ライフサイエンスコーパス: hnRNP U

1 hnRNP U interacts specifically with the proline-rich ami

2 hnRNP U, however, appears to dissociate from the Pol II

3 hnRNP-U directly interacts with NEIL1 in vitro via the N

4 hnRNP-U stimulates the NEIL1 in vitro base excision acti

5 Although hnRNP U and YAP localize to both the nucleus and the cyt

6 AP does not translocate to the nucleus in an hnRNP U-dependent manner.

7 either associated hnRNP protein (hnRNP C and hnRNP U) or either NTPase protein (NAT10 and GNL3L) indu

8 Mutations of human Slo2 channel and hnRNP U are strongly linked to epileptic disorders and i

9 d SRp20, DNA-methyltransferase, hnRNP L, and hnRNP U.

10 S-1 cells, we demonstrate that hnRNP-A/B and hnRNP-U proteins serve antagonistic transcriptional regu

11 th human and rat hnRNP-U, although chURP and hnRNP-U appear not to be orthologous proteins.

12 association of NEIL2, RNA polymerase II, and hnRNP-U on transcribed but not on transcriptionally sile

13 underlying neurological disorders caused by hnRNP U mutations.

14 In contrast, hnRNP U has no effect when co-expressed with a truncated

15 and its Pol II association are necessary for hnRNP U to mediate the repression of Pol II elongation.

16 With such functions, hnRNP U might provide one of the mechanisms by which the

17 Furthermore, hnRNP U and YAP only interact in the nucleus, suggesting

18 We demonstrated that a subfraction of human hnRNP U is associated with the Pol II holoenzyme in vivo

19 In this study, we identified hnRNP U as an RNA trans-factor associated with C9/E3.

20 Importantly, hnRNP U bound specifically to C9/E3 at an RNA cis-elemen

21 The lack of such enhancement in hnRNP-U-depleted cells suggests its involvement in repai

22 The interacting regions in hnRNP-U, mapped to both termini, suggest their proximity

23 tions of HRPU-2, a worm homolog of mammalian hnRNP U, result in dysfunction of a Slo2 potassium chann

24 uorescence labeling and confocal microscopy, hnRNP U appears to colocalize with the virus in the cyto

25 The abilities of hnRNP U to inhibit TFIIH-mediated CTD phosphorylation an

26 AKT pathway in modulating the association of hnRNP U to C9/E3.

27 We find that the middle domain of hnRNP U is sufficient to mediate its Pol II association

28 Co-expression of hnRNP U attenuates the ability of YAP to increase the ac

29 study describes a potential new function of hnRNP U as an RNA polymerase (Pol II) elongation inhibit

30 Loss of hnRNP U expression in cardiomyocytes also leads to aberr

31 tablished a strong link between mutations of hnRNP U and human epilepsies and intellectual disability

32 However, it is unclear how mutations of hnRNP U may cause such disorders.

33 hat SMN interacts with the RGG box region of hnRNP U, with itself, with fibrillarin and with several

34 Down-regulation of hnRNP U led to a decrease in the caspase-9a/9b mRNA rati

35 onclusive evidence for the essential role of hnRNP U in heart development and function and in the reg

36 servations, we suggest that a subfraction of hnRNP U, as a component of the Pol II holoenzyme, may do

37 Finally, depletion of hnRNP-U and NEIL1 epistatically sensitized human cells a

38 zinc-fingers of WT1 and the middle domain of hnRNP-U, and that hnRNP-U can modulate WT1 transcription

39 s 41% amino acid identity with human and rat hnRNP-U, although chURP and hnRNP-U appear not to be ort

40 Subsequently, hnRNP-U binds to the same site to further augment OPN pr

41 eficiency virus type 1 transcription system, hnRNP U inhibits elongation rather than initiation of tr

42 We also demonstrate that hnRNP U is associated with the leader RNA in the nuclei

43 Taken together, these findings show that hnRNP U competes with hnRNP L for binding to C9/E3 to en

44 We showed that hnRNP U can bind TFIIH in vivo under certain conditions

45 These results strongly suggest that hnRNP U plays an important role in the life cycle of VSV

46 1 and the middle domain of hnRNP-U, and that hnRNP-U can modulate WT1 transcriptional activation of a

47 These procedures confirmed that hnRNP-U, hnRNP-D, PCAF, and P-300 bind to the KLF2 promo

48 criptional regulatory role and suggests that hnRNP-U may be a candidate Wilms' tumour gene at 1q44.

49 sed with a truncated YAP protein lacking the hnRNP U-binding site.

50 oxidative genome damage, suggesting that the hnRNP-U protection of cells after oxidative stress is la

51 NEIL1 disordered C-terminal region binds to hnRNP-U at equimolar ratio with high affinity (K(d) = ap

52 ovel nuclear protein structurally related to hnRNP-U (heterogeneous nuclear ribonuclear protein U).

53 eneous nuclear ribonucleoprotein particle U (hnRNP U), which is involved in pre-mRNA processing.

54 heterogeneous nuclear ribonuclear protein U (hnRNP U), an RNA- and DNA-binding protein enriched in th

55 heterogeneous nuclear ribonuclear protein U (hnRNP U).

56 T Heterogeneous nuclear ribonucleoprotein U (hnRNP U) belongs to a family of RNA-binding proteins tha

57 e heterogeneous nuclear ribonucleoprotein U (hnRNP U) in the heart develop lethal dilated cardiomyopa

58 n heterogeneous nuclear ribonucleoprotein U (hnRNP U), plays an important role in regulating the expr

59 e heterogeneous nuclear ribonucleoprotein U (hnRNP U).

60 heterogenous nuclear ribonuclear protein U (hnRNP-U), is phosphorylated on serine 59 by the DNA-depe

61 heterogeneous nuclear ribonuclear protein U (hnRNP-U), that this interaction does not require any oth

62 r heterogeneous nuclear ribonucleoprotein-U (hnRNP-U), both in vitro and in cells.

63 f heterogeneous nuclear ribonucleoprotein-U (hnRNP-U), identified in the immunoprecipitate of human N

64 Phosphorylated hnRNP L interfered with hnRNP U binding to C9/E3, and our results demonstrate th

65 ydroxyuracil in the transcribed strand, with hnRNP-U playing a critical role.

66 by its proline-rich amino terminus, the YAP-hnRNP U interaction may uniquely regulate the nuclear fu

67 The YAP-hnRNP U interaction provides another mechanism of YAP tr