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1 released into the media as a membrane-bound GPI-linked protein.
2 rotein tyrosine kinase and a ligand-specific GPI-linked protein.
3 st in part within clusters that also include GPI-linked proteins.
4 inct from caveolin-1-containing caveolae and GPI-linked proteins.
5 n might mechanistically couple caveolin-1 to GPI-linked proteins.
6 and restores the cell surface expression of GPI-linked proteins.
7 t have almost 100% of red cells deficient in GPI-linked proteins.
8 red cells to express low residual levels of GPI-linked proteins.
9 ice had up to 100% of red cells deficient in GPI-linked proteins.
10 of both dorsal and ventral tissues requires GPI-linked proteins.
11 ng are mosaic for cells that express or lack GPI-linked proteins.
12 ctive, suggesting that these tissues require GPI-linked proteins.
13 and absent or reduced surface expression of GPI-linked proteins.
14 monkeys, give rise to efficiently processed GPI-linked proteins.
15 that organize glycosylphosphatidylinositol (GPI)-linked proteins.
16 Isolated raft fractions were enriched in a GPI-linked protein, alkaline phosphatase, and were poor
17 nship between glycosylphosphatidyl inositol (GPI)-linked proteins and caveolins remains controversial
20 oes not vary with the level of expression of GPI-linked proteins, and stable introduction of PIG-A cD
23 type or the recombined allele, implying that GPI-linked proteins are not essential for the derivation
27 GPI anchor is not fully understood; however, GPI-linked proteins cluster into lipid rafts, structures
29 igand-binding glycosyl-phosphatidylinositol (GPI)-linked protein (designated GDNFR-alpha) and the tra
30 ce of a novel glycosyl-phosphatidylinositol (GPI)-linked protein (designated GDNFR-alpha) that is exp
31 identification and tissue distribution of a GPI-linked protein (designated NTNR-alpha) that is struc
32 l analysis, cells acquired new copies of the GPI-linked proteins during incubation with the nonprosta
34 onstrate that Fc gamma RIIA association with GPI-linked proteins facilitates Fc gamma R signal transd
39 roteins (the plasma membrane H+-ATPase and a GPI-linked protein Gas1p) are preferentially excluded fr
41 cient in the glycosyl-phosphatidyl inositol (GPI) -linked protein GFRalpha1 (GDNFRalpha) display defi
42 es of elongation are prevented by removal of GPI-linked proteins implies that they share a common mol
44 wth behavior, and to investigate the role of GPI-linked proteins in hematopoietic differentiation, we
48 uPAR;CD87), a glycosyl-phosphatidylinositol (GPI)-linked protein, in resting neutrophil membranes.
49 erm bone marrow repopulating cells that lack GPI-linked proteins, indicating that recombination of th
52 glycosylated, glycosylphosphatidylinositol (GPI)-linked protein, is expressed preferentially by myof
53 raise the possibility that lipid-associated GPI-linked proteins may be suitable for therapeutic appl
55 s the loss of glycosyl phosphatidylinositol (GPI)-linked proteins on blood cells from patients with p
56 cells lacking glycosylphosphatidylinositol (GPI)-linked proteins on their surface (GPI(neg)) exist a
57 the recombined Piga gene are viable and lack GPI-linked proteins on a proportion of circulating blood
58 g Fc gamma RIIA with CD59 or CD48, two other GPI-linked proteins on Jurkat T cells also led to a syne
61 deficient in glycosyl phosphatidylinositol (GPI)-linked proteins owing to a somatic mutation in the
62 rgent-resistant membrane domains, into which GPI-linked proteins partition, are enriched in cholester
64 that axial mesoderm cells might display the GPI-linked proteins required for elongation of the embry
65 soluble GFRalpha-1 to an embryo lacking all GPI-linked proteins rescues PND migration in a dose-depe
69 family encode glycosyl-phosphatidylinositol (GPI)-linked proteins that are essential for activity of
70 roduced by infected T-cell lines acquire the GPI-linked proteins Thy-1 and CD59, as well as the gangl
72 Endocytosis of glycosylphosphatidylinositol (GPI)-linked proteins via a specific pathway into GPI-enr
73 expression of glycosylphosphatidylinositol (GPI)-linked proteins was analyzed by flow cytometry on m
75 sis of JY5 with stable surface expression of GPI-linked proteins was not statistically different from
77 membrane-bound glycosylphosphatidylinositol (GPI)-linked protein, which functions as an inhibitor of
78 g15) encodes a glycosylphosphatidylinositol (GPI)-linked protein whose in vivo expression increases t
79 hat HDL is a carrier of plasma RT6 and other GPI-linked proteins, with equilibrium between the lipopr
80 by host cell cholesterol, sphingolipids, and GPI-linked proteins within these domains are incorporate
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