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William P. Schneider
Researcher at Stanford University
Publications - 19
Citations - 2881
William P. Schneider is an academic researcher from Stanford University. The author has contributed to research in topics: Antibody & Recombinant DNA. The author has an hindex of 13, co-authored 19 publications receiving 2835 citations. Previous affiliations of William P. Schneider include Becton Dickinson.
Papers
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Journal ArticleDOI
A humanized antibody that binds to the interleukin 2 receptor.
Cary L. Queen,William P. Schneider,Harold E. Selick,Philip W. Payne,Nicholas F. Landolfi,James F. Duncan,Nevenka M. Avdalovic,Michael Levitt,Richard P. Junghans,Thomas A. Waldmann +9 more
TL;DR: A "humanized" antibody is constructed by combining the complementarity-determining regions (CDRs) of the anti-Tac antibody with human framework and constant regions and has an affinity for p55 of 3 x 10(9) M-1, about 1/3 that of murine anti- Tac.
Patent
Polynucleotides encoding improved humanized immunoglobulins
TL;DR: In this paper, a method for producing, and compositions of, humanized immunoglobulins having one or more complementarity determining regions (CDR's) and possible additional amino acids from a donor immunoglobalin and a framework region from an accepting human immunoglobin are provided.
Journal Article
Anti-Tac-H, a humanized antibody to the interleukin 2 receptor with new features for immunotherapy in malignant and immune disorders.
Richard P. Junghans,Thomas A. Waldmann,Nicholas F. Landolfi,Nevenka M. Avdalovic,William P. Schneider,Cary L. Queen +5 more
TL;DR: In this article, humanized anti-Tac antibodies were developed to a tumor-associated antigen and activated T-cell marker with significant features that offer new therapeutic possibilities for select neoplastic and immune disorders.
Patent
Improved humanized immunoglobulins
TL;DR: In this paper, humanized immunoglobulins having one or more complementarity determining regions (CDR's) and possible additional amino acids from a donor immunoglobalin and a framework region from an accepting human immunoglobin are provided for a number of antigens.
Journal ArticleDOI
Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides.
TL;DR: The stability differences suggest that, as amino acid changes occurred in these proteins during the course of evolution, subsequent changes were limited to those that would allow retention of a desired protein conformation.