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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 ve been widely reported, less is known about hnRNP U's RNA-binding selectivity.
6                                     Although hnRNP U and YAP localize to both the nucleus and the cyt
7 AP does not translocate to the nucleus in an hnRNP U-dependent manner.
8 either associated hnRNP protein (hnRNP C and hnRNP U) or either NTPase protein (NAT10 and GNL3L) indu
9          Mutations of human Slo2 channel and hnRNP U are strongly linked to epileptic disorders and i
10 d SRp20, DNA-methyltransferase, hnRNP L, and hnRNP U.
11 neous nuclear ribonucleoproteins hnRNP R and hnRNP U as KPNA7-interacting proteins.
12 S-1 cells, we demonstrate that hnRNP-A/B and hnRNP-U proteins serve antagonistic transcriptional regu
13 th human and rat hnRNP-U, although chURP and hnRNP-U appear not to be orthologous proteins.
14 association of NEIL2, RNA polymerase II, and hnRNP-U on transcribed but not on transcriptionally sile
15  underlying neurological disorders caused by hnRNP U mutations.
16                                 In contrast, hnRNP U has no effect when co-expressed with a truncated
17 and its Pol II association are necessary for hnRNP U to mediate the repression of Pol II elongation.
18                         With such functions, hnRNP U might provide one of the mechanisms by which the
19                                 Furthermore, hnRNP U and YAP only interact in the nucleus, suggesting
20  We demonstrated that a subfraction of human hnRNP U is associated with the Pol II holoenzyme in vivo
21 o quantitatively assess the ability of human hnRNP U RBD to interact with segments of cellular RNAs i
22                 In this study, we identified hnRNP U as an RNA trans-factor associated with C9/E3.
23                                 Importantly, hnRNP U bound specifically to C9/E3 at an RNA cis-elemen
24              The lack of such enhancement in hnRNP-U-depleted cells suggests its involvement in repai
25                   The interacting regions in hnRNP-U, mapped to both termini, suggest their proximity
26 tions of HRPU-2, a worm homolog of mammalian hnRNP U, result in dysfunction of a Slo2 potassium chann
27 uorescence labeling and confocal microscopy, hnRNP U appears to colocalize with the virus in the cyto
28                             The abilities of hnRNP U to inhibit TFIIH-mediated CTD phosphorylation an
29 AKT pathway in modulating the association of hnRNP U to C9/E3.
30            We find that the middle domain of hnRNP U is sufficient to mediate its Pol II association
31                             Co-expression of hnRNP U attenuates the ability of YAP to increase the ac
32  study describes a potential new function of hnRNP U as an RNA polymerase (Pol II) elongation inhibit
33                                      Loss of hnRNP U expression in cardiomyocytes also leads to aberr
34 tablished a strong link between mutations of hnRNP U and human epilepsies and intellectual disability
35      However, it is unclear how mutations of hnRNP U may cause such disorders.
36 hat SMN interacts with the RGG box region of hnRNP U, with itself, with fibrillarin and with several
37                           Down-regulation of hnRNP U led to a decrease in the caspase-9a/9b mRNA rati
38          In contrast, the isolated RGG/RG of hnRNP U motif exhibits a strong preference for G-quadrup
39 onclusive evidence for the essential role of hnRNP U in heart development and function and in the reg
40 servations, we suggest that a subfraction of hnRNP U, as a component of the Pol II holoenzyme, may do
41                        Finally, depletion of hnRNP-U and NEIL1 epistatically sensitized human cells a
42 zinc-fingers of WT1 and the middle domain of hnRNP-U, and that hnRNP-U can modulate WT1 transcription
43                 The abundant nuclear protein hnRNP U interacts with a broad array of RNAs along with
44 s 41% amino acid identity with human and rat hnRNP-U, although chURP and hnRNP-U appear not to be ort
45                                Subsequently, hnRNP-U binds to the same site to further augment OPN pr
46 eficiency virus type 1 transcription system, hnRNP U inhibits elongation rather than initiation of tr
47                     We also demonstrate that hnRNP U is associated with the leader RNA in the nuclei
48 rthermore, while it is well established that hnRNP U binds numerous nuclear RNAs, it remains unknown
49     Taken together, these findings show that hnRNP U competes with hnRNP L for binding to C9/E3 to en
50                               We showed that hnRNP U can bind TFIIH in vivo under certain conditions
51          These results strongly suggest that hnRNP U plays an important role in the life cycle of VSV
52 1 and the middle domain of hnRNP-U, and that hnRNP-U can modulate WT1 transcriptional activation of a
53              These procedures confirmed that hnRNP-U, hnRNP-D, PCAF, and P-300 bind to the KLF2 promo
54 criptional regulatory role and suggests that hnRNP-U may be a candidate Wilms' tumour gene at 1q44.
55 sed with a truncated YAP protein lacking the hnRNP U-binding site.
56                   These data reveal that the hnRNP U RBD attenuates the RNA binding selectivity of it
57 lysis of several target RNAs reveal that the hnRNP U RBD binds RNA in a promiscuous manner with high
58 oxidative genome damage, suggesting that the hnRNP-U protection of cells after oxidative stress is la
59  NEIL1 disordered C-terminal region binds to hnRNP-U at equimolar ratio with high affinity (K(d) = ap
60 ovel nuclear protein structurally related to hnRNP-U (heterogeneous nuclear ribonuclear protein U).
61 eneous nuclear ribonucleoprotein particle U (hnRNP U), which is involved in pre-mRNA processing.
62 heterogeneous nuclear ribonuclear protein U (hnRNP U), an RNA- and DNA-binding protein enriched in th
63 heterogeneous nuclear ribonuclear protein U (hnRNP U).
64 T Heterogeneous nuclear ribonucleoprotein U (hnRNP U) belongs to a family of RNA-binding proteins tha
65 e heterogeneous nuclear ribonucleoprotein U (hnRNP U) in the heart develop lethal dilated cardiomyopa
66 n heterogeneous nuclear ribonucleoprotein U (hnRNP U), plays an important role in regulating the expr
67 e heterogeneous nuclear ribonucleoprotein U (hnRNP U).
68  heterogenous nuclear ribonuclear protein U (hnRNP-U), is phosphorylated on serine 59 by the DNA-depe
69 heterogeneous nuclear ribonuclear protein U (hnRNP-U), that this interaction does not require any oth
70 r heterogeneous nuclear ribonucleoprotein-U (hnRNP-U), both in vitro and in cells.
71 f heterogeneous nuclear ribonucleoprotein-U (hnRNP-U), identified in the immunoprecipitate of human N
72       Phosphorylated hnRNP L interfered with hnRNP U binding to C9/E3, and our results demonstrate th
73 ydroxyuracil in the transcribed strand, with hnRNP-U playing a critical role.
74  by its proline-rich amino terminus, the YAP-hnRNP U interaction may uniquely regulate the nuclear fu
75                                      The YAP-hnRNP U interaction provides another mechanism of YAP tr