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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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Forms of deoxyribonucleic acid produced by virions of the ribonucleic acid tumor viruses.

TL;DR: The in vitro product of mouse leukemia virus deoxyribonucleic acid (DNA) polymerase can be separated into two fractions by sedimentation in sucrose gradients and the following model is postulate: the first DNA synthesis occurs in a replicative complex containing growing DNA molecules attached to an RNA molecule.
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Molecular evolution of the vertebrate immune system.

TL;DR: This work has shown that T cells use T-cell receptors to respond to antigen in the form of processed peptides bound to cell surface proteins encoded in the major histocompatibility complex (MHC).
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The promoter of the human interleukin-2 gene contains two octamer-binding sites and is partially activated by the expression of Oct-2.

TL;DR: Both the signal requirements and the magnitude of the transcription response of the IL-2 promoter can be modulated by Oct-2, which potentiated transcription 13-fold in response to TPA plus PHA and permitted the enhancer to respond to the single stimulus of TPA.
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Vectored immunoprophylaxis protects humanized mice from mucosal HIV transmission.

TL;DR: It is demonstrated that VIP is capable of protecting humanized mice from intravenous as well as vaginal challenge with diverse viral strains, despite repeated exposures, suggesting that VIP may be effective in preventing vaginal transmission of HIV between humans.
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Complete translation of poliovirus RNA in a eukaryotic cell-free system

TL;DR: The results strongly support the model of translation of poliovirus RNA from a single initiation site into a continuous polyprotein that is cleaved to form the functional proteins and it is suggested that uninfected HeLa cell extracts can carry out the cleavages of nascent polyprotein.