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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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Journal ArticleDOI

Localization of tyrosine kinase-coding region in v-abl oncogene by the expression of v-abl-encoded proteins in bacteria.

TL;DR: These experiments show that the 5'-1.2 kilobases of v-abl is necessary and sufficient to produce an active tyrosine kinase which is functional as a monomeric soluble protein.
Journal Article

The p65 subunit of NF-kappa B is redundant with p50 during B cell proliferative responses, and is required for germline CH transcription and class switching to IgG3.

TL;DR: A role for the p65 subunit of NF-kappa B in germline CH gene expression as well as functional redundancy between p50 and p65 during proliferative responses are demonstrated.
Book ChapterDOI

[13] Purification of the RNA-directed DNA polymerase from avian myeloblastosis virus and its assay with polynucleotide templates

TL;DR: This chapter describes two activities that have been extensively purified: DNA polymerase that can utilize both ribo- and deoxyribonucleotide templates and ribonuclease H that selectively degrades RNA from an RNA-DNA hybrid.
Journal ArticleDOI

Lessons from people with nonprogressive HIV infection.

TL;DR: Infectious diseases can be extremely variable in their manifestations, but human immunodeficiency virus (HIV) infection is notorious for its protean manifestations, and the absence of any apparent progression of disease over a decade or more is particularly intriguing.
Journal ArticleDOI

Terminal deoxynucleotidyltransferase. Serological studies and radioimmunoassay.

TL;DR: Mouse antisera against calf terminal deoxynucleotidyltransferase (terminal transferase) indicate that terminal transferase is a tissue-specific enzyme and is not related to other DNA polymerases.