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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.

Papers
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Journal ArticleDOI

Filamin inhibits actin activation of heavy meromyosin ATPase.

Peter J.A. Davies, +2 more
- 15 May 1977 - 
TL;DR: The effects of filamin on F-actin activation of HMM ATPase and myosin ATPase are studied and it is found that filamin markedly reduced actinactivation of these activities.
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Rapid humanization of the Fv of monoclonal antibody B3 by using framework exchange of the recombinant immunotoxin B3(Fv)-PE38.

Itai Benhar, +4 more
- 06 Dec 1994 - 
TL;DR: Humanized B3(Fv)-PE38 lost immunogenic epitopes recognized by sera from monkeys that had been immunized with B3 (Fv-PE38), and this basic design resulted in some 20-fold loss of activity.
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The direction and role of phenotypic transition between podocytes and parietal epithelial cells in focal segmental glomerulosclerosis.

Kazuo Sakamoto, +7 more
- 01 Jan 2014 - 
TL;DR: The results suggest that the major direction of epithelial phenotypic transition in cellular FSGS is from podocytes to PECs and that these cells were less represented in the active lesions of FSGS.
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Stimulation in vitro of glucose oxidation in thyroid by acetylcholine.

Ira Pastan, +3 more
- 01 Feb 1961 - 
TL;DR: It was found that the increase with acetylcholine seemed to be independent of changes in blood flow and suggested a direct effect on thyroid epithelial cells, and it seemed of interest to investigate the effects of acetyl choline on the glucose oxidation of the thyroid.
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Cloning, expression and characterization of the Fv fragments of the anti-carbohydrate mAbs B1 and B5 as single-chain immunotoxins.

Itai Benhar, +1 more
- 01 Dec 1994 - 
TL;DR: The mAbs B1 and B5 variable domains replaced their corresponding B3 domains in the expression plasmid by 'variable domain shuffling' without subcloning, reflecting its higher affinity to the target cells.