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1 ASGPR is composed of two highly homologous subunits, ter
3 space around the well-known GalNAc-ligand as ASGPR-binder, a high-throughput screening campaign was p
4 dified siRNA has enabled asialoglycoprotein (ASGPR)-mediated targeted delivery of therapeutically act
5 rf1) of HuH-7 alters the asialoglycoprotein (ASGPR) and transferrin receptor subcellular distribution
8 uman primates with antigens fused to anti-DC-ASGPR monoclonal antibody generates antigen-specific CD4
9 hich provides a molecular explanation for DC-ASGPR-mediated programing of DCs to control host immune
10 gation of DC-asialoglycoprotein receptor (DC-ASGPR), a C-type lectin receptor (CLR) expressed on huma
14 that targeting antigens to human DCs via DC-ASGPR, but not lectin-like oxidized-LDL receptor, Dectin
16 on experiments suggest that other endogenous ASGPR ligands, the nature of which remain to be determin
18 designed ligands had similar affinities for ASGPR and similar silencing activity in mice as the pare
19 new ligands were obtained with affinity for ASGPR as good as or better than that of the parent N-ace
21 njugated ASOs showed high affinity for mouse ASGPR, which results in enhanced ASO delivery to hepatoc
22 r1-/- mice demonstrated that neither MGL nor ASGPR plays significant roles in regulating CHO-rVWF cle
25 ference in the kinetics of ER degradation of ASGPR H2a in susceptible as compared with protected host
27 dase gene (LacZ) resulted in transduction of ASGPR-positive cells (rat hepatocytes or Hepa1 cell line
29 the function of these compounds showed rapid ASGPR-dependent cellular uptake in vitro and high levels
31 subunit of the asialoglycoprotein receptor (ASGPR H2a) were expressed in skin fibroblast cell lines
32 content of the asialoglycoprotein receptor (ASGPR) and three trafficking proteins, Rab3D, Rab7and Ra
34 The mammalian asialoglycoprotein receptor (ASGPR) is located on the sinusoidal membrane of hepatocy
35 binding to the asialoglycoprotein receptor (ASGPR) on the surface of hepatocytes, facilitating liver
38 ins through the asialoglycoprotein receptor (ASGPR)), which mediate the degradation of extracellular
39 that engage the asialoglycoprotein receptor (ASGPR), a liver-specific lysosome-targeting receptor, to
40 tocyte-specific asialoglycoprotein receptor (ASGPR), enhances the potency of second-generation gapmer
41 tor (IGF2R) and asialoglycoprotein receptor (ASGPR), sortilin and transferrin receptors, and show tha
42 apical membrane asialoglycoprotein receptor (ASGPR), which is related to the ASGPR of liver cells.
47 ocyte-specific asialoglycoprotein receptors (ASGPR) to enhance uptake to hepatocytes and to increase
49 inent regression in tumor size confirmed the ASGPR-mediated uptake of ligand-anchored NCs and silenci
50 dependent sorting proteins from cytosol, the ASGPR cytoplasmic domain was expressed as a GST fusion p
51 internalized by HepG2 cells that express the ASGPR but were not taken up by HEK-293 cells that lack t
52 provide a hitherto unsuspected role for the ASGPR in transcriptional signaling, aside from its role
54 provide evidence that phosphorylation of the ASGPR cytoplasmic domain is required for the binding of
57 he coordination of the Ca(2+)-ion within the ASGPR-binding site by the cis-diol motif of the ribose u