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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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TGFα-anti-Tac(Fv)-PE40: A bifunctional toxin cytotoxic for cells with EGF or IL2 receptors

TL;DR: This report describes the construction of a chimeric molecule TGFα-antiTac(Fv)-PE40 which is composed of human transforming growth factor type α attached to anti-Tac (Fv) which is in turn attached to PE40, a form of pseudomonas exotoxin, devoid of its cell recognition domain.
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The heparin-binding domain of heparin-binding EGF-like growth factor can target Pseudomonas exotoxin to kill cells exclusively through heparan sulfate proteoglycans

TL;DR: It is concluded that the HB domain of HB-EGF is able to mediate internalization through HSPGs, without requiring the EGF receptor.
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The multidrug-resistance gene in gene therapy of cancer and hematopoietic disorders.

TL;DR: Approaches which use the multidrug-resistance gene as a selectable markerin vivo to increase the expression of nonselectable genes which correct hereditary diseases of the hematopoietic system are reviewed.
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Whole-genome RNAi screen highlights components of the endoplasmic reticulum/Golgi as a source of resistance to immunotoxin-mediated cytotoxicity

TL;DR: Genes related to the ER-associated degradation system were not among high-ranking mitigator or sensitizer candidates and the p97 inhibitor eeyarestatin 1 enhanced immunotoxin killing, indicating that these gene products normally contribute to inefficiencies in the killing pathway.
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Designing the furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A.

TL;DR: It is found that changes to the furin site could greatly influence both cleavage and cytotoxicity, but the two parameters were not directly correlated and informs the design of protease-sensitive linkers and suggests that HA22-LR/FUR may be a candidate for further preclinical development.