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1 nd that binds with its erythrocyte receptor, Basigin.
2 acid (SA), complement receptor 1 (CR1), and basigin.
3 g the interaction of PfRH5 with its receptor basigin.
4 t mouse basigin can functionally replace fly basigin.
5 fects and neuron-glia interaction defects of basigin.
6 o determine the identity of the receptor for basigin.
7 We show that RdCVF acts through binding to Basigin-1 (BSG1), a transmembrane protein expressed spec
8 The specific and limited expression of 5A11/Basigin-2 explicitly within photoreceptor cells implies
12 in tissue remodeling and angiogenesis makes basigin a potential target for the development of strate
13 ial binding of PfRh5/CyRPA/PfRipr complex to basigin, a step linked to the formation of a pore betwee
16 recombinant chimeric antibody (Ab-1) against basigin, an erythrocyte receptor necessary for parasite
17 PvTRAg38 binds to two erythrocyte receptors basigin and band 3 through P2 and P4 regions, respective
20 ting that simultaneous blockade of the PfRH5-Basigin and PfRH5/PfRipr/CyRPA interactions produced an
21 functions as a membrane receptor for soluble basigin and this homophilic interaction is not dependent
24 ely blocked using low concentrations of anti-basigin antibodies; importantly, these effects were obse
27 ng CRISPR/Cas9, we deleted two host factors, basigin (BSG) and CD44, for which no natural nulls exist
30 atrix metalloproteinase (MMP)-2, MMP-14, and basigin (BSG) are major enzymes involved in the maintena
31 Reticulocyte-binding protein Homolog 5 (RH5)-Basigin (BSG) interaction in host-species selectivity an
34 identified as the transmembrane glycoprotein basigin (BSG, CD147); more particularly, its low glycosy
37 ibodies or other therapeutics targeting host basigin could be an effective treatment for patients inf
40 results demonstrate that rBSG interacts with basigin expressed on the surface of fibroblasts and is s
42 rane protein CD147 (also known as EMMPRIN or basigin) forms a specific heterodimeric complex in the m
43 nd the extracellular domains are crucial for basigin function in the visual system while the short in
46 alternative transcription initiation of BSG (Basigin) gene by differentially influencing RNAPII densi
47 srupted, via zinc finger nucleases, MCT4 and BASIGIN genes in colon adenocarcinoma (LS174T) and gliob
54 r transgenic fly basigin or transgenic mouse basigin in the photoreceptors demonstrating that mouse b
55 the neural retina supporting a role for 5A11/basigin in the targeting of these transporters to the pl
56 hermal-shift-assays confirmed ACF binding to basigin in vitro and in live glioblastoma cells, respect
58 following: 1) the ability to block the PfRH5-basigin interaction in vitro is predictive of functional
59 sought to determine if disruption of the MCT-Basigin interaction may be achieved with a small molecul
64 In summary, our results demonstrate that basigin is very likely the apoD receptor and provide add
67 lin superfamily glycoprotein CD147 (emmprin; basigin) is associated with an invasive phenotype in var
68 oproteinase inducer) also known as CD147 and basigin, is a member of the immunoglobulin family that i
69 longer form, a splice variant of mouse 5A11/Basigin, is a member of the immunoglobulin gene superfam
70 have found that the Ok blood group antigen, basigin, is a receptor for PfRh5, a parasite ligand that
71 corresponding to the extracellular domain of basigin, it was demonstrated that the native, nonglycosy
72 potently inhibited by soluble basigin or by basigin knockdown, and invasion could be completely bloc
76 disruption of MCT binding to their chaperon, Basigin, may be an effective approach to target GSC and
78 itudes in the electroretinograms in the 5A11/basigin null mouse (Bsg(-/-)) may be linked to altered e
79 e invasion was potently inhibited by soluble basigin or by basigin knockdown, and invasion could be c
80 oproteinase inducer (EMMPRIN), also known as basigin or CD147, is a glycoprotein that is enriched on
81 scued by expression of either transgenic fly basigin or transgenic mouse basigin in the photoreceptor
82 15 monoclonal antibodies recognizing EMMPRIN/basigin/OX-47/M6, a 45-55-kDa transmembrane protein with
88 osaic animals that are mutant in the eye for basigin show altered cell structure with nuclei, mitocho
89 an effort to determine the function of 5A11/Basigin, the molecular diversity of its expression was e
90 er and (2) disrupting a key interaction with basigin, thereby reducing cell-surface localization.
94 h of these functions, we have created mutant basigin transgenes coding for proteins that are altered
95 ermore, Ok(a-) erythrocytes, which express a basigin variant that has a weaker binding affinity for P
96 cificity of interaction between PvTRAg38 and basigin was confirmed by direct interaction where basigi
97 r mediator of SA-independent invasion, while basigin was essential for both SA-dependent and SA-indep
98 in was confirmed by direct interaction where basigin was specifically recognized by P2 and not by the
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