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1 al antibodies against ezrin, the canalicular actin-associated protein.
2 rafts is mediated through interactions with actin-associated proteins.
3 hat reside at the C-terminus of a variety of actin-associated proteins.
4 polymerization per se and through binding of actin-associated proteins.
5 ts as well as its interaction with a host of actin-associated proteins.
6 tion of the actin cytoskeleton by regulating actin-associated proteins.
13 are consensus binding sites for a number of actin-associated proteins and are also near to sites of
14 which, via PKCs, mediates phosphorylation of actin-associated proteins and cytoskeletal rearrangement
16 leton regulation, including actin itself, 10 actin-associated proteins, and 3 regulatory proteins.
17 also be used to model the action of several actin-associated proteins, and for large-scale simulatio
18 show that the septin Peanut, actin, and the actin-associated protein Anillin, do not become correctl
22 h that the interaction between microRNAs and actin-associated protein Arpc5 sets the stage for an ela
23 zed a genome-wide screen to identify several actin-associated proteins as candidate LMP1-binding prot
24 for Dcx, widespread differences are found in actin-associated proteins as compared with wild-type axo
29 s have demonstrated how collective action of actin-associated proteins can organize actin filaments i
30 ortex and functions in a novel mitochondrial/actin-associated protein complex that sequesters Bcl-xL.
33 ion is dependent on its interaction with the actin-associated protein Enabled (Ena) via a conserved L
36 , which shares significant homology with the actin-associated proteins ezrin, radixin and moesin (ERM
37 ting protein (PSTPIP), a novel member of the actin- associated protein family that is homologous to S
38 ding member of a novel class of proline-rich actin-associated proteins highly expressed in telencepha
39 ly member 3 (SHROOM3) gene, which encodes an actin-associated protein important in epithelial morphog
40 of the F-actin cytoskeleton, but the role of actin-associated proteins in this process is not well ch
41 These findings identify a unique role for actin-associated proteins in translational regulation, a
42 ve tissues affects the dynamics of actin and actin-associated proteins, in turn disrupting the organi
48 tions in the actin gene or in genes encoding actin-associated proteins: MATa/alpha cells were defecti
50 re, we investigate the specific roles of two actin-associated proteins, myosin II and myristoylated a
55 ndings thus reveal a novel mechanism whereby actin-associated proteins regulate proliferation by medi
57 [1,2]D) targeting signals and identified the actin-associated protein Sla1p as the adaptor for NPFX(1
59 in filament network topology and the role of actin-associated proteins such as Arp2/3 are examined.
60 Moreover, we see a higher concentration of actin-associated proteins such as vinculin, talin, and a
62 -binding) motif and interacted with FLNa, an actin-associated protein that integrates cell mechanics
63 the C-terminal tail of ClC-5 and cofilin, an actin-associated protein that is crucial in the regulati
64 horylated protein (MAYP), p37 is the major F-actin-associated protein that is tyrosine-phosphorylated
66 w for the first time that LKB1 is a dynamic, actin-associated protein that rapidly polarizes to the l
68 ut the mechanisms of how this occurs and the actin-associated proteins that function in this process
69 spectrin, actin, protein 4.1R, ankyrin, and actin-associated proteins that laminates the inner membr
70 ofilament rearrangement and translocation of actin-associated proteins, the current study correlates
71 a natural fusion of two canonical classes of actin-associated proteins, the ezrin-radixin-moesin fami
74 inosomes, and a concentrated accumulation of actin-associated proteins was observed to occur in respo
75 phenotype resulting from silencing of other actin-associated proteins, we show that this phenotype i
76 ssays with LMP1 induced biotinylation of the actin-associated proteins, which were shifted in molecul
77 sgelins are members of a conserved family of actin-associated proteins widely expressed from yeast to
78 f budding yeast contains an extensive set of actin-associated proteins with conserved mammalian count
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