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David Baltimore

Researcher at California Institute of Technology

Publications -  882
Citations -  168784

David Baltimore is an academic researcher from California Institute of Technology. The author has contributed to research in topics: RNA & Virus. The author has an hindex of 203, co-authored 876 publications receiving 162955 citations. Previous affiliations of David Baltimore include Thomas Jefferson University & Johns Hopkins University.

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Proline-rich sequences that bind to Src homology 3 domains with individual specificities.

TL;DR: To study the binding specificity of Src homology 3 (SH3) domains, a mouse embryonic expression library is screened for peptide fragments that interact with them and several clones were identified that express fragments of proteins which, through proline-rich binding sites, exhibit differential binding specificity to various SH3 domains.
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Cloning of a lymphoid-specific cDNA encoding a protein binding the regulatory octamer DNA motif

TL;DR: This cDNA derives from a gene (oct-2) that specifies an octamer binding protein expressed preferentially in B lymphocytes, proving that, for at least one gene, a cell-specific transcription factor exists and its amount is controlled through messenger RNA availability.
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Differentiation requires continuous regulation.

TL;DR: Article de synthese traitant des mecanismes biochimiques et genetiques regulant le phenomene de differenciation cellulaire pour 2 especes d'insectes presentant ou non des mutations dans leur genome
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Lack of a negative influence on viral growth by the nef gene of human immunodeficiency virus type 1

TL;DR: The data suggest that the Nef protein does not act as a negative factor, at least in the experimental systems employed in the studies, and is compared to two isogenic HIV-1 strains, one of which lacks nef expression and found little difference between them in in vitro growth.
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Alternative 5′ exons in c-abl mRNA

TL;DR: Four types of mouse c-abl cDNAs have been cloned from 70Z/3 lymphoid cells that have different 5' sequences encoding predicted N-terminal regions of 20-45 amino acids, which appears to be generated by alternative addition of 5' exon onto a common set of 3' exons.