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1 snRNPs are assembled in the cytoplasm in a stepwise mann
3 nome-wide studies revealed that KAP1 and 7SK snRNP co-occupy most promoter-proximal regions containin
4 f an unprecedented mechanism controlling 7SK snRNP delivery to promoter-proximal regions to facilitat
5 pathway, calpain 2 cleavage of the core 7SK snRNP component MePCE promoted P-TEFb release and conseq
9 oop, liberating P-TEFb from the inactive 7SK snRNP, and inducing the formation of the Tat-SEC complex
11 ARP7) is a constitutive component of the 7SK snRNP and localizes to the 3' terminus of the 7SK long n
13 on elongation factor b (P-TEFb) from the 7SK snRNP in a manner that is dependent on its helicase acti
14 elongation and sn/snoRNA synthesis, the 7SK snRNP is a key regulator of nuclear RNA production by RN
16 is study, the release of P-TEFb from the 7SK snRNP led to increased synthesis of HEXIM1 but not HEXIM
19 regulator KAP1 continuously tethers the 7SK snRNP to PRG promoters to facilitate P-TEFb recruitment
25 ted WT mice showed elevated anti-dsDNA, anti-snRNP, CXCL1, and MCP-1 levels compared to untreated mic
26 ed to untreated mice; however levels of anti-snRNP, MCP-1, and CXCL1 were reduced in pristane-treated
27 ts that have been characterized thus far are snRNP proteins because, in contrast to individual snRNPs
28 proliferating cells, which actively assemble snRNPs, as a readout for unperturbed SMN complex functio
29 d intracellular localization of autoantibody snRNP complexes was measured by flow cytometry and confo
31 ith both in vitro-reconstituted and cellular snRNPs led to similar changes in SHAPE reactivities, con
35 investigated the mechanism of SMN-dependent snRNP assembly, as well as the downstream effects on pre
36 /U6 di-small nuclear RNA-protein complex (di-snRNP) during spliceosome activation via ATP-driven tran
37 ein components to the snRNA duplex during di-snRNP assembly by electrophoretic mobility shift assay a
38 Base-pairing of U4 and U6 snRNAs during di-snRNP assembly requires large-scale remodeling of RNA st
39 of human RNPC3, also known as the U11/U12 di-snRNP 65-kDa protein, a unique component of the U12-type
41 6 helix II and an interface between U4/U6 di-snRNP and the U2 snRNP SF3b-containing domain, which als
43 set up a recombinant Brr2-mediated U4/U6 di-snRNP disruption system, showing that sequential additio
44 of the function played by SART3 in U4/U6 di-snRNP formation, our discovery points to a direct link b
49 es not play a significant role in Drosophila snRNP import and demonstrate a crucial function for Msk
59 proteins because, in contrast to individual snRNPs, purification of intact spliceosomes has not been
61 s and a longer helix 1 to discover new intra-snRNP synergies with U1 subunits Nam8 and Mud1 and the t
62 PN1, which is essential for TMG cap-mediated snRNP import in humans, is not well conserved in flies.
63 ges of SMN give rise to loss of SMN-mediated snRNP assembly and support the hypothesis that this loss
69 lfils essential functions in the assembly of snRNPs, which are key components in the splicing of pre-
72 le of cells subjected to knockdown of Gro or snRNP-U1-C (a component of U1 snRNP) showed a significan
73 er tri-snRNP complex proteins, but not other snRNP spliceosome complexes, selectively abrogated growt
74 U2 small nuclear ribonucleoprotein particle (snRNP) are also subunits of the Spt-Ada-Gcn5 acetyltrans
75 U2 small nuclear ribonucleoprotein particle (snRNP) associates with U4/U6.U5 tri-snRNP through the U2
76 U2 small nuclear ribonucleoprotein particle (snRNP) complex, which assembles across the intron at the
79 and U2 small nuclear ribonucleic particles (snRNPs) and suggested that RBM20-dependent splicing repr
80 in the form of ribonucleoprotein particles (snRNPs) that are comprised of the U1 snRNA and 10 core c
81 2 small nuclear ribonucleoprotein particles (snRNPs), and transforms into a catalytically active spli
83 Gemin5 in small nuclear ribonucleic protein (snRNP) biogenesis as well as, potentially, other cellula
87 wed that U1 small nuclear ribonucleoprotein (snRNP) associates with RNAP II, and both RNAP II and U1
88 ccurs by U1 small nuclear ribonucleoprotein (snRNP) binding the 5' SS and recognition of the BS by th
92 and coilin/small nuclear ribonucleoprotein (snRNP) co-localization are significantly impaired in SH-
93 of the 7SK small nuclear ribonucleoprotein (snRNP) complex, is recruited to the promoters of Pol II-
96 the key U2 small nuclear ribonucleoprotein (snRNP) component SF3B1 (subunit 1 of the splicing factor
98 The 7SK small nuclear ribonucleoprotein (snRNP) plays a central role in RNA polymerase II elongat
99 nals and U1 small nuclear ribonucleoprotein (snRNP) recognition sites to be the most depleted and enr
100 The 7SK small nuclear ribonucleoprotein (snRNP) sequesters and inactivates the positive transcrip
101 in the 7SK small nuclear ribonucleoprotein (snRNP), which contains, additionally, 7SK snRNA, methyl
104 omposed of small nuclear ribonucleoproteins (snRNPs) and accessory proteins that excises introns from
109 RNA-protein complexes, including ribosomes, snRNPs, snoRNPs, telomerase, microRNAs, and long ncRNAs.
110 ated huge protein) and U7 small nuclear RNP (snRNP) are HLB components that participate in 3' process
113 ed the IFNalpha response to both anti-U1 RNP-snRNP complexes and anti-DNA-DNA complexes, but not to o
114 taining apoptotic cells, small nuclear RNPs (snRNPs), or DNA, or directly with TLR-7 and TLR-9 agonis
116 es (CBs), major NBs involved in spliceosomal snRNP assembly and their role in genome organization.
117 n orchestrating the assembly of spliceosomal snRNP particles and subsequently regulating the alternat
121 though mechanisms of P-TEFb release from the snRNP are becoming clearer, how P-TEFb remains in the 7S
123 nd that msk-null mutants are depleted of the snRNP assembly factor, survival motor neuron, and the Ca
125 y of PPM1G blocks P-TEFb reassembly onto the snRNP to sustain NF-kappaB-mediated Pol II transcription
128 construction of Saccharomyces cerevisiae tri-snRNP at 5.9 A resolution to reveal the essentially comp
129 e either reverses assembly by discarding tri-snRNP or proceeds to activation by irreversible U4 loss.
132 nd protrudes over the concave surface of tri-snRNP, where the U1 snRNP may reside before its release
134 he Prp8 and U1 snRNA interaction reduces tri-snRNP level in the spliceosome, suggesting a previously
136 0 can be successfully assembled into the tri-snRNP (albeit at a lower level than the WT Brr2) and the
137 e first time that PRPF6, a member of the tri-snRNP (small ribonucleoprotein) spliceosome complex, dri
138 rtant bridge between U4/U6 and U5 in the tri-snRNP and comparison with a Prp24-U6 snRNA recycling com
143 ure of Saccharomyces cerevisiae U4/U6.U5 tri-snRNP at 3.7 A resolution led to an essentially complete
144 s in assembly of the megaDalton U4/U6.U5 tri-snRNP complex, and lead to a dynamic model for U4/U6 pai
146 ron microscopy structure of the U4/U6.U5 tri-snRNP illustrates how proteins scaffold the RNA and dram
149 article (snRNP) associates with U4/U6.U5 tri-snRNP through the U2/U6 helix II and an interface betwee
150 n eukaryotes and is part of the U4/U6.U5 tri-snRNP, a large ribonucleoprotein complex that comprises
159 t this interaction between the galectin-3-U1 snRNP particle and the pre-mRNA results in a productive
160 ct can be reconstituted by the galectin-3-U1 snRNP particle, isolated by immunoprecipitation of the 1
161 hese results indicate that the galectin-3-U1 snRNP-pre-mRNA ternary complex is a functional E complex
163 0S particle that contained galectin-3 and U1 snRNP and this particle was sufficient to load the galec
164 ciates with RNAP II, and both RNAP II and U1 snRNP are also the most abundant factors associated with
165 flanking introns allowed normal U2AF and U1 snRNP binding to the target exon splice sites but blocke
168 mpletely disrupts the association between U1 snRNP and both FUS and RNAP II, but has no effect on the
170 election of 5'-splice site nucleotides by U1 snRNP is achieved predominantly through basepairing with
174 tes via formation of a complex comprising U1 snRNP bound at the 5' splice site (5'SS) and the Msl5*Mu
175 varying degrees and associated with core U1 snRNP proteins to a lesser extent than the canonical U1
177 g an essential canonical splicing factor (U1 snRNP) to this pathway provides strong new evidence that
178 Our findings underscore a wider role for U1 snRNP in splicing regulation and reveal a novel approach
179 factors transiently associate with human U1 snRNP and are not amenable for structural studies, while
181 essential subunits of the yeast and human U1 snRNP, respectively, that are implicated in the establis
185 further demonstrate that RBFOX2 increases U1 snRNP recruitment to the weak 5' splice site through dir
187 t that a U1-PAS axis characterized by low U1 snRNP recognition and a high density of PASs in the upst
188 roteins and U1 snRNA), but not the mature U1 snRNP-specific proteins (U1-70K, U1A and U1C), co-misloc
195 r antisense oligonucleotide inhibition of U1 snRNP increases the protein level of amyloid precursor p
196 of splicing proteins, and in the case of U1 snRNP we saw reciprocal changes in the levels of U1 snRN
198 down of Gro or snRNP-U1-C (a component of U1 snRNP) showed a significant overlap between genes regula
201 of these transcripts, suggesting that PSI-U1 snRNP interactions coordinate the behavioral network und
206 ing Gems, and motor neurons indicate that U1 snRNP is a component of a molecular pathway associated w
207 omplex is a functional E complex and that U1 snRNP is required to assemble galectin-3 onto an active
211 Here, we report that components of the U1 snRNP core particle (Sm proteins and U1 snRNA), but not
212 e concave surface of tri-snRNP, where the U1 snRNP may reside before its release from the pre-mRNA 5'
213 new synthetic genetic interactions of the U1 snRNP with Msl5 and Mud2 and with the nuclear cap-bindin
215 interaction between the pre-mRNA and the U1 snRNP, in which a short RNA duplex is established betwee
218 bserved with FUS, knockdown of any of the U1 snRNP-specific proteins results in a dramatic loss of SM
222 Thus, our results demonstrate unique U1 snRNP pathology and implicate abnormal RNA splicing in A
223 alectin-3 molecules not in a complex with U1 snRNP (fraction 1 of the same gradient), failed to resto
224 otein and RNA-protein interactions within U1 snRNP, and show how the 5' splice site of pre-mRNA is re
225 rroring yeast Prp42/Prp39, supports yeast U1 snRNP as a model for understanding how transiently assoc
226 , we report the cryoEM structure of yeast U1 snRNP at 3.6 A resolution with atomic models for ten cor
228 which is characterized by the presence of U1 snRNPs base-paired to the 5' splice site, components rec
229 methods to determine the stoichiometry of U1 snRNPs bound to pre-mRNA with one or two strong 5' splic
234 s indicate that endogenous RNA-containing U1-snRNP could be a signal that activates the NLRP3 inflamm
235 The U1-small nuclear ribonucleoprotein (U1-snRNP) that includes U1-small nuclear RNA is a highly co
240 are especially dependent on a functional U2 snRNP (small nuclear RNA [snRNA] plus associated protein
241 Pcbp1, and RBM39 stabilizes or increases U2 snRNP recruitment, enhances spliceosome A complex format
243 Notably, pharmacologic inhibition of U2 snRNP activity phenocopied PHF5A knockdown in GSCs and a
244 ior data showing that loss of function of U2 snRNP components can interfere with cell growth and indu
245 udemycin E interferes with the ability of U2 snRNP to maintain an H3K36me3 modification in actively t
247 nRNP, as H2A.Z loss results in persistent U2 snRNP association and decreased recruitment of downstrea
251 in facilitating interactions between the U2 snRNP complex and ATP-dependent helicases, we examined c
252 nked to interactions of alphaCPs with the U2 snRNP complex and may be mediated by cooperative interac
256 interface between U4/U6 di-snRNP and the U2 snRNP SF3b-containing domain, which also transiently con
258 n, the proteins U2AF35 and U2AF65 and the U2 snRNP, are able to recognize alternative candidate sites
259 spliceosomal rearrangements involving the U2 snRNP, as H2A.Z loss results in persistent U2 snRNP asso
265 shows extensive genetic interactions with U2 snRNP-associated proteins, and RNA sequencing (RNA-seq)
267 e expression of core components of U1 and U2 snRNPs, splicing regulators and other post-transcription
268 forms with stoichiometric association of U2 snRNPs and the U2 snRNA is base-paired to the pre-mRNA.
269 ion, the antibody to PRPF40A precipitated U2 snRNPs from nuclear extracts, indicating that PRPF40A as
271 Sudemycin E induces a dissociation of the U2 snRNPs and decreases their interaction with nucleosomes.
276 entosa assemble less efficiently with the U5 snRNP and bind more strongly to R2TP, with one mutant re
277 PRP31 regulates its interaction with the U5 snRNP component PRP8, which is required for the efficien
278 th RNA splicing regulators, including the U5 snRNP components of the spliceosome, such as EFTUD2.
279 actor PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a
285 ively, these data identify domains of the U6 snRNP that are critical for one of the first steps in as
286 exes (designated B(028)) revealed that U4/U6 snRNP proteins are released during activation before the
287 te post-transcriptional assembly of yeast U6 snRNP in vitro, and propose a model for U6 snRNP assembl
288 he post-transcriptional assembly of yeast U6 snRNP in vitro, which occurs through a complex series of
289 seems to be critical for retaining U5 and U6 snRNPs during/after spliceosomal activation through its
290 Thus, the HLB concentrates FLASH and U7 snRNP, promoting efficient histone mRNA biosynthesis and
291 at the 3' end by a complex that contains U7 snRNP, the FLICE-associated huge protein (FLASH) and his
292 actors are associated with the endogenous U7 snRNP and are recruited in a U7-dependent manner to hist
293 hat distinct domains of FLASH involved in U7 snRNP binding, histone pre-mRNA cleavage, and HLB locali
295 that failure to concentrate FLASH and/or U7 snRNP in the HLB impairs histone pre-mRNA processing.
297 LASH interacts with the N terminus of the U7 snRNP protein Lsm11, and together they recruit the HCC.
298 s, reveal an unexpected complexity of the U7 snRNP, and suggest that in animal cells polyadenylation
299 Previous studies indicated that vertebrate snRNP import requires importin-beta, the transport recep
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