J
Jacob Barg
Researcher at Weizmann Institute of Science
Publications - 63
Citations - 5886
Jacob Barg is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Receptor & Enkephalin. The author has an hindex of 31, co-authored 63 publications receiving 5656 citations. Previous affiliations of Jacob Barg include Wolfson Medical Center.
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Journal ArticleDOI
Identification of an endogenous 2-monoglyceride, present in canine gut, that binds to cannabinoid receptors.
Raphael Mechoulam,Shimon Ben-Shabat,Lumir Hanus,Moshe Ligumsky,Norbert E. Kaminski,Anthony R. Schatz,Asher Gopher,Shlomo Almog,Billy R. Martin,David R. Compton,Roger G. Pertwee,Graeme Griffin,Michael Bayewitch,Jacob Barg,Zvi Vogel +14 more
TL;DR: Upon intravenous administration to mice, 2-Ara-Gl caused the typical tetrad of effects produced by THC: antinociception, immobility, reduction of spontaneous activity, and lowering of the rectal temperature.
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Anandamide, a brain endogenous compound, interacts specifically with cannabinoid receptors and inhibits adenylate cyclase.
TL;DR: Data indicate that anandamide is an endogenous agonist that may serve as a genuine neurotransmitter for the cannabinoid receptor and was blocked by treatment with pertussis toxin.
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The peripheral cannabinoid receptor: adenylate cyclase inhibition and G protein coupling
TL;DR: It is shown, using a CB2 transfected Chinese hamster ovary cell line, that this receptor binds a variety of tricyclic cannabinoid ligands as well as the endogenous ligand anandamide, which characterize the CB2 receptor as a functional and distinctive member of the cannabinoid receptor family.
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Subcellular localization of tau mRNA in differentiating neuronal cell culture: Implications for neuronal polarity
TL;DR: It is demonstrated that unlike tubulin mRNA, which is confined to cell bodies, or MAP2 mRNA,Which extends into dendrites, tau mRNA was observed to enter the proximal portion of the axon, and could have important implications for the development of neuronal polarity.
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The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction
Janna Blechman,Sima Lev,Jacob Barg,Jacob Barg,Miriam Eisenstein,Baruch Vaks,Zvi Vogel,David Givol,Yosef Yarden +8 more
TL;DR: Using a dimerization-inhibitory monoclonal antibody to the SCF receptor, deletion of the fourth immunoglobulin-like domain of the receptor is identified and insights are provided into the mechanism of the coupling of ligand binding to dimer formation.