Zobrazeno 1 - 10
of 31
pro vyhledávání: '"D L, Newton"'
Autor:
D L, Newton, S M, Rybak
Publikováno v:
Methods in molecular medicine. 25
Selective cytotoxicity is an important goal of specific drug targeting. Toward this end, toxins isolated primarily from higher plants and bacteria have been coupled to monoclonal antibodies (MAbs) and evaluated for their clinical efficacy in cancer,
Autor:
D L, Newton, S M, Rybak
Publikováno v:
Methods in molecular medicine. 25
Immunotoxins based on human and humanized ribonuclease may have potential for cancer therapy while exhibiting less toxic side effects and stimulating less of an immune response in humans than immunotoxins based on plant and bacterial toxins (1). Both
Autor:
D L, Newton, S M, Rybak
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 160
Publikováno v:
Cancer research. 60(7)
Cytotoxic endoribonucleases (RNases) possess a potential for use in cancer therapy. However, the molecular determinants of RNase-induced cell death are not well understood. In this work, we identify such determinants of the cytotoxicity induced by on
Publikováno v:
Occupational medicine (Philadelphia, Pa.). 12(1)
This information is intended to guide scientists and technicians working with pharmaceutical substances early in development, before occupational exposure levels (OELs) can be set. The focus is on determining hazard categories, or occupational exposu
Publikováno v:
The Journal of biological chemistry. 269(43)
The gene for the human recombinant eosinophil-derived neurotoxin (rEDN) was synthesized and fused to the gene encoding a single chain antibody (sFv) to the human transferrin receptor (EDNsFv). Both rEDN and EDNsFv were expressed as insoluble proteins
Publikováno v:
Therapeutic immunology. 1(1)
Publikováno v:
The Journal of biological chemistry. 267(27)
Monoclonal antibodies to the transferrin receptor or to the T cell antigen, CD5, were chemically linked to mammalian RNase A and found to specifically inhibit protein synthesis in antigen-positive cells. Antibody-mediated specificity of these cytotox
Autor:
D L, Newton, R, Wales, P T, Richardson, S, Walbridge, S K, Saxena, E J, Ackerman, L M, Roberts, J M, Lord, R J, Youle
Publikováno v:
The Journal of biological chemistry. 267(17)
The role of the two galactose binding sites of ricin B chain in ricin toxicity was evaluated by studying a series of ricin point mutants. Wild-type (WT) ricin and three ricin B chain point mutants having mutations in either 1) the first galactose bin
Publikováno v:
Soil Horizons. 36:49