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Salvador E. Luria

Researcher at Massachusetts Institute of Technology

Publications -  57
Citations -  7459

Salvador E. Luria is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Colicin & Bacteriophage. The author has an hindex of 29, co-authored 57 publications receiving 7250 citations. Previous affiliations of Salvador E. Luria include Carnegie Institution for Science & University of Illinois at Urbana–Champaign.

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Mutations of bacteria from virus sensitivity to virus resistance

TL;DR: This article reported Luria and Delbruck's breakthrough study in which they established that viruses do not induce mutations in bacteria, but that virus-resisting mutations are spontaneous.
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Hybridization between Escherichia coli and Shigella.

TL;DR: It is established that these two types of intestinal bacteria could mate and produce hybrids possessing characteristics of each, and this had implications for laboratory diagnosis, raising the possibility that a hybrid possessing Shigella's pathogenic qualities could test as an E. coli, or vice-versa.
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Transduction of lactose-utilizing ability among strains of E. coli and S. dysenteriae and the properties of the transducing phage particles.

TL;DR: Transduction of the lac + property by phage P1 among strains of Escherichia coli K12 and Shigella dysenteriae Sh has been studied and a variety of P1 dl elements is postulated to account for the properties of different Sh lac v transductant strains.
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A nonhereditary, host-induced variation of bacterial viruses.

TL;DR: In this article, Luria reported that some bacteria, when infected with phage, would modify the phage in such a way so that it cannot reproduce in that particular bacteria type, but the variation gives thephage the ability to infect a different bacterial species, in this instance Shigella.
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Genetics and Physiology of Colicin-tolerant Mutants of Escherichia coli

TL;DR: Colicin-tolerant mutations are interpreted as affecting some components of the cytoplasmic membrane which mediate between the adsorbed colicin molecules and the target sites of their biochemical effects in the bacterial cell.