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Ira Pastan

Researcher at Laboratory of Molecular Biology

Publications -  1304
Citations -  113191

Ira Pastan is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Immunotoxin & Pseudomonas exotoxin. The author has an hindex of 160, co-authored 1286 publications receiving 110069 citations. Previous affiliations of Ira Pastan include Heidelberg University & National Institutes of Health.

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Pulsed high-intensity focused ultrasound enhances uptake of radiolabeled monoclonal antibody to human epidermoid tumor in nude mice.

TL;DR: It is demonstrated that pulsed-HIFU significantly enhances the delivery of 111In-MX-B3 in human epidermoid tumors xenografted in nude mice and warrant further evaluation of other treatment regimens for greater delivery enhancement.
Journal Article

Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: disulfide-stabilized Fv immunotoxins.

TL;DR: A new type of recombinant Fv immunotoxin is developed in which the targeting variable domains of the Fv are stabilized by an interchain disulfide bond located in structurally conserved framework positions of the VH and VL domains, termeddisulfide-stabilized Fvs (dsFv) or dsFV immunotoxins.
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Characterization of immunotoxins active against ovarian cancer cell lines.

TL;DR: To investigate the basis of antibody-dependent differences in activity of the various immunotoxins, antibody uptake was studied in OVCAR-2 cells, and the results indicate that antibody internalization is one important factor in the activity of immunotoxin.
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Identification and elimination of an immunodominant T-cell epitope in recombinant immunotoxins based on Pseudomonas exotoxin A.

TL;DR: The observation of T-cell responses in 50 of 50 individuals correlates with the frequency of antibody formation in patients with normal immune systems, and a single, highly immunodominant epitope is found in 46% (23/50) of the donors.
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Repression of β-Galactosidase Synthesis by Glucose in Phosphotransferase Mutants of Escherichia coli: REPRESSION IN THE ABSENCE OF GLUCOSE PHOSPHORYLATION

TL;DR: Glucose and α-methyl glucoside repress β-galactosidase synthesis in wild type Escherichia coli and in mutant strains deficient in Enzyme I or in the heat-stable protein of the phosphoenolpyruvate-phosphotransferase system, apparently not required for lactose utilization by E. coli.