M
Mike Clark
Researcher at University of Cambridge
Publications - 95
Citations - 9995
Mike Clark is an academic researcher from University of Cambridge. The author has contributed to research in topics: Antibody & Monoclonal antibody. The author has an hindex of 38, co-authored 95 publications receiving 9849 citations. Previous affiliations of Mike Clark include Laboratory of Molecular Biology.
Papers
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Journal ArticleDOI
Reshaping human antibodies for therapy.
TL;DR: A human IgGI antibody has been reshaped for serotherapy in humans by introducing the six hypervariable regions from the heavy- and light-chain variable domains of a rat antibody directed against human lymphocytes.
Journal ArticleDOI
Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies.
Marianne Brüggemann,Gareth T. Williams,C Bindon,Mike Clark,M R Walker,R Jefferis,Herman Waldmann,Michael S. Neuberger +7 more
TL;DR: The results suggest that IgG1 might be the favoured IgG subclass for therapeutic applications in complement-dependent hemolysis and in antibody-dependent cell-mediated cytotoxicity using both human effector and human target cells.
Journal ArticleDOI
Remission induction in non-hodgkin lymphoma with reshaped human monoclonal antibody campath-1h
G. Hale,Mike Clark,Robert Marcus,Greg Winter,Martin J. S. Dyer,Jenny M. Phillips,Lutz Riechmann,Herman Waldmann +7 more
TL;DR: A genetically reshaped human IgG1 monoclonal antibody (CAMPATH-1H) was used to treat two patients with non-Hodgkin lymphoma and might have an important use in the treatment of lymphoproliferative disorders and additionally as an immunosuppressive agent.
Journal ArticleDOI
Recombinant human IgG molecules lacking Fcγ receptor I binding and monocyte triggering activities
TL;DR: The aim is to engineer non‐destructive human IgG constant regions for therapeutic applications where depletion of cells bearing the target antigen is undesirable and a lack of killing via Fcγ receptors (R) and complement but retention of neonatal FcR binding to maintain placental transport and the prolonged half‐life of IgG.
Patent
Binding molecules derived from immunoglobulins which do not trigger complement mediated lysis
TL;DR: In this paper, the authors defined a class of binding molecules which are recombinant polypeptides comprising: (i) a binding domain capable of binding a target molecule, and (ii) an effector domain having an amino acid sequence substantially homologous to all or part of a constant domain of a human immunoglobulin heavy chain.