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Irving M. London

Researcher at NewYork–Presbyterian Hospital

Publications -  53
Citations -  2956

Irving M. London is an academic researcher from NewYork–Presbyterian Hospital. The author has contributed to research in topics: Protein biosynthesis & Reticulocyte. The author has an hindex of 34, co-authored 53 publications receiving 2927 citations. Previous affiliations of Irving M. London include Columbia University.

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On the origin of bile pigment in normal man.

TL;DR: The studies described in this report offer evidence pertinent to the problem of the biologic origin of bile pigment that glycine is specifically utilized in the biosynthesis of protoporphyrin and that the administration of N16-labeled glycine provides a method for the determination of the average life span and pattern of destruction of the human erythrocyte in normal and pathologic states.
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Regulation of protein synthesis in reticulocyte lysates: phosphorylation of methionyl-tRNAf binding factor by protein kinase activity of translational inhibitor isolated from hemedeficient lysates.

TL;DR: The observation that the Met-tRNAf binding factor is phosphorylated by PC2 supports the hypothesis that this initiation factor is a target for the action of the translational inhibitor activated in heme deficiency.
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Regulation of protein synthesis: Activation by double-stranded RNA of a protein kinase that phosphorylates eukaryotic initiation factor 2

TL;DR: It is shown that incubation of reticulocyte lysates or isolated crude ribosomes with low levels of double-stranded RNA induces the formation of an inhibitor of protein synthesis initiation similar to that observed in heme deficiency.
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Patterns of RNA metabolism in a differentiated cell: a rapidly labeled, unstable 60S RNA with messenger properties in duck erythroblasts

TL;DR: Investigating RNA synthesis in the highly diff erentiated, nonproliferating cells of the avian erythropoietic line in which the level of ribosome synthesis is considerably reduced is of particular interest because it affords the possibility of studying the relationship of RNA synthesis to the differentiation of the erythroid cell and the phenotypic expression of a very small part of the genome.
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Heme synthesis and red blood cell dynamics in normal humans and in subjects with polycythemia vera, sickle-cell anemia, and pernicious anemia.

TL;DR: By following the isotope concentration in hemin isolated from the red blood cells the length of time that labeled hemoglobin remains in the blood, and thus the survival time of thered blood cells containing the labeled heme, can be determined.