D
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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Blocked early-stage latency in the peripheral blood cells of certain individuals infected with human immunodeficiency virus type 1.
TL;DR: It is suggested that asymptomatic clinical HIV-1 infection is characterized by a preponderance of HIV- 1-infected peripheral blood cells blocked at an early stage ofAIDS, and this viral expression pattern, which is called blocked early-stage latency, may constitute a reservoir of latently infected cells in certain HIV-2 infected persons.
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Synthesis of Long, Representative DNA Copies of the Murine RNA Tumor Virus Genome
TL;DR: The ability to make long, representative DNA transcripts of tumor virus RNA provides a source of excellent probes for molecular hybridization.
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Depletion of the predominant B-cell population in immunoglobulin µ heavy-chain transgenic mice
Leonore A. Herzenberg,Alan M. Stall,Jonathan Braun,David Weaver,David Baltimore,Leonard A. Herzenberg,Rudolf Grosschedl +6 more
TL;DR: The presence of the rearranged immunoglobulin heavy-chain transgene in M54 mice results in an unexpected selective developmental defect that impairs the development of bone-marrow-derived pre-B and B cells without affecting Ly-1 B cells.
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Antibodies against the chemically synthesized genome-linked protein of poliovirus react with native virus-specific proteins.
TL;DR: The genome-linked protein (VPg) of poliovirus has been chemically synthesized, coupled to bovine serum albumin carrier and injected into rabbits and an antibody response was elicited not only by the full-length synthetic VPg peptide, but also by a synthetic 14-amino acid carboxy-terminal peptide.
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Localization, interaction, and RNA binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2
Eugenia Spanopoulou,Patricia Cortes,Charles Shih,Chun-Ming Huang,Daniel P. Silver,Pamela Svec,David Baltimore +6 more
TL;DR: RAG1 appears to have a binary structure, each half containing multiple regions that can act as NLSs, binding sites for the SRP1/Rch1 family, and RNA binding domains, indicating that RAG1 has affinity for RNA or ssDNA.