ライフサイエンスコーパス: CUG-BP1

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1 CUG-BP1 is thus a previously unidentified downstream tar

2 Thus, we propose that SRp20, SF2/ASF, and CUG-BP1 act antagonistically to regulate IR alternative

3 Rp20 and SF2/ASF to the exonic enhancers and CUG-BP1 to the exonic silencer by RNA affinity chromatog

4 essor complex consisting of both hnRNP H and CUG-BP1, which is required to maximally inhibit IR exon

5 e demonstrated that the mRNA of survivin and CUG-BP1 each contain two functional miR-214-3p-binding s

6 ls leads to an increase in both survivin and CUG-BP1 mRNA and protein.

7 arget prediction programs, both survivin and CUG-BP1 mRNA were found to contain potential binding sit

8 mRNA and protein levels of both survivin and CUG-BP1.

9 cancer cells by targeting both survivin and CUG-BP1.

10 Both CUG-BP1 and CUG-BP2 have been identified as isoforms of

11 n established between splicing regulation by CUG-BP1, a member of the CELF family of proteins, and DM

12 d CUGBP2) is one of six members of the CELF (CUG-BP1- and ETR-3-like factor) family of splicing regul

13 and functional interactions between hnRNP H, CUG-BP1 and MBNL1 dictate IR splicing in normal and DM1

14 n which expanded repeats result in increased CUG-BP1 activity and/or other CELF family members and ha

15 To determine whether increased CUG-BP1 function was sufficient to model DM, transgenic

16 ion is necessary for the binding activity of CUG-BP1 and the consequent increase in LIP expression, a

17 this leads to an increase in the binding of CUG-BP1 to C/EBP beta mRNA and elevated expression of th

18 ns and an increase in steady state levels of CUG-BP1 (CUGBP-ETR-3 like factor 1, CELF1).

19 muscleblind proteins and increased levels of CUG-BP1 are reported.

20 signaling results in the phosphorylation of CUG-BP1 and this leads to an increase in the binding of

21 oblasts, overexpression of either hnRNP H or CUG-BP1 results in the formation of an RNA-dependent sup

22 ogated with rescue expression of survivin or CUG-BP1.

23 to model DM, transgenic mice overexpressing CUG-BP1 (MCKCUG-BP1) in heart and skeletal muscle, two t

24 crossing these mice with mice overexpressing CUG-BP1, a wild-type CELF protein, rescues defects in al

25 teins SRp20 and SF2/ASF and the CELF protein CUG-BP1.

26 ved increased levels of CUG-binding protein (CUG-BP1) in skeletal muscle, as seen in individuals with

27 n referred to as CUG repeat binding protein (CUG-BP1).

28 were responsive to two other CELF proteins (CUG-BP1 and CELF4), indicating that different members of

29 Two HeLa cell proteins, CUG-BP1 and CUG-BP2, have been purified based upon their

30 sly shown that the RNA-binding protein (RBP) CUG-BP1 is overexpressed in esophageal cancer cells and

31 and SF2/ASF increase exon inclusion but that CUG-BP1 causes exon skipping.

32 We found that CUG-BP1 also binds to an additional intronic splicing si

33 The PBEs and the CUG-BP1 sites were necessary but not sufficient for tran

34 ng elements (PBEs) and binding sites for the CUG-BP1 protein.

35 ivin expression was direct, mediated through CUG-BP1, or both, binding studies utilizing biotin pull-

36 the relative ratios of SRp20 and SF2/ASF to CUG-BP1 in different cells determine the degree of exon

37 While CUG-BP1 is the major (CUG)8-binding activity in normal c

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