J
Jacob S. Appelbaum
Researcher at Yale University
Publications - 12
Citations - 1187
Jacob S. Appelbaum is an academic researcher from Yale University. The author has contributed to research in topics: Cell therapy & Chronic lymphocytic leukemia. The author has an hindex of 10, co-authored 12 publications receiving 1091 citations. Previous affiliations of Jacob S. Appelbaum include Fred Hutchinson Cancer Research Center & University of Washington.
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Journal ArticleDOI
Suppression of IL7Ralpha transcription by IL-7 and other prosurvival cytokines: a novel mechanism for maximizing IL-7-dependent T cell survival.
Jung-Hyun Park,Qing Yu,Batu Erman,Jacob S. Appelbaum,Diego E. Montoya-Durango,H. Leighton Grimes,Alfred Singer +6 more
TL;DR: A novel regulatory mechanism that specifically suppresses IL7Ralpha transcription in response to IL-7 and other prosurvival cytokines is described, suggesting that this homeostatic regulatory mechanism promotes survival of the maximum possible number of T cells for the amount ofIL-7 available.
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Selective recognition of protein tetraserine motifs with a cell-permeable, pro-fluorescent bis-boronic acid.
TL;DR: RhoBo functions as a cell-permeable, turn-on fluorescent sensor for tetraserine motifs in recombinant proteins and current efforts to identify optimal serine-rich sequences for RhoBo suggest it to function effectively as a selective small-molecule label for appropriately tagged proteins either upon or within living cells.
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Arginine Topology Controls Escape of Minimally Cationic Proteins from Early Endosomes to the Cytoplasm
Jacob S. Appelbaum,Jonathan R. LaRochelle,Betsy A. Smith,Daniel M. Balkin,Justin M. Holub,Alanna Schepartz +5 more
TL;DR: These results suggest that the ability of 5.3 and ZF5.3 to escape from early endosomes is a unique feature and imply the existence of distinct signals, encodable within short sequences, that favor early versus late endosomal release.
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Bridged β3-Peptide Inhibitors of p53-hDM2 Complexation: Correlation between Affinity and Cell Permeability
TL;DR: The results highlight the relative merits of the cationic-patch and hydrophobic-bridge strategies for improving beta-peptide uptake and identify a surprising correlation between uptake efficiency and hDM2 affinity.
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Bipartite tetracysteine display reveals allosteric control of ligand-specific EGFR activation.
TL;DR: It is discovered that EGF binding is communicated to the cytosol through formation of an antiparallel coiled coil within the intracellular juxtamembrane (JM) domain, which suggests that the JM region can differentially decode extracellular signals and transmit them to the cell interior.