Accurate cleavage and polyadenylation of exogenous RNA substrate
about
The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factorMultiple forms of poly(A) polymerases in human cellsGenetic complementation in the Xenopus oocyte: co-expression of sea urchin histone and U7 RNAs restores 3' processing of H3 pre-mRNA in the oocyteA novel endoribonuclease cleaves at a priming site of mouse mitochondrial DNA replicationA CPSF-73 homologue is required for cell cycle progression but not cell growth and interacts with a protein having features of CPSF-100Cleavage and polyadenylation factor CPF specifically interacts with the pre-mRNA 3' processing signal AAUAAAAssembly of a processive messenger RNA polyadenylation complexElements upstream of the AAUAAA within the human immunodeficiency virus polyadenylation signal are required for efficient polyadenylation in vitroCharacterization of cleavage and polyadenylation specificity factor and cloning of its 100-kilodalton subunitRNA-binding protein HuR autoregulates its expression by promoting alternative polyadenylation site usageCloning of cDNAs encoding the 160 kDa subunit of the bovine cleavage and polyadenylation specificity factorFunctional analysis of the sea urchin U7 small nuclear RNAFive subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I.Fip1 regulates the activity of Poly(A) polymerase through multiple interactions.Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor.A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonucleaseThe mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradationFormation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesisA multicomponent complex is required for the AAUAAA-dependent cross-linking of a 64-kilodalton protein to polyadenylation substratesStructurally diverse low molecular weight activators of the mammalian pre-mRNA 3' cleavage reactionDelineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Nucleophosmin is selectively deposited on mRNA during polyadenylation.Downstream sequence elements with different affinities for the hnRNP H/H' protein influence the processing efficiency of mammalian polyadenylation signalsHeterogeneity in mammalian RNA 3' end formation.Mutational analysis of a yeast transcriptional terminator.Generation of histone mRNA 3' ends by endonucleolytic cleavage of the pre-mRNA in a snRNP-dependent in vitro reaction.Cleavage and polyadenylation of messenger RNA precursors in vitro occurs within large and specific 3' processing complexes.Activation of HIV-1 pre-mRNA 3' processing in vitro requires both an upstream element and TAR.SL1 trans splicing and 3'-end formation in a novel class of Caenorhabditis elegans operon.RNA polymerase III defects suppress a conditional-lethal poly(A) polymerase mutation in Saccharomyces cerevisiae.Coupled RNA polymerase II transcription and 3' end formation with yeast whole-cell extracts.Ending the message: poly(A) signals then and nowFunctional importance of conserved nucleotides at the histone RNA 3' processing siteIsolation and characterization of polyadenylation complexes assembled in vitro.A poly(A) addition site and a downstream termination region are required for efficient cessation of transcription by RNA polymerase II in the mouse beta maj-globin gene.Fractionation of HeLa cell nuclear extracts reveals minor small nuclear ribonucleoprotein particlesHeat-labile regulatory factor is required for 3' processing of histone precursor mRNAs.Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism.The G-rich auxiliary downstream element has distinct sequence and position requirements and mediates efficient 3' end pre-mRNA processing through a trans-acting factor.Cleavage site determinants in the mammalian polyadenylation signal
P2860
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P2860
Accurate cleavage and polyadenylation of exogenous RNA substrate
description
1985 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1985
@ast
im Juli 1985 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1985/07/01)
@sk
vědecký článek publikovaný v roce 1985
@cs
wetenschappelijk artikel (gepubliceerd op 1985/07/01)
@nl
наукова стаття, опублікована в липні 1985
@uk
مقالة علمية (نشرت في يوليو 1985)
@ar
name
Accurate cleavage and polyadenylation of exogenous RNA substrate
@ast
Accurate cleavage and polyadenylation of exogenous RNA substrate
@en
Accurate cleavage and polyadenylation of exogenous RNA substrate
@nl
type
label
Accurate cleavage and polyadenylation of exogenous RNA substrate
@ast
Accurate cleavage and polyadenylation of exogenous RNA substrate
@en
Accurate cleavage and polyadenylation of exogenous RNA substrate
@nl
prefLabel
Accurate cleavage and polyadenylation of exogenous RNA substrate
@ast
Accurate cleavage and polyadenylation of exogenous RNA substrate
@en
Accurate cleavage and polyadenylation of exogenous RNA substrate
@nl
P1433
P1476
Accurate cleavage and polyadenylation of exogenous RNA substrate
@en
P2093
C. L. Moore
P. A. Sharp
P304
P356
10.1016/S0092-8674(85)80065-9
P407
P577
1985-07-01T00:00:00Z