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1 gulates GLUT1-mediated glucose transport via stomatin.
2 3, flotillin-1 and -2, peroxiredoxin-2, and stomatin.
3 s overall approximately 20% similar to human stomatin.
4 ning these three components is equivalent to stomatin.
5 s a close homologue of the mammalian protein stomatin.
6 t does contain an orthologue of human band 7 stomatin, a protein known to oligomerize, associate with
11 sterol and major raft proteins flotillin and stomatin and contain low levels of cytoskeleton, all cha
12 e switch is mediated by the membrane protein stomatin and is an evolutionary adaptation to vitamin C
15 ved in proliferation and cell cycle control, stomatins are involved in ion channel regulation, and th
20 s report describes the cloning of the murine stomatin chromosomal gene, determination of its genomic
23 ersity of signaling protein genes, including stomatin (Epb7.2), S100A5, Ddit3, Sirt2, CD81, Sdc2, Omp
24 Its product, podocin, is a new member of the stomatin family, which consists of hairpin-like integral
26 raft-associated integral membrane proteins (stomatin, flotillin 1, and flotillin 2), extracellular s
27 oncordance between the exon structure of the stomatin gene and the locations of three domains predict
29 s identify a novel and unusual member of the stomatin gene superfamily that interacts with the periph
33 ng and characterization of a new and unusual stomatin homologue, human SLP-2 (stomatin-like protein 2
35 )-terminal hydrophobic domain found in other stomatin homologues and (unlike stomatin) is fully extra
41 und in other stomatin homologues and (unlike stomatin) is fully extractable from erythrocyte membrane
46 ate that Parkin interacts with mitochondrial Stomatin-like protein 2 (SLP-2), which also binds the mi
47 romatography and tandem mass spectrometry as stomatin-like protein 2 (Stoml2), previously described a
50 on), suppresses three phenotypes of neuronal stomatin-like protein deficiency as follows: volatile an
51 lone molecules, it has now been shown that a stomatin-like protein regulates a gap junction channel i
52 and functions synergistically with MEC-2 (a stomatin-like protein that regulates MEC-4(d)/MEC-10(d)
56 anically gated ion channels is controlled by stomatin-like protein-3 (STOML3), which is required for
58 enome contains two paralogous genes encoding stomatin-like proteins (SLPs; AtSLP1 and AtSLP2) that ar
59 y that similar ion channels may be formed by stomatin-like proteins and DEG/ENaC proteins that are co
61 cate that modulation of DEG/ENaC channels by stomatin-like proteins is evolutionarily conserved and m
62 d ssu-1 is the first association of neuronal stomatin-like proteins sharing regulatory roles with a s
65 e integral membrane protein MEC-2 contains a stomatin-like region that is highly conserved from bacte
67 eract with the MEC-4 degenerin through their stomatin-like regions, which act as protein binding doma
68 Thus, like caveolin-1 and flotillin-1, a stomatin may also associate with non-clathrin coated, DR
69 channel subunit MEC-4 and channel-associated stomatin MEC-2 are specifically required for neural resp
71 es that are membrane raft associated, namely stomatin, paraslipin (previously SLP-2) and flotillin.
73 , as with the erythrocyte lipid raft protein stomatin, podocin is present in high-order oligomers and
76 rug resistance proteins, and proteins of the stomatin/prohibitin/hypersensitive response family, sugg
77 d' form shows very leaky cells and the 32 kD stomatin protein is missing, although the gene is not mu
78 yed a greater association with flotillin and stomatin, proteins known to associate with sphingolipid-
79 dentified in nonerythroid tissues, and other stomatin related proteins are found in Drosophila, Caeno
81 ral, stomatin-like domain of MEC-2 nor human stomatin retained the activity of full-length MEC-2, bot
82 unc-24, named ssu-1(fc73) (for suppressor of stomatin uncoordination), suppresses three phenotypes of
83 To establish the identity of the signal, stomatin was fractionated by combinations of cation exch
85 phb1, Zm-phb2, Zm-phb3, and Zm-phb4), one to stomatins (Zm-stm1), and three to a gene implicated in p
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