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1 study, we replaced the first luminal loop of cellugyrin, a 4-transmembrane protein that does not resp
2 these regions were sufficient to relocalize cellugyrin, a nonneuronal form of synaptogyrin, from non
3 vesicles and have identified this protein as cellugyrin, a ubiquitously expressed homologue of a majo
4 studies in COS cells demonstrated that both cellugyrin and synaptogyrin are tyrosine phosphorylated
8 The conserved tyrosine phosphorylation of cellugyrin and synaptogyrins suggests a link between tyr
9 ynaptogyrin 1 is a synaptic vesicle protein; cellugyrin, by contrast, is absent from synaptic vesicle
10 enomena and found that ectopic expression of cellugyrin increases the number of SLMVs in PC12 cells.
11 microscopy, we have shown that virtually all cellugyrin is co-localized with Glut4 in the same vesicl
18 RAP), or transferrin receptor (TfR), whereas cellugyrin-negative vesicles contain five to six molecul
22 y epithelial cell line COS7 and found that a cellugyrin-positive microvesicular compartment was prese
23 est that synaptic vesicles have evolved from cellugyrin-positive ubiquitous microvesicles and that ne
25 125)I-labeled transferrin are accumulated in cellugyrin-positive vesicles and to a lesser extent in c
26 l surface after insulin stimulation, whereas cellugyrin-positive vesicles maintain intracellular loca
30 that synaptogyrin or its nonneuronal paralog cellugyrin targets efficiently to synaptic-like microves
31 ified a novel isoform of synaptogyrin called cellugyrin that exhibits 47% sequence identity with syna
32 st luminal loop and the carboxyl terminus of cellugyrin were found to be critical for the formation o
34 specialized version of a ubiquitous protein, cellugyrin, with the two proteins sharing structural sim
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