ライフサイエンスコーパス: hnRNP C

1 hnRNP C exists as a stable tetramer that binds about 230

2 RL system supplemented with exogenous active hnRNP C.

3 gesting a potential role for PTEN, alongside hnRNP C, in RNA regulation.

4 he AU-rich element-binding proteins AUF1 and hnRNP C with GM-CSF mRNA, accelerating or slowing decay,

5 ein (GFP) tags we have shown that CUG-BP and hnRNP C do not co-localise with expanded repeat foci in

6 ns, the 56-kD heat shock protein, hsp56, and hnRNP C do not export from nuclei of permeabilized cells

7 tion and RNA binding proteins YB-1, HuR, and hnRNP C.

8 the large pyrimidine-rich region by PTB and hnRNP C may play a role in the initiation and/or regulat

9 role of three RNA-binding proteins, CUG-BP, hnRNP C and MBNL, as possible sequestered factors.

10 Therefore, occupancy of the 29 nt element by hnRNP C stabilized APP mRNA and enhanced its translation

11 lacking the 29 nt element were unaffected by hnRNP C supplementation.

12 t heterogeneous nuclear ribonucleoprotein C (hnRNP C) and nucleolin bound specifically to a 29 nt seq

13 d heterogeneous nuclear ribonucleoprotein C (hnRNP C) as a novel protein recruited to higher molecula

14 e heterogeneous nuclear ribonucleoprotein C (hnRNP C) family.

15 s heterogeneous nuclear ribonucleoprotein C (hnRNP C).

16 r heterogeneous nuclear ribonucleoprotein C (hnRNP C).

17 f heterogeneous nuclear ribonucleoprotein C (hnRNP-C), a nuclear restricted pre-mRNA-binding protein,

18 ation of peripheral blood mononuclear cells, hnRNP C and nucleolin acquired APP mRNA binding activity

19 y preventing U2AF65 binding to Alu elements, hnRNP C plays a critical role as a genome-wide sentinel

20 Further analysis indicates that endogenous hnRNP C and PTEN interact and co-localize within the nuc

21 NA is capable of interacting with endogenous hnRNP C, as well as with poliovirus nonstructural protei

22 We identified four RNA splicing factors--hnRNP C, U2AF (U2 auxiliary factor), PTB (polypyrimidine

23 hnRNP A1 binding site, or binding sites for hnRNP C and L are unable to stimulate Rev-mediated RNA t

24 ex containing the proteins hnRNP M, hnRNP H, hnRNP C, Matrin3, NF110/NFAR-2, NF45, and DDX5, all appr

25 ciated mutations in Alu elements that hamper hnRNP C binding.

26 anner similar to the cognate region of human hnRNP-C.

27 e cross-link distribution of the full-length hnRNP C on short uridine tracts.

28 We propose that the association of hnRNP C with poliovirus negative-strand termini acts to

29 Indirect functional depletion of hnRNP C from in vitro replication reactions, using polio

30 RNA synthesis in vitro and that depletion of hnRNP C proteins in cultured cells results in decreased

31 suggested that the regulated interaction of hnRNP C and nucleolin with APP mRNA controlled its stabi

32 Loss of hnRNP C leads to formation of previously suppressed Alu

33 ng the biological functions and structure of hnRNP C tetramers, we have determined the high-resolutio

34 lation modulates the mRNA binding ability of hnRNP-C.

35 n mouse liver that phosphorylates the ACD of hnRNP-C at Ser(240) and at two sites at Ser(225)-Ser(228

36 l cell nuclei also phosphorylated the ACD of hnRNP-C at these positions.

37 ng a recombinant acidic C-terminal domain of hnRNP-C overexpressed in Escherichia coli demonstrate th

38 d the H(2)O(2)-stimulated phosphorylation of hnRNP-C.

39 mutations, the effects of phosphorylation on hnRNP-C function were investigated by quantitative equil

40 C after TNF-alpha plus fibronectin but only hnRNP C after HA.

41 RNPs lacking interaction with Sm proteins or hnRNP C remain fully functional for telomere elongation.

42 of potential interaction surfaces for other hnRNP C domains along the coiled coil exterior and the a

43 iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many

44 pression of either associated hnRNP protein (hnRNP C and hnRNP U) or either NTPase protein (NAT10 and

45 te that the addition of recombinant purified hnRNP C proteins can stimulate virus RNA synthesis in vi

46 of endogenous nucleolin, but failed to show hnRNP C binding activity.

47 We analyze RNA-Seq data to show that hnRNP C is a potential regulator of SMN6B expression and

48 Here we show that hnRNP C proteins are restricted to the nucleus not becau

49 nd other findings it has been suggested that hnRNP C functions as a chaperonin to maintain long lengt

50 The hnRNP C protein tetramer cooperatively binds 230 nt incr

51 The hnRNP C proteins are representative of the nonshuttling

52 demonstrate that two subsets of hnRNPs, the hnRNP C and M proteins, are substrates for SUMO modifica

53 gs, we propose that SUMO modification of the hnRNP C and M proteins may occur at NPCs and facilitate

54 NPCs, enhances the SUMO modification of the hnRNP C and M proteins.

55 RRM as the primary RNA-binding domain of the hnRNP C tetramer and provides a proof of concept for int

56 We demonstrate that the hnRNP C proteins are modified by SUMO at a single lysine

57 The domain is structurally homologous to hnRNP-C from higher organisms.