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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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Domain-dependent function of the rasGAP-binding protein p62Dok in cell signaling.

TL;DR: It is demonstrated here that the expression of Dok can inhibit cellular transformation by the Src tyrosine kinase, and it is suggested that Dok oligomerization through its multiple domains plays a critical role in Dok signaling in response to tyrosin kinase activation.
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Regulation of stress-induced hematopoiesis

TL;DR: These exciting new findings will shape the fundamental understanding of how inflammatory signaling regulates hematopoiesis in health and disease, and facilitate the development of potential interventions to treat hematologic diseases associated with altered inflammatory signaling.
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3BP-1, an SH3 domain binding protein, has GAP activity for Rac and inhibits growth factor-induced membrane ruffling in fibroblasts.

TL;DR: 3BP‐1 is a new and specific Rac GAP that can act in cells to counter Rac‐mediated membrane ruffling and how its SH3 binding site interacts with its GAP activity remains to be understood.
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Mechanism of formation of pseudotypes between vesicular stomatitis virus and murine leukemia virus.

TL;DR: Results suggest that small numbers of VSV G protein are obligately incorporated into VSV(MuLV) pseudotypes, and there appears to be a stringent requirement for recognition of the viral core by homologous envelope components as the nucleating step in the budding process.
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Polyadenylic acid on poliovirus RNA. II. poly(A) on intracellular RNAs.

TL;DR: Investigation of the kinetics of poly(A) appearance in the replicative intermediate and in finished 35S molecules indicated that poly (A) is the last portion of the 35S RNA to be synthesized, which indicates that poliovirus RNA is synthesized 5' leads to 3' like other RNA's.