Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Marc D. Better"'
Autor:
Marc D. Better, Patrick D. Gavit
Publikováno v:
Antibody Therapeutics ISBN: 9780429260360
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e9f956dd95103843efe28f80de03798
https://doi.org/10.1201/9780429260360-13
https://doi.org/10.1201/9780429260360-13
Autor:
Patrick D. Gavit, Marc D. Better
Publikováno v:
Journal of Biotechnology. 79:127-136
Antifungal peptides derived from the human bactericidal/permeability-increasing protein (BPI) were produced in Escherichia coli as fusion proteins with human BoneD. Bacterial cultures transformed with the gene encoding the fusion protein were grown t
Autor:
Scott D. Leigh, Robert J. Bauer, Ada H. C. Kung, Dianne M. Fishwild, Susan L. Bernhard, Stephen F. Carroll, Marc D. Better, Robert E. Williams
Publikováno v:
Journal of Biological Chemistry. 270:14951-14957
Fusion proteins between cell-targeting domains and cytotoxic proteins should be particularly effective therapeutic reagents. We constructed a family of immunofusion proteins linking humanized Fab, F(ab')2, or single chain antibody forms of the H65 an
Publikováno v:
Molecular Immunology. 31:683-692
Immunoglobulin light chain proteins are generally thought to be readily secreted without their corresponding heavy chains; non-secreted light chains have been viewed as aberrant forms. We have re-examined this assumption by expressing chimeric mouse-
Autor:
Sandra Soares, Arnold H. Horwitz, Gary M. Studnicka, Marc D. Better, Robert E. Williams, Rossana Nadell
Publikováno v:
"Protein Engineering, Design and Selection". 7:805-814
Humanization of murine monoclonal antibodies for human therapy has commonly been achieved by complementarity-determining region (CDR) grafting, in which murine CDR loops are grafted onto human framework regions. Difficulties with that method have rev
Publikováno v:
Journal of Biological Chemistry. 267:16712-16718
A synthetic gene for the Aspergillus protein toxin mitogillin has been synthesized and expressed in Escherichia coli. The recombinant mitogillin is a potent inhibitor of protein synthesis in vitro with an IC50 of 9.7 pM. Immunoconjugates of recombina
Autor:
Arnold H. Horwitz, Marc D. Better
Publikováno v:
Protein Folding ISBN: 9780841226401
Protein Folding: In Vivo and In Vitro
Protein Folding: In Vivo and In Vitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b607bc015531aa547e8333e820410e7
https://doi.org/10.1021/bk-1993-0526.ch016
https://doi.org/10.1021/bk-1993-0526.ch016