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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  Here we demonstrate that the RBPs CELF2 and hnRNP C regulate the expression of each other, such that
7 ns, the 56-kD heat shock protein, hsp56, and hnRNP C do not export from nuclei of permeabilized cells
8 tion and RNA binding proteins YB-1, HuR, and hnRNP C.
9  the large pyrimidine-rich region by PTB and hnRNP C may play a role in the initiation and/or regulat
10                        Knockdown of RALY and hnRNP-C increased levels of viral RNA splicing, protein
11 at viral-mediated ubiquitination of RALY and hnRNP-C relieves a restriction on viral RNA processing a
12 ocused on two RNA-binding proteins, RALY and hnRNP-C, which we confirm are ubiquitinated without degr
13  role of three RNA-binding proteins, CUG-BP, hnRNP C and MBNL, as possible sequestered factors.
14 Therefore, occupancy of the 29 nt element by hnRNP C stabilized APP mRNA and enhanced its translation
15 lacking the 29 nt element were unaffected by hnRNP C supplementation.
16 t heterogeneous nuclear ribonucleoprotein C (hnRNP C) and nucleolin bound specifically to a 29 nt seq
17 d heterogeneous nuclear ribonucleoprotein C (hnRNP C) as a novel protein recruited to higher molecula
18 e heterogeneous nuclear ribonucleoprotein C (hnRNP C) family.
19 s heterogeneous nuclear ribonucleoprotein C (hnRNP C).
20 r heterogeneous nuclear ribonucleoprotein C (hnRNP C).
21 f heterogeneous nuclear ribonucleoprotein C (hnRNP-C), a nuclear restricted pre-mRNA-binding protein,
22 ation of peripheral blood mononuclear cells, hnRNP C and nucleolin acquired APP mRNA binding activity
23 y preventing U2AF65 binding to Alu elements, hnRNP C plays a critical role as a genome-wide sentinel
24   Further analysis indicates that endogenous hnRNP C and PTEN interact and co-localize within the nuc
25 NA is capable of interacting with endogenous hnRNP C, as well as with poliovirus nonstructural protei
26     We identified four RNA splicing factors--hnRNP C, U2AF (U2 auxiliary factor), PTB (polypyrimidine
27  hnRNP A1 binding site, or binding sites for hnRNP C and L are unable to stimulate Rev-mediated RNA t
28 ex containing the proteins hnRNP M, hnRNP H, hnRNP C, Matrin3, NF110/NFAR-2, NF45, and DDX5, all appr
29 ciated mutations in Alu elements that hamper hnRNP C binding.
30 anner similar to the cognate region of human hnRNP-C.
31 e cross-link distribution of the full-length hnRNP C on short uridine tracts.
32 ogether, this work reveals new activities of hnRNP C and CELF2, provides insight into a previously un
33           We propose that the association of hnRNP C with poliovirus negative-strand termini acts to
34             Indirect functional depletion of hnRNP C from in vitro replication reactions, using polio
35 RNA synthesis in vitro and that depletion of hnRNP C proteins in cultured cells results in decreased
36  of CELF2 results in decreased efficiency of hnRNP C translation.
37  suggested that the regulated interaction of hnRNP C and nucleolin with APP mRNA controlled its stabi
38                                      Loss of hnRNP C leads to formation of previously suppressed Alu
39           Specifically, we show that loss of hnRNP C reduces the transcription of CELF2 mRNA, while l
40 ng the biological functions and structure of hnRNP C tetramers, we have determined the high-resolutio
41 lation modulates the mRNA binding ability of hnRNP-C.
42 n mouse liver that phosphorylates the ACD of hnRNP-C at Ser(240) and at two sites at Ser(225)-Ser(228
43 l cell nuclei also phosphorylated the ACD of hnRNP-C at these positions.
44 ng a recombinant acidic C-terminal domain of hnRNP-C overexpressed in Escherichia coli demonstrate th
45 irus resulted in an increased interaction of hnRNP-C with viral RNA and attenuation of viral RNA proc
46 d the H(2)O(2)-stimulated phosphorylation of hnRNP-C.
47 mutations, the effects of phosphorylation on hnRNP-C function were investigated by quantitative equil
48  C after TNF-alpha plus fibronectin but only hnRNP C after HA.
49 RNPs lacking interaction with Sm proteins or hnRNP C remain fully functional for telomere elongation.
50  of potential interaction surfaces for other hnRNP C domains along the coiled coil exterior and the a
51 iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many
52 pression of either associated hnRNP protein (hnRNP C and hnRNP U) or either NTPase protein (NAT10 and
53 te that the addition of recombinant purified hnRNP C proteins can stimulate virus RNA synthesis in vi
54  of endogenous nucleolin, but failed to show hnRNP C binding activity.
55         We analyze RNA-Seq data to show that hnRNP C is a potential regulator of SMN6B expression and
56                            Here we show that hnRNP C proteins are restricted to the nucleus not becau
57 nd other findings it has been suggested that hnRNP C functions as a chaperonin to maintain long lengt
58                                          The hnRNP C protein tetramer cooperatively binds 230 nt incr
59                                          The hnRNP C proteins are representative of the nonshuttling
60  demonstrate that two subsets of hnRNPs, the hnRNP C and M proteins, are substrates for SUMO modifica
61 gs, we propose that SUMO modification of the hnRNP C and M proteins may occur at NPCs and facilitate
62  NPCs, enhances the SUMO modification of the hnRNP C and M proteins.
63 RRM as the primary RNA-binding domain of the hnRNP C tetramer and provides a proof of concept for int
64                      We demonstrate that the hnRNP C proteins are modified by SUMO at a single lysine
65     The domain is structurally homologous to hnRNP-C from higher organisms.