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      KCI등재 SCIE SCOPUS

      Engineering Antibodies for Dual Specificity and Enhanced Potency

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      https://www.riss.kr/link?id=A103681714

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      다국어 초록 (Multilingual Abstract)

      Despite the tremendous success of monoclonal antibodies for human therapeutics, there remain several diseases that escape monospecific IgG antibody-mediated immunotherapy. However, the recent in-depth understanding of antibody structure and function, ...

      Despite the tremendous success of monoclonal antibodies for human therapeutics, there remain several diseases that escape monospecific IgG antibody-mediated immunotherapy. However, the recent in-depth understanding of antibody structure and function, and significant advances in antibody engineering techniques, have facilitated the development of unnatural bispecific antibodies, which are capable of recruiting more powerful effector cells, retargeting target cells, and blocking two different disease mechanisms simultaneously. Conventionally, bispecific antibodies were generated by the fusion of two different hybridoma cells or chemical coupling of two monospecific antibodies. Recently, however, versatile genetic approaches have been devised to produce more homogenous and correctly assembled bispecific antibodies. To ensure improved efficacy, safety, and efficient manufacturing, a variety of strategies to create bispecific antibody fragments and native IgG-like bispecific antibody formats have been developed and are discussed in this review.

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      참고문헌 (Reference)

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      1 Holliger, P, "“Diabodies”: small bivalent and bispecific antibody fragments" 90 : 6444-6448, 1993

      2 Ridgway, J. B. B, "‘Knobs-intoholes’engineering of antibody CH3 domains for heavy chain heterodimerization" 9 : 617-621, 1996

      3 Bostrom, J, "Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site" 323 : 1610-1614, 2009

      4 Bargou, R, "Tumor regression in cancer patients by very low doses of a T cell–engaging antibody" 321 : 974-977, 2008

      5 Weis, S. M, "Tumor angiogenesis:molecular pathways and therapeutic targets" 17 : 1359-1370, 2011

      6 Hartmann, F, "Treatment of refractory Hodgkin’s disease with an anti-CD16/CD30 bispecific antibody" 89 : 2042-2047, 1997

      7 Dimitrov, D. S, "Therapeutic proteins: Methods in Molecular Biology" Humana Press 1-26, 2012

      8 Jäger, M, "The trifunctional antibody ertumaxomab destroys tumor cells that express low levels of human epidermal growth factor receptor 2" 69 : 4270-4276, 2009

      9 Correia, I, "The structure of dual-variable-domain immunoglobulin molecules alone and bound to antigen" 5 : 364-372, 2013

      10 Zeidler, R, "The Fc-region of a new class of intact bispecific antibody mediates activation of accessory cells and NK cells and induces direct phagocytosis of tumour cells" 83 : 261-266, 2000

      11 정상택, "Tailoring Immunoglobulin Fc for Highly Potent and Serum-stable Therapeutic Antibodies" 한국생물공학회 18 (18): 625-636, 2013

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      28 Arndt, K. M, "Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment" 37 : 12918-12926, 1998

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      42 Chames, P, "Bispecific antibodies for cancer therapy: the light at the end of the tunnel?" 1 : 539-547, 2009

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      52 Fury, M, "A phase-I trial of the epidermal growth factor receptor directed bispecific antibody MDX-447 without and with recombinant human granulocyte-colony stimulating factor in patients with advanced solid tumors" 57 : 155-163, 2008

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      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
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      2001-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      2016 1.14 0.13 0.75
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
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