (2015) Pharm Res , vol.32 , pp. 3494-3507
    • Damelin, M.1    Zhong, W.2    Myers, J.3    Sapra, P.4
  • 13
    • 55349136976 scopus 로고    scopus 로고
    • A history of cancer chemotherapy
    • COI: 1:CAS:528:DC%2BD1cXhtlSktbbJ, PID: 18974103
    • DeVita VT, Chu E (2008) A history of cancer chemotherapy. Cancer Res 68:8643–8653
    • (2008) Cancer Res , vol.68 , pp. 8643-8653
    • DeVita, V.T.1    Chu, E.2
  • 14
    • 84953431794 scopus 로고    scopus 로고
    • Antibody-drug conjugates-an emerging class of cancer treatment
    • COI: 1:CAS:528:DC%2BC28XlvVGqsg%3D%3D, PID: 26742008
    • Diamantis N, Banerji U (2016) Antibody-drug conjugates-an emerging class of cancer treatment. Br J Cancer 114:362–367
    • (2016) Br J Cancer , vol.114 , pp. 362-367
    • Diamantis, N.1    Banerji, U.2
  • 15
    • 84940838464 scopus 로고    scopus 로고
    • An emerging playbook for antibody-drug conjugates: lessons from the laboratory and clinic suggest a strategy for improving efficacy and safety
    • COI: 1:CAS:528:DC%2BC2MXhsVKksr3I, PID: 26342601
    • Drake PM, Rabuka D (2015) An emerging playbook for antibody-drug conjugates: lessons from the laboratory and clinic suggest a strategy for improving efficacy and safety. Curr Opin Chem Biol 28:174–180
    • (2015) Curr Opin Chem Biol , vol.28 , pp. 174-180
    • Drake, P.M.1    Rabuka, D.2
  • 16
    • 0036074253 scopus 로고    scopus 로고
    • Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity
    • COI: 1:CAS:528:DC%2BD38XksFentr8%3D
    • Dubowchik GM, Firestone RA, Padilla L, Willner D, Hofstead SJ, Mosure K, Knipe JO, Lasch SJ, Trail PA (2002) Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity. Bioconjugate Chem 13:855–869
    • (2002) Bioconjugate Chem , vol.13 , pp. 855-869
    • Dubowchik, G.M.1    Firestone, R.A.2    Padilla, L.3    Willner, D.4    Hofstead, S.J.5    Mosure, K.6    Knipe, J.O.7    Lasch, S.J.8    Trail, P.A.9
  • 17
    • 84937416363 scopus 로고
    • Address in pathology, ON CHEMIOTHERAPY: delivered before the seventeenth International Congress of Medicine
    • COI: 1:STN:280:DC%2BC3MzivVShsg%3D%3D, PID: 20766753
    • Ehrlich P (1913) Address in pathology, ON CHEMIOTHERAPY: delivered before the seventeenth International Congress of Medicine. Br Med J 2:353–359
    • (1913) Br Med J , vol.2 , pp. 353-359
    • Ehrlich, P.1
  • 18
    • 0018875031 scopus 로고
    • The specificity of uptake of model immune complexes and other protein aggregates by the murine reticuloendothelial system
    • COI: 1:CAS:528:DyaL3cXlsVOqt7w%3D, PID: 7410828
    • Finbloom DS, Abeles D, Rifai A, Plotz PH (1980) The specificity of uptake of model immune complexes and other protein aggregates by the murine reticuloendothelial system. J Immunol 125:1060–1065
    • (1980) J Immunol , vol.125 , pp. 1060-1065
    • Finbloom, D.S.1    Abeles, D.2    Rifai, A.3    Plotz, P.H.4
  • 19
    • 0020674198 scopus 로고
    • Localisation and toxicity study of a vindesine-anti-CEA conjugate in patients with advanced cancer
    • COI: 1:STN:280:DyaL3s7gtFSnsw%3D%3D, PID: 6821632
    • Ford CH, Newman CE, Johnson JR, Woodhouse CS, Reeder TA, Rowland GF, Simmonds RG (1983) Localisation and toxicity study of a vindesine-anti-CEA conjugate in patients with advanced cancer. Br J Cancer 47:35–42
    • (1983) Br J Cancer , vol.47 , pp. 35-42
    • Ford, C.H.1    Newman, C.E.2    Johnson, J.R.3    Woodhouse, C.S.4    Reeder, T.A.5    Rowland, G.F.6    Simmonds, R.G.7
  • 20
    • 84873894410 scopus 로고    scopus 로고
    • Cathepsin B as a cancer target
    • COI: 1:CAS:528:DC%2BC3sXislOnur8%3D, PID: 23293836
    • Gondi CS, Rao JS (2013) Cathepsin B as a cancer target. Expert Opin Ther Targets 17:281–291
    • (2013) Expert Opin Ther Targets , vol.17 , pp. 281-291
    • Gondi, C.S.1    Rao, J.S.2
  • 21
    • 79955867207 scopus 로고    scopus 로고
    • The development of pyrrolobenzodiazepines as antitumour agents
    • COI: 1:CAS:528:DC%2BC3MXlvVSktbc%3D, PID: 21457108
    • Hartley JA (2011) The development of pyrrolobenzodiazepines as antitumour agents. Expert Opin Investig Drugs 20:733–744
    • (2011) Expert Opin Investig Drugs , vol.20 , pp. 733-744
    • Hartley, J.A.1
  • 22
    • 84943585919 scopus 로고    scopus 로고
    • Current ADC linker chemistry
    • COI: 1:CAS:528:DC%2BC2MXkt1Omu70%3D, PID: 25759187
    • Jain N, Smith SW, Ghone S, Tomczuk B (2015) Current ADC linker chemistry. Pharm Res 32:3526–3540
    • (2015) Pharm Res , vol.32 , pp. 3526-3540
    • Jain, N.1    Smith, S.W.2    Ghone, S.3    Tomczuk, B.4
  • 25
    • 84957563041 scopus 로고    scopus 로고
    • Discovery of pyrophosphate diesters as tunable, soluble, and bioorthogonal linkers for site-specific antibody-drug conjugates
    • COI: 1:CAS:528:DC%2BC28XltFCgsw%3D%3D, PID: 26745435
    • Kern JC, Cancilla M, Dooney D, Kwasnjuk K, Zhang R, Beaumont M, Figueroa I, Hsieh S, Liang L, Tomazela D et al (2016) Discovery of pyrophosphate diesters as tunable, soluble, and bioorthogonal linkers for site-specific antibody-drug conjugates. J Am Chem Soc 138:1430–1445
    • (2016) J Am Chem Soc , vol.138 , pp. 1430-1445
    • Kern, J.C.1    Cancilla, M.2    Dooney, D.3    Kwasnjuk, K.4    Zhang, R.5    Beaumont, M.6    Figueroa, I.7    Hsieh, S.8    Liang, L.9    Tomazela, D.10
  • 26
    • 0037068501 scopus 로고    scopus 로고
    • Monoclonal antibody conjugates of doxorubicin prepared with branched peptide linkers: inhibition of aggregation by methoxytriethyleneglycol chains
    • COI: 1:CAS:528:DC%2BD38XmtVCntbs%3D, PID: 12213074
    • King HD, Dubowchik GM, Mastalerz H, Willner D, Hofstead SJ, Firestone RA, Lasch SJ, Trail PA (2002) Monoclonal antibody conjugates of doxorubicin prepared with branched peptide linkers: inhibition of aggregation by methoxytriethyleneglycol chains. J Med Chem 45:4336–4343
    • (2002) J Med Chem , vol.45 , pp. 4336-4343
    • King, H.D.1    Dubowchik, G.M.2    Mastalerz, H.3    Willner, D.4    Hofstead, S.J.5    Firestone, R.A.6    Lasch, S.J.7    Trail, P.A.8
  • 27
    • 84886825064 scopus 로고    scopus 로고
    • SGN-CD33A: a novel CD33-targeting antibody-drug conjugate using a pyrrolobenzodiazepine dimer is active in models of drug-resistant AML
    • PID: 23770776
    • Kung Sutherland MS, Walter RB, Jeffrey SC, Burke PJ, Yu C, Kostner H, Stone I, Ryan MC, Sussman D, Lyon RP et al (2013) SGN-CD33A: a novel CD33-targeting antibody-drug conjugate using a pyrrolobenzodiazepine dimer is active in models of drug-resistant AML. Blood 122:1455–1463
    • (2013) Blood , vol.122 , pp. 1455-1463
    • Kung Sutherland, M.S.1    Walter, R.B.2    Jeffrey, S.C.3    Burke, P.J.4    Yu, C.5    Kostner, H.6    Stone, I.7    Ryan, M.C.8    Sussman, D.9    Lyon, R.P.10
  • 28
    • 0024561482 scopus 로고
    • New antitumor monoclonal antibody-vinca conjugates LY203725 and related compounds: design, preparation, and representative in vivo activity
    • COI: 1:CAS:528:DyaL1MXhtVOks7o%3D, PID: 2783975
    • Laguzza BC, Nichols CL, Briggs SL, Cullinan GJ, Johnson DA, Starling JJ, Baker AL, Bumol TF, Corvalan JR (1989) New antitumor monoclonal antibody-vinca conjugates LY203725 and related compounds: design, preparation, and representative in vivo activity. J Med Chem 32:548–555
    • (1989) J Med Chem , vol.32 , pp. 548-555
    • Laguzza, B.C.1    Nichols, C.L.2    Briggs, S.L.3    Cullinan, G.J.4    Johnson, D.A.5    Starling, J.J.6    Baker, A.L.7    Bumol, T.F.8    Corvalan, J.R.9
  • 29
    • 21244469077 scopus 로고    scopus 로고
    • Analysis of the composition of immunoconjugates using size-exclusion chromatography coupled to mass spectrometry
    • COI: 1:CAS:528:DC%2BD2MXmtVegt70%3D, PID: 15945030
    • Lazar AC, Wang L, Blättler WA, Amphlett G, Lambert JM, Zhang W (2005) Analysis of the composition of immunoconjugates using size-exclusion chromatography coupled to mass spectrometry. Rapid Commun Mass Spectrom 19:1806–1814
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 1806-1814
    • Lazar, A.C.1    Wang, L.2    Blättler, W.A.3    Amphlett, G.4    Lambert, J.M.5    Zhang, W.6
  • 30
    • 11844250025 scopus 로고    scopus 로고
    • A passionate kiss, then run: exocytosis and recycling of IgG by FcRn
    • COI: 1:CAS:528:DC%2BD2MXkslOrsA%3D%3D, PID: 15653072
    • Lencer WI, Blumberg RS (2005) A passionate kiss, then run: exocytosis and recycling of IgG by FcRn. Trends Cell Biol 15:5–9
    • (2005) Trends Cell Biol , vol.15 , pp. 5-9
    • Lencer, W.I.1    Blumberg, R.S.2
  • 32
    • 80054092983 scopus 로고    scopus 로고
    • Trastuzumab emtansine: a unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer
    • COI: 1:CAS:528:DC%2BC3MXhtlSksr3N, PID: 22003071
    • LoRusso PM, Weiss D, Guardino E, Girish S, Sliwkowski MX (2011) Trastuzumab emtansine: a unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer. Clin Cancer Res 17:6437–6447
    • (2011) Clin Cancer Res , vol.17 , pp. 6437-6447
    • LoRusso, P.M.1    Weiss, D.2    Guardino, E.3    Girish, S.4    Sliwkowski, M.X.5
  • 34
    • 84859891859 scopus 로고    scopus 로고
    • Engineering of an anti-epidermal growth factor receptor antibody to single chain format and labeling by Sortase A-mediated protein ligation
    • COI: 1:CAS:528:DC%2BC3MXhs1Oiur%2FE, PID: 22170409
    • Madej MP, Coia G, Williams CC, Caine JM, Pearce LA, Attwood R, Bartone NA, Dolezal O, Nisbet RM, Nuttall SD et al (2012) Engineering of an anti-epidermal growth factor receptor antibody to single chain format and labeling by Sortase A-mediated protein ligation. Biotechnol Bioeng 109:1461–1470
    • (2012) Biotechnol Bioeng , vol.109 , pp. 1461-1470
    • Madej, M.P.1    Coia, G.2    Williams, C.C.3    Caine, J.M.4    Pearce, L.A.5    Attwood, R.6    Bartone, N.A.7    Dolezal, O.8    Nisbet, R.M.9    Nuttall, S.D.10
  • 35
    • 84926284885 scopus 로고    scopus 로고
    • A plug-and-play approach to antibody-based therapeutics via a chemoselective dual click strategy
    • COI: 1:CAS:528:DC%2BC2MXotlWqt7s%3D, PID: 25824906
    • Maruani A, Smith MEB, Miranda E, Chester KA, Chudasama V, Caddick S (2015) A plug-and-play approach to antibody-based therapeutics via a chemoselective dual click strategy. Nat Commun 6:6645
    • (2015) Nat Commun , vol.6 , pp. 6645
    • Maruani, A.1    Smith, M.E.B.2    Miranda, E.3    Chester, K.A.4    Chudasama, V.5    Caddick, S.6
  • 36
    • 84961023030 scopus 로고
    • Effect on mouse leukemia 1210 of a combination by diazo-reaction of amethopterin and gamma-globulins from hamsters inoculated with such leukemia by heterografts
    • COI: 1:CAS:528:DyaG1cXptl2ksA%3D%3D, PID: 13537412
    • Mathe G, Loc TB, Bernard J (1958) Effect on mouse leukemia 1210 of a combination by diazo-reaction of amethopterin and gamma-globulins from hamsters inoculated with such leukemia by heterografts. C R Hebd Seances Acad Sci 246:1626–1628
    • (1958) C R Hebd Seances Acad Sci , vol.246 , pp. 1626-1628
    • Mathe, G.1    Loc, T.B.2    Bernard, J.3
  • 37
    • 84939974152 scopus 로고    scopus 로고
    • Antibody drug conjugates: design and selection of linker, payload and conjugation chemistry
    • COI: 1:CAS:528:DC%2BC2MXhslaksrc%3D, PID: 25604608
    • McCombs JR, Owen SC (2015) Antibody drug conjugates: design and selection of linker, payload and conjugation chemistry. AAPS J 17:339–351
    • (2015) AAPS J , vol.17 , pp. 339-351
    • McCombs, J.R.1    Owen, S.C.2
  • 38
    • 0030576641 scopus 로고    scopus 로고
    • Differential distribution of free and bound glutathione and cyst(e)ine in human blood
    • COI: 1:CAS:528:DyaK28Xkt1Ogtbw%3D, PID: 8687493
    • Mills BJ, Lang CA (1996) Differential distribution of free and bound glutathione and cyst(e)ine in human blood. Biochem Pharmacol 52:401–406
    • (1996) Biochem Pharmacol , vol.52 , pp. 401-406
    • Mills, B.J.1    Lang, C.A.2
  • 39
    • 84877310777 scopus 로고    scopus 로고
    • Maturing antibody-drug conjugate pipeline hits 30
    • COI: 1:CAS:528:DC%2BC3sXms1Oiurc%3D, PID: 23629491
    • Mullard A (2013) Maturing antibody-drug conjugate pipeline hits 30. Nat Rev Drug Discov 12:329–332
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 329-332
    • Mullard, A.1
  • 40
    • 84903762549 scopus 로고    scopus 로고
    • Antibody–drug conjugates: current status and future directions
    • COI: 1:CAS:528:DC%2BC3sXhvV2gu7zN, PID: 24239727
    • Perez HL, Cardarelli PM, Deshpande S, Gangwar S (2014) Antibody–drug conjugates: current status and future directions. Drug Discov Today 19:869–881
    • (2014) Drug Discov Today , vol.19 , pp. 869-881
    • Perez, H.L.1    Cardarelli, P.M.2    Deshpande, S.3    Gangwar, S.4
  • 41
    • 78650286160 scopus 로고    scopus 로고
    • Investigational antibody-drug conjugates for hematological malignancies
    • COI: 1:CAS:528:DC%2BC3cXhsFOjsbrP, PID: 21142808
    • Polson AG, Ho WY, Ramakrishnan V (2011) Investigational antibody-drug conjugates for hematological malignancies. Expert Opin Investig Drugs 20:75–85
    • (2011) Expert Opin Investig Drugs , vol.20 , pp. 75-85
    • Polson, A.G.1    Ho, W.Y.2    Ramakrishnan, V.3
  • 42
    • 65249086717 scopus 로고    scopus 로고
    • Site-specific protein labeling via sortase-mediated transpeptidation
    • PID: 19365788
    • Popp MWL, Antos JM, Ploegh HL (2009) Site-specific protein labeling via sortase-mediated transpeptidation. Curr Protoc Protein Sci. doi:10.1002/0471140864.ps1503s56
    • (2009) Curr Protoc Protein Sci
    • Popp, M.W.L.1    Antos, J.M.2    Ploegh, H.L.3
  • 43
    • 84927150740 scopus 로고    scopus 로고
    • Immune checkpoint blockade in cancer therapy
    • COI: 1:CAS:528:DC%2BC2MXhsFKmt7%2FN, PID: 25605845
    • Postow MA, Callahan MK, Wolchok JD (2015) Immune checkpoint blockade in cancer therapy. J Clin Oncol 33:1974–1982
    • (2015) J Clin Oncol , vol.33 , pp. 1974-1982
    • Postow, M.A.1    Callahan, M.K.2    Wolchok, J.D.3
  • 44
    • 79952741743 scopus 로고    scopus 로고
    • Influence of affinity and antigen internalization on the uptake and penetration of Anti-HER2 antibodies in solid tumors
    • COI: 1:CAS:528:DC%2BC3MXjtFWgtLg%3D, PID: 21406401
    • Rudnick SI, Lou J, Shaller CC, Tang Y, Klein-Szanto AJP, Weiner LM, Marks JD, Adams GP (2011) Influence of affinity and antigen internalization on the uptake and penetration of Anti-HER2 antibodies in solid tumors. Cancer Res 71:2250–2259
    • (2011) Cancer Res , vol.71 , pp. 2250-2259
    • Rudnick, S.I.1    Lou, J.2    Shaller, C.C.3    Tang, Y.4    Klein-Szanto, A.J.P.5    Weiner, L.M.6    Marks, J.D.7    Adams, G.P.8
  • 45
    • 0347926091 scopus 로고    scopus 로고
    • Drug delivery strategy utilizing conjugation via reversible disulfide linkages: role and site of cellular reducing activities
    • COI: 1:CAS:528:DC%2BD3sXmsVGiug%3D%3D, PID: 12564977
    • Saito G, Swanson JA, Lee K-D (2003) Drug delivery strategy utilizing conjugation via reversible disulfide linkages: role and site of cellular reducing activities. Adv Drug Deliv Rev 55:199–215
    • (2003) Adv Drug Deliv Rev , vol.55 , pp. 199-215
    • Saito, G.1    Swanson, J.A.2    Lee, K.-D.3
  • 49
    • 84872871265 scopus 로고    scopus 로고
    • Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes
    • PID: 23297227
    • Swee LK, Guimaraes CP, Sehrawat S, Spooner E, Barrasa MI, Ploegh HL (2013) Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes. Proc Natl Acad Sci USA 110:1428–1433
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 1428-1433
    • Swee, L.K.1    Guimaraes, C.P.2    Sehrawat, S.3    Spooner, E.4    Barrasa, M.I.5    Ploegh, H.L.6
  • 50
    • 80054098573 scopus 로고    scopus 로고
    • Antibody conjugate therapeutics: challenges and potential
    • COI: 1:CAS:528:DC%2BC3MXhtlSksrzK, PID: 22003066
    • Teicher BA, Chari RVJ (2011) Antibody conjugate therapeutics: challenges and potential. Clin Cancer Res 17:6389–6397
    • (2011) Clin Cancer Res , vol.17 , pp. 6389-6397
    • Teicher, B.A.1    Chari, R.V.J.2
  • 51
    • 68749099507 scopus 로고    scopus 로고
    • A novel AML-selective TRAIL fusion protein that is superior to Gemtuzumab Ozogamicin in terms of in vitro selectivity, activity and stability
    • PID: 19262596
    • ten Cate B, Bremer E, de Bruyn M, Bijma T, Samplonius D, Schwemmlein M, Huls G, Fey G, Helfrich W (2009) A novel AML-selective TRAIL fusion protein that is superior to Gemtuzumab Ozogamicin in terms of in vitro selectivity, activity and stability. Leukemia 23:1389–1397
    • (2009) Leukemia , vol.23 , pp. 1389-1397
    • ten Cate, B.1    Bremer, E.2    de Bruyn, M.3    Bijma, T.4    Samplonius, D.5    Schwemmlein, M.6    Huls, G.7    Fey, G.8    Helfrich, W.9
  • 54
    • 84945366854 scopus 로고    scopus 로고
    • Chemoenzymatic conjugation of toxic payloads to the globally conserved n-glycan of native mAbs provides homogeneous and highly efficacious antibody-drug conjugates
    • van Geel R, Wijdeven MA, Heesbeen R, Verkade JMM, Wasiel AA, van Berkel SS, van Delft FL (2015) Chemoenzymatic conjugation of toxic payloads to the globally conserved n-glycan of native mAbs provides homogeneous and highly efficacious antibody-drug conjugates. Bioconjugate Chem 26:2233–2242
    • (2015) Bioconjugate Chem , vol.26 , pp. 2233-2242
    • van Geel, R.1    Wijdeven, M.A.2    Heesbeen, R.3    Verkade, J.M.M.4    Wasiel, A.A.5    van Berkel, S.S.6    van Delft, F.L.7
  • 55
    • 84947782114 scopus 로고    scopus 로고
    • Genetically encoded azide containing amino acid in mammalian cells enables site-specific antibody-drug conjugates using click cycloaddition chemistry
    • COI: 1:CAS:528:DC%2BC2MXhsVart7fI
    • VanBrunt MP, Shanebeck K, Caldwell Z, Johnson J, Thompson P, Martin T, Dong H, Li G, Xu H, D’Hooge F et al (2015) Genetically encoded azide containing amino acid in mammalian cells enables site-specific antibody-drug conjugates using click cycloaddition chemistry. Bioconjugate Chem 26:2249–2260
    • (2015) Bioconjugate Chem , vol.26 , pp. 2249-2260
    • VanBrunt, M.P.1    Shanebeck, K.2    Caldwell, Z.3    Johnson, J.4    Thompson, P.5    Martin, T.6    Dong, H.7    Li, G.8    Xu, H.9    D’Hooge, F.10
  • 57
    • 84945561397 scopus 로고    scopus 로고
    • Organometallic palladium reagents for cysteine bioconjugation
    • COI: 1:CAS:528:DC%2BC2MXhslCnu7zK, PID: 26511579
    • Vinogradova EV, Zhang C, Spokoyny AM, Pentelute BL, Buchwald SL (2015) Organometallic palladium reagents for cysteine bioconjugation. Nature 526:687–691
    • (2015) Nature , vol.526 , pp. 687-691
    • Vinogradova, E.V.1    Zhang, C.2    Spokoyny, A.M.3    Pentelute, B.L.4    Buchwald, S.L.5
  • 60
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • COI: 1:CAS:528:DC%2BD2cXitlCrurc%3D, PID: 14988435
    • Wu G, Fang Y-Z, Yang S, Lupton JR, Turner ND (2004) Glutathione metabolism and its implications for health. J Nutr 134:489–492
    • (2004) J Nutr , vol.134 , pp. 489-492
    • Wu, G.1    Fang, Y.-Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.