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1 and podocalyxin comprise the CD34 family of sialomucins.
2 es a sulfated oligosaccharide carried by the sialomucins.
3 m selective metastasis of cells that produce sialomucins.
4 decrease in cell surface 9-O-acetylation of sialomucins.
5 des, O-linked chains carried on cell surface sialomucins.
6 gs to the CD34-family of highly glycosylated sialomucins.
7 The C2-O-sLe(X) motif occurs primarily on sialomucins and has been directly shown to contribute to
10 mmune checkpoint receptor, selectively binds sialomucins as biological ligands, whereas the related r
11 rodimeric glycoprotein complex composed of a sialomucin ascites sialoglycoprotein (ASGP)-1 and a tran
12 ed expression of cell surface 9-O-acetylated sialomucins (but not the 9-O-acetylated ganglioside).
13 digestion with a glycoprotease that digests sialomucins, but no adhesion to cells that express selec
14 clonal antibody MECA-79 reacts with the PNAd sialomucins by recognizing an N-acetylglucosamine (GlcNA
18 One such stem cell-associated antigen is the sialomucin CD34, a highly O-glycosylated cell surface gl
19 and demonstrated increased expression of the sialomucins CD34 and ENCM, which were also observed at t
20 reported that MAb L11, against the leukocyte sialomucin CD43, blocks T-lymphocyte binding to lymph no
22 Overexpression of the membrane mucin MUC4/Sialomucin complex (SMC) has been observed during malign
27 mucin is considered as the homologue of rat sialomucin complex (SMC, rat Muc4) due to its similar st
32 munofluorescence staining was used to detect sialomucin complex in frozen sections and impression cyt
37 ent epitope on the mucin subunit (ASGP-1) of sialomucin complex occurs in a differentiation-dependent
43 Northern blot analyses were used to identify sialomucin complex/Muc4 (SMC/Muc4) mRNA in rat lacrimal
44 d peripheral node addressin (PNAd), a set of sialomucins displayed on high endothelial venules (HEVs)
45 nsin-180 contains 17 leucine-rich repeats, a sialomucin domain, an apparent transmembrane domain, and
46 re with the other family members including a sialomucin domain, but also possesses an extremely acidi
50 selectin glycoprotein ligand 1 (PSGL-1) is a sialomucin expressed on leukocytes that mediates neutrop
51 in ligand-1 (PSGL-1), a heavily glycosylated sialomucin expressed on most leukocytes, has dual functi
52 cantly increased levels of mRNA for CD164, a sialomucin found on human CD34+ hematopoietic stem cells
53 We show that purified neutrophil PSGL-1, a sialomucin glycoprotein that serves as a ligand for both
56 heavily O-glycosylated single-transmembrane sialomucin, interferes with the interactions between inf
58 teractions mediated by L-selectin binding to sialomucin ligands in high endothelial venules (HEVs).
59 ectin expressed on lymphocytes with sulfated sialomucin ligands such as CD34 and GlyCAM-1 on high end
64 ion into lymphoid tissues through binding to sialomucin-like receptors on the surface of high endothe
65 ll incompletely defined, they share a common sialomucin-like structure which is thought to present cl
66 P-selectin glycoprotein ligand-1 (PSGL-1), a sialomucin on human leukocytes, mediates rolling of leuk
67 nitor cells (HSPCs) express platelet-binding sialomucin P-selectin (CD162) and integrin Mac-1 (CD11b-
68 y and confirmed recently that podocalyxin, a sialomucin, plays a major role in maintaining the urinar
71 m that results in expression of glycosylated sialomucin proteins and the vesicle tethering and fusion
72 ning of neutrophils was diminished following sialomucin removal by O-glycoprotease, and its reactivit
73 differentiation of cultured myoblasts, (ii) sialomucins represent a class of potential effectors of
74 calyxin, and endoglycan comprise a family of sialomucins sharing both structural similarity and seque
75 an endopeptidase that selectively degrades O-sialomucins such as PSGL-1, abolished P-selectin but not
77 D164 encodes a widely expressed cell surface sialomucin that has been implicated in regulation of cel
78 odocalyxin is an anti-adhesive transmembrane sialomucin that has been implicated in the development o
79 lyxin-like protein (PCLP) is a transmembrane sialomucin that is similar in structure to the well-char
81 L-selectin on lymphocytes and PNAd, a set of sialomucins that are constitutively displayed on high en
82 se-dependent expression of this CD34-related sialomucin was discovered in Kit(+)CD71(high) proerythro
83 D34 and podocalyxin are structurally related sialomucins, which are expressed in multiple tissues inc
84 Furthermore, we show that GD3.5 and WC1 are sialomucins, which provides important clues to their fun
85 hepatic endothelial cells, and inhibition of sialomucin with antisense to the MUC2 gene inhibited adh