메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages

Reorienting the Fab Domains of Trastuzumab Results in Potent HER2 Activators

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; TRASTUZUMAB;

EID: 84871457674     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051817     Document Type: Article
Times cited : (35)

References (33)
  • 1
    • 49449087300 scopus 로고    scopus 로고
    • Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index
    • Junutula JR, Raab H, Clark S, Bhakta S, Leipold DD, et al. (2008) Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nature Biotechnology 26: 925-932.
    • (2008) Nature Biotechnology , vol.26 , pp. 925-932
    • Junutula, J.R.1    Raab, H.2    Clark, S.3    Bhakta, S.4    Leipold, D.D.5
  • 2
    • 77957590621 scopus 로고    scopus 로고
    • Engineered thio-trastuzumab-DM1 conjugate with an improved therapeutic index to target human epidermal growth factor receptor 2-positive breast cancer
    • Junutula JR, Flagella KM, Graham RA, Parsons KL, Ha E, et al. (2010) Engineered thio-trastuzumab-DM1 conjugate with an improved therapeutic index to target human epidermal growth factor receptor 2-positive breast cancer. Clinical Cancer Research 16: 4769-4778.
    • (2010) Clinical Cancer Research , vol.16 , pp. 4769-4778
    • Junutula, J.R.1    Flagella, K.M.2    Graham, R.A.3    Parsons, K.L.4    Ha, E.5
  • 3
    • 70350494468 scopus 로고    scopus 로고
    • Therapeutic potential of an anti-CD79b antibody-drug conjugate, anti-CD79b-vc-MMAE, for the treatment of non-Hodgkin lymphoma
    • Dornan D, Bennett F, Chen Y, Dennis M, Eaton D, et al. (2009) Therapeutic potential of an anti-CD79b antibody-drug conjugate, anti-CD79b-vc-MMAE, for the treatment of non-Hodgkin lymphoma. Blood 114: 2721-2729.
    • (2009) Blood , vol.114 , pp. 2721-2729
    • Dornan, D.1    Bennett, F.2    Chen, Y.3    Dennis, M.4    Eaton, D.5
  • 4
    • 40649126110 scopus 로고    scopus 로고
    • Rapid identification of reactive cysteine residues for site-specific labeling of antibody-Fabs
    • Junutula JR, Bhakta S, Raab H, Ervin KE, Eigenbrot C, et al. (2008) Rapid identification of reactive cysteine residues for site-specific labeling of antibody-Fabs. J Immunol Methods 332: 41-52.
    • (2008) J Immunol Methods , vol.332 , pp. 41-52
    • Junutula, J.R.1    Bhakta, S.2    Raab, H.3    Ervin, K.E.4    Eigenbrot, C.5
  • 5
    • 44449127592 scopus 로고    scopus 로고
    • The epidermal growth factor receptor family: biology driving targeted therapeutics
    • Wieduwilt MJ, Moasser MM, (2008) The epidermal growth factor receptor family: biology driving targeted therapeutics. Cell Mol Life Sci 65: 1566-1584.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1566-1584
    • Wieduwilt, M.J.1    Moasser, M.M.2
  • 7
    • 77950628416 scopus 로고    scopus 로고
    • Mechanisms of resistance to HER family targeting antibodies
    • Kruser TJ, Wheeler DL, (2010) Mechanisms of resistance to HER family targeting antibodies. Exp Cell Res 316: 1083-1100.
    • (2010) Exp Cell Res , vol.316 , pp. 1083-1100
    • Kruser, T.J.1    Wheeler, D.L.2
  • 8
    • 0026502047 scopus 로고
    • High level Escherichia coli expression and production of a bivalent humanized antibody fragment
    • Carter P, Kelley RF, Rodrigues ML, Snedecor B, Covarrubias M, et al. (1992) High level Escherichia coli expression and production of a bivalent humanized antibody fragment. Biotechnology (N Y) 10: 163-167.
    • (1992) Biotechnology (N Y) , vol.10 , pp. 163-167
    • Carter, P.1    Kelley, R.F.2    Rodrigues, M.L.3    Snedecor, B.4    Covarrubias, M.5
  • 9
    • 18344372376 scopus 로고    scopus 로고
    • Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies
    • Simmons LC, Reilly D, Klimowski L, Raju TS, Meng G, et al. (2002) Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies. J Immunol Methods 263: 133-147.
    • (2002) J Immunol Methods , vol.263 , pp. 133-147
    • Simmons, L.C.1    Reilly, D.2    Klimowski, L.3    Raju, T.S.4    Meng, G.5
  • 12
    • 48649092620 scopus 로고    scopus 로고
    • A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy
    • Lee-Hoeflich ST, Crocker L, Yao E, Pham T, Munroe X, et al. (2008) A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy. Cancer Res 68: 5878-5887.
    • (2008) Cancer Res , vol.68 , pp. 5878-5887
    • Lee-Hoeflich, S.T.1    Crocker, L.2    Yao, E.3    Pham, T.4    Munroe, X.5
  • 13
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling
    • Engelman JA, Zejnullahu K, Mitsudomi T, Song Y, Hyland C, et al. (2007) MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling. Science 316: 1039-1043.
    • (2007) Science , vol.316 , pp. 1039-1043
    • Engelman, J.A.1    Zejnullahu, K.2    Mitsudomi, T.3    Song, Y.4    Hyland, C.5
  • 14
    • 62149138484 scopus 로고    scopus 로고
    • Bispecific antibodies for cancer therapy
    • Chames P, Baty D, (2009) Bispecific antibodies for cancer therapy. Curr Opin Drug Discov Devel 12: 276-283.
    • (2009) Curr Opin Drug Discov Devel , vol.12 , pp. 276-283
    • Chames, P.1    Baty, D.2
  • 15
    • 11844273237 scopus 로고    scopus 로고
    • Recombinant bispecific antibodies for cancer therapy
    • Kontermann RE, (2005) Recombinant bispecific antibodies for cancer therapy. Acta Pharmacol Sin 26: 1-9.
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 1-9
    • Kontermann, R.E.1
  • 17
    • 29144434036 scopus 로고    scopus 로고
    • 2C4, a monoclonal antibody against HER2, disrupts the HER kinase signaling pathway and inhibits ovarian carcinoma cell growth
    • Takai N, Jain A, Kawamata N, Popoviciu LM, Said JW, et al. (2005) 2C4, a monoclonal antibody against HER2, disrupts the HER kinase signaling pathway and inhibits ovarian carcinoma cell growth. Cancer 104: 2701-2708.
    • (2005) Cancer , vol.104 , pp. 2701-2708
    • Takai, N.1    Jain, A.2    Kawamata, N.3    Popoviciu, L.M.4    Said, J.W.5
  • 18
    • 60749095127 scopus 로고    scopus 로고
    • Anti-epidermal growth factor receptor monoclonal antibody cetuximab inhibits EGFR/HER-2 heterodimerization and activation
    • Patel D, Bassi R, Hooper A, Prewett M, Hicklin DJ, et al. (2009) Anti-epidermal growth factor receptor monoclonal antibody cetuximab inhibits EGFR/HER-2 heterodimerization and activation. International Journal of Oncology 34: 25-32.
    • (2009) International Journal of Oncology , vol.34 , pp. 25-32
    • Patel, D.1    Bassi, R.2    Hooper, A.3    Prewett, M.4    Hicklin, D.J.5
  • 19
    • 1942441770 scopus 로고    scopus 로고
    • Blockade of epidermal growth factor- or heregulin-dependent ErbB2 activation with the anti-ErbB2 monoclonal antibody 2C4 has divergent downstream signaling and growth effects
    • Jackson JG, St Clair P, Sliwkowski MX, Brattain MG, (2004) Blockade of epidermal growth factor- or heregulin-dependent ErbB2 activation with the anti-ErbB2 monoclonal antibody 2C4 has divergent downstream signaling and growth effects. Cancer Res 64: 2601-2609.
    • (2004) Cancer Res , vol.64 , pp. 2601-2609
    • Jackson, J.G.1    St Clair, P.2    Sliwkowski, M.X.3    Brattain, M.G.4
  • 20
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, et al. (2003) Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 421: 756-760.
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5
  • 21
    • 1842605531 scopus 로고    scopus 로고
    • Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
    • Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, et al. (2004) Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell 5: 317-328.
    • (2004) Cancer Cell , vol.5 , pp. 317-328
    • Franklin, M.C.1    Carey, K.D.2    Vajdos, F.F.3    Leahy, D.J.4    de Vos, A.M.5
  • 22
    • 65349101151 scopus 로고    scopus 로고
    • Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941
    • Junttila TT, Akita RW, Parsons K, Fields C, Lewis Phillips GD, et al. (2009) Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. Cancer Cell 15: 429-440.
    • (2009) Cancer Cell , vol.15 , pp. 429-440
    • Junttila, T.T.1    Akita, R.W.2    Parsons, K.3    Fields, C.4    Lewis Phillips, G.D.5
  • 23
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J, (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125: 1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 24
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick DS, Gerber SA, Gygi SP, (2005) The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 35: 265-273.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 25
    • 57649148679 scopus 로고    scopus 로고
    • Human IgG2 antibody disulfide rearrangement in vivo
    • Liu YD, Chen X, Enk JZ, Plant M, Dillon TM, et al. (2008) Human IgG2 antibody disulfide rearrangement in vivo. J Biol Chem 283: 29266-29272.
    • (2008) J Biol Chem , vol.283 , pp. 29266-29272
    • Liu, Y.D.1    Chen, X.2    Enk, J.Z.3    Plant, M.4    Dillon, T.M.5
  • 26
    • 0019405463 scopus 로고
    • Improved fitting of radioimmunoassay data by Scatchard analysis
    • Smigel MD, Lazar JD, (1981) Improved fitting of radioimmunoassay data by Scatchard analysis. Int J Biomed Comput 12: 189-203.
    • (1981) Int J Biomed Comput , vol.12 , pp. 189-203
    • Smigel, M.D.1    Lazar, J.D.2
  • 27
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura N, Endres NF, Engel K, Deindl S, Das R, et al. (2009) Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 137: 1293-1307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1    Endres, N.F.2    Engel, K.3    Deindl, S.4    Das, R.5
  • 28
    • 76049128717 scopus 로고    scopus 로고
    • Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
    • Jura N, Shan Y, Cao X, Shaw DE, Kuriyan J, (2009) Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc Natl Acad Sci U S A 106: 21608-21613.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21608-21613
    • Jura, N.1    Shan, Y.2    Cao, X.3    Shaw, D.E.4    Kuriyan, J.5
  • 29
    • 67449146917 scopus 로고    scopus 로고
    • The juxtamembrane region of the EGF receptor functions as an activation domain
    • Red Brewer M, Choi SH, Alvarado D, Moravcevic K, Pozzi A, et al. (2009) The juxtamembrane region of the EGF receptor functions as an activation domain. Mol Cell 34: 641-651.
    • (2009) Mol Cell , vol.34 , pp. 641-651
    • Red Brewer, M.1    Choi, S.H.2    Alvarado, D.3    Moravcevic, K.4    Pozzi, A.5
  • 31
    • 0037431430 scopus 로고    scopus 로고
    • Structural analysis of the ErbB-2 receptor using monoclonal antibodies: Implications for receptor signalling
    • Yip YL, Novotny J, Edwards M, Ward RL, (2003) Structural analysis of the ErbB-2 receptor using monoclonal antibodies: Implications for receptor signalling. International Journal of Cancer 104: 303-309.
    • (2003) International Journal of Cancer , vol.104 , pp. 303-309
    • Yip, Y.L.1    Novotny, J.2    Edwards, M.3    Ward, R.L.4
  • 32
    • 79952233837 scopus 로고    scopus 로고
    • Trastuzumab Has Preferential Activity against Breast Cancers Driven by HER2 Homodimers
    • Ghosh R, Narasanna A, Wang SE, Liu S, Chakrabarty A, et al. (2011) Trastuzumab Has Preferential Activity against Breast Cancers Driven by HER2 Homodimers. Cancer Research 71: 1871-1882.
    • (2011) Cancer Research , vol.71 , pp. 1871-1882
    • Ghosh, R.1    Narasanna, A.2    Wang, S.E.3    Liu, S.4    Chakrabarty, A.5
  • 33
    • 0027196997 scopus 로고
    • Studies on antigen binding by intact and hinge-deleted chimeric antibodies
    • Horgan C, Brown K, Pincus SH, (1993) Studies on antigen binding by intact and hinge-deleted chimeric antibodies. J Immunol 150: 5400-5407.
    • (1993) J Immunol , vol.150 , pp. 5400-5407
    • Horgan, C.1    Brown, K.2    Pincus, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.