Daisuke Yasuda
Akita University
10 Papers
29 Citations
Daisuke Yasuda is an academic researcher from Akita University. The author has contributed to research in topics: Receptor & Endoplasmic reticulum. The author has an hindex of 9, co-authored 10 publications. Previous affiliations of Daisuke Yasuda include University of Tokyo.
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Papers
Helix 8 of leukotriene B4 type-2 receptor is required for the folding to pass the quality control in the endoplasmic reticulum.
Daisuke Yasuda,Toshiaki Okuno,Takehiko Yokomizo,Tetsuya Hori,Nobuaki Hirota,Tomomi Hashidate,Masashi Miyano,Takao Shimizu,Motonao Nakamura +8 more
TL;DR: Results suggest that the H8 region of hBLT2 plays an important role in transport‐competent receptor folding, which is required for the folding to pass the quality control in the endoplasmic reticulum.
30
Amino acid residues critical for endoplasmic reticulum export and trafficking of platelet-activating factor receptor.
Nobuaki Hirota,Daisuke Yasuda,Tomomi Hashidate,Teruyasu Yamamoto,Satoshi Yamaguchi,Teruyuki Nagamune,Takahide Nagase,Takao Shimizu,Motonao Nakamura +8 more
TL;DR: It is demonstrated that a conserved proline, Pro247, in TM6 of platelet-activating factor receptor (PAFR) is required for endoplasmic reticulum (ER) export and trafficking after agonist-induced internalization.
26
The atypical N-glycosylation motif, Asn-Cys-Cys, in human GPR109A is required for normal cell surface expression and intracellular signaling
TL;DR: The results suggest that the atypical N‐glycosylation motif, Asn17‐Cys18‐CYS19, in human GPR109A is required for normal cell surface expression and intracellular signaling and the disulfide bond formations of these residues with other Cys existed in the extracellular loops for the proper folding.
14
Amino acid residues of G-protein-coupled receptors critical for endoplasmic reticulum export and trafficking.
Motonao Nakamura,Daisuke Yasuda,Nobuaki Hirota,Teruyasu Yamamoto,Satoshi Yamaguchi,Takao Shimizu,Teruyuki Nagamune +6 more
TL;DR: The novel technique of site-specific N-terminal labeling of cell surface proteins in living cells with Sortase-A, a transpeptidase isolated from Staphylococcus aureus, is introduced to evaluate the trafficking of receptors after agonist stimulation.
3
Specific ligands as pharmacological chaperones: The transport of misfolded G-protein coupled receptors to the cell surface
TL;DR: This review summarizes the current knowledge about the requirement of these consensus domains and amino acid residues for the passing through the quality control of the ER and proposes the utilization of membrane permeable ligands for the transport of their cognate, ER‐retained GPCRs to the cell surface.