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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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Guanylate cyclase and cyclic guanosine 3':5'-monophosphate phosphodiesterase activities and cyclic guanosine 3':5'-monophosphate levels in normal and transformed fibroblasts in culture.
TL;DR: The results do not appear to support the suggestion that cyclic GMP promotes the growth of fibroblastic cells, and indicate that the absence of cyclicGMP phosphodiesterase activity in KNRK cells is not due to a loss of the phosphodiedterase activator.
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Molecular cloning and expression of a cDNA encoding a protein detected by the K1 antibody from an ovarian carcinoma (OVCAR-3) cell line.
Kai Chang,Ira Pastan +1 more
TL;DR: Data indicate that the cloned cDNA encodes a cytosolk protein that reacted with MAb Kl, suggesting that the 2 proteins could be structurally related.
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Mutagenesis of Pseudomonas exotoxin in identification of sequences responsible for the animal toxicity.
TL;DR: The data indicate that amino acids at positions 246, 247, and 249 have an important role in the toxicity of PE and when combined with a mutation at position 57 a molecule is created that has very low toxicity against cultured cells or in mice.
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Cytotoxicity and antitumor effects of growth factor-toxin fusion proteins on human glioblastoma multiforme cells.
TL;DR: The overexpression of the epidermal growth factor receptor in glioblastomas multiforme and the potency and specificity of the TGF-alpha-PE40 construct designed to target this receptor suggests that TGF/PE40 has the potential to be an effective antitumor agent for the adjuvant therapy of these carcinomas.
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A recombinant form of Pseudomonas exotoxin directed at the epidermal growth factor receptor that is cytotoxic without requiring proteolytic processing.
TL;DR: This study constructed a mutant protein (PE37), composed of amino acids 280-613 of Pseudomonas exotoxin A, which does not require proteolysis to translocate, and was targeted specifically to cells with epidermal growth factor receptors by inserting transforming growth factor-alpha (TGF-alpha) after amino acid 607 near the carboxyl terminus.