16 Papers
298 Citations
Ling Wang is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Thrombin receptor & Receptor. The author has an hindex of 8, co-authored 10 publications. Previous affiliations of Ling Wang include University of California & Cardiovascular Institute Hospital.
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Papers
Specificity of the thrombin receptor for agonist peptide is defined by its extracellular surface
Robert E. Gerszten,Ji Chen,M. Ishii,K. Ishii,Ling Wang,Ling Wang,T. Nanevicz,C. W. Turck,T.-K. H. Vu,Shaun R. Coughlin,Shaun R. Coughlin +10 more
TL;DR: The results indicate that agonist interaction with extracellular domains is important for thrombin receptor activation and identifies receptor domains that confer this agonist specificity by replacing the Xenopus receptor's amino-terminal exodomain and threeextracellular loops with the corresponding human structures.
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Thrombin Receptor Activation CONFIRMATION OF THE INTRAMOLECULAR TETHERED LIGANDING HYPOTHESIS AND DISCOVERY OF AN ALTERNATIVE INTERMOLECULAR LIGANDING MODE* (Received for publication, February 18, 1994, and in revised form, March 29, 1994)
Ji Chen,Maki Ishii,Ling Wang,Kenji Ishii,Shaun R. CoughlinS +4 more
- 01 Jan 1994
TL;DR: In this paper, it was shown that the SFLLRN sequence is a tethered peptide ligand; receptor cleavage unmasks this agonist which then binds intramolecularly to effect receptor activation.
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Mechanisms of Thrombin Receptor Agonist Specificity CHIMERIC RECEPTORS AND COMPLEMENTARY MUTATIONS IDENTIFY AN AGONIST RECOGNITION SITE
Tania Nanevicz,Maki Ishii,Ling Wang,Mian Chen,Ji Chen,Christoph W. Turck,Fred E. Cohen,Shaun R. Coughlin +7 more
TL;DR: Two independent approaches, chimeric receptors and arginine scanning for complementary mutations, identified the Glu region and to a lesser degree Phe as important determinants of agonist specificity.
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Thrombin Receptor Activating Mutations ALTERATION OF AN EXTRACELLULAR AGONIST RECOGNITION DOMAIN CAUSES CONSTITUTIVE SIGNALING
TL;DR: The site of the activating mutation in XECL2B coincides with a putative agonist-docking site, supporting the hypothesis that agonist interactions with the thrombin receptor's extracellular loops contribute to receptor activation.
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The thrombin receptor second cytoplasmic loop confers coupling to Gq-like G proteins in chimeric receptors. Additional evidence for a common transmembrane signaling and G protein coupling mechanism in G protein-coupled receptors.
TL;DR: In this paper, the authors examined the signaling properties of chimeric receptors in which thrombin receptor cytoplasmic sequences replaced the cognate sequences in the Gi-coupled dopamine D2 receptor (D2R) or the β2-adrenergic receptor (β2AR).
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