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PUBMED FOR HANDHELDS

Journal Abstract Search


521 related items for PubMed ID: 15226427

  • 1. Identification of cis elements directing termination of yeast nonpolyadenylated snoRNA transcripts.
    Carroll KL, Pradhan DA, Granek JA, Clarke ND, Corden JL.
    Mol Cell Biol; 2004 Jul; 24(14):6241-52. PubMed ID: 15226427
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  • 2. Ssu72 protein mediates both poly(A)-coupled and poly(A)-independent termination of RNA polymerase II transcription.
    Steinmetz EJ, Brow DA.
    Mol Cell Biol; 2003 Sep; 23(18):6339-49. PubMed ID: 12944462
    [Abstract] [Full Text] [Related]

  • 3. Transcriptome-wide binding sites for components of the Saccharomyces cerevisiae non-poly(A) termination pathway: Nrd1, Nab3, and Sen1.
    Creamer TJ, Darby MM, Jamonnak N, Schaughency P, Hao H, Wheelan SJ, Corden JL.
    PLoS Genet; 2011 Oct; 7(10):e1002329. PubMed ID: 22028667
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  • 4. Interaction of yeast RNA-binding proteins Nrd1 and Nab3 with RNA polymerase II terminator elements.
    Carroll KL, Ghirlando R, Ames JM, Corden JL.
    RNA; 2007 Mar; 13(3):361-73. PubMed ID: 17237360
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  • 5. Polyadenylation linked to transcription termination directs the processing of snoRNA precursors in yeast.
    Grzechnik P, Kufel J.
    Mol Cell; 2008 Oct 24; 32(2):247-58. PubMed ID: 18951092
    [Abstract] [Full Text] [Related]

  • 6. Regulation of yeast NRD1 expression by premature transcription termination.
    Arigo JT, Carroll KL, Ames JM, Corden JL.
    Mol Cell; 2006 Mar 03; 21(5):641-51. PubMed ID: 16507362
    [Abstract] [Full Text] [Related]

  • 7. A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation.
    Sheldon KE, Mauger DM, Arndt KM.
    Mol Cell; 2005 Oct 28; 20(2):225-36. PubMed ID: 16246725
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  • 8. Yeast Nrd1, Nab3, and Sen1 transcriptome-wide binding maps suggest multiple roles in post-transcriptional RNA processing.
    Jamonnak N, Creamer TJ, Darby MM, Schaughency P, Wheelan SJ, Corden JL.
    RNA; 2011 Nov 28; 17(11):2011-25. PubMed ID: 21954178
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  • 11. A network of interdependent molecular interactions describes a higher order Nrd1-Nab3 complex involved in yeast transcription termination.
    Loya TJ, O'Rourke TW, Degtyareva N, Reines D.
    J Biol Chem; 2013 Nov 22; 288(47):34158-34167. PubMed ID: 24100036
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  • 12. The RNA polymerase II C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome.
    Heo DH, Yoo I, Kong J, Lidschreiber M, Mayer A, Choi BY, Hahn Y, Cramer P, Buratowski S, Kim M.
    J Biol Chem; 2013 Dec 20; 288(51):36676-90. PubMed ID: 24196955
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  • 13. A yeast heterogeneous nuclear ribonucleoprotein complex associated with RNA polymerase II.
    Conrad NK, Wilson SM, Steinmetz EJ, Patturajan M, Brow DA, Swanson MS, Corden JL.
    Genetics; 2000 Feb 20; 154(2):557-71. PubMed ID: 10655211
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  • 14. Distinct pathways for snoRNA and mRNA termination.
    Kim M, Vasiljeva L, Rando OJ, Zhelkovsky A, Moore C, Buratowski S.
    Mol Cell; 2006 Dec 08; 24(5):723-734. PubMed ID: 17157255
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  • 17. Pti1p and Ref2p found in association with the mRNA 3' end formation complex direct snoRNA maturation.
    Dheur S, Vo le TA, Voisinet-Hakil F, Minet M, Schmitter JM, Lacroute F, Wyers F, Minvielle-Sebastia L.
    EMBO J; 2003 Jun 02; 22(11):2831-40. PubMed ID: 12773397
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  • 18. Control of pre-mRNA accumulation by the essential yeast protein Nrd1 requires high-affinity transcript binding and a domain implicated in RNA polymerase II association.
    Steinmetz EJ, Brow DA.
    Proc Natl Acad Sci U S A; 1998 Jun 09; 95(12):6699-704. PubMed ID: 9618475
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  • 19. The Nrd1-Nab3-Sen1 termination complex interacts with the Ser5-phosphorylated RNA polymerase II C-terminal domain.
    Vasiljeva L, Kim M, Mutschler H, Buratowski S, Meinhart A.
    Nat Struct Mol Biol; 2008 Aug 09; 15(8):795-804. PubMed ID: 18660819
    [Abstract] [Full Text] [Related]

  • 20. Yeast RNA-Binding Protein Nab3 Regulates Genes Involved in Nitrogen Metabolism.
    Merran J, Corden JL.
    Mol Cell Biol; 2017 Sep 15; 37(18):. PubMed ID: 28674185
    [Abstract] [Full Text] [Related]


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