P Mitchell

Summary

Affiliation: University of Edinburgh
Country: UK

Publications

  1. ncbi request reprint Musing on the structural organization of the exosome complex
    P Mitchell
    Wellcome Trust Centre for Cell Biology, ICMB, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, UK
    Nat Struct Biol 7:843-6. 2000
  2. ncbi request reprint mRNA turnover
    P Mitchell
    Wellcome Trust Centre for Cell Biology, ICMB, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, UK
    Curr Opin Cell Biol 13:320-5. 2001
  3. ncbi request reprint An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3'-->5' degradation
    Philip Mitchell
    Wellcome Trust Centre for Cell Biology, Institute for Cell and Molecular Biology, King s Buildings, University of Edinburgh, EH9 3JR, United Kingdom
    Mol Cell 11:1405-13. 2003
  4. pmc Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs
    Philip Mitchell
    Wellcome Trust Centre for Cell Biology, Institute for Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom
    Mol Cell Biol 23:6982-92. 2003
  5. pmc Functions of the exosome in rRNA, snoRNA and snRNA synthesis
    C Allmang
    Institute of Cell and Molecular Biology, University of Edinburgh, Swann Building, King s Buildings, Edinburgh EH9 3JR, UK
    EMBO J 18:5399-410. 1999
  6. ncbi request reprint mRNA stability in eukaryotes
    P Mitchell
    Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh, EH9 3JR, UK
    Curr Opin Genet Dev 10:193-8. 2000

Collaborators

Detail Information

Publications6

  1. ncbi request reprint Musing on the structural organization of the exosome complex
    P Mitchell
    Wellcome Trust Centre for Cell Biology, ICMB, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, UK
    Nat Struct Biol 7:843-6. 2000
    ..As no detailed structural data are yet available for the exosome complex, or any of its constituent enzymes, this discussion will rely heavily on rather speculative models...
  2. ncbi request reprint mRNA turnover
    P Mitchell
    Wellcome Trust Centre for Cell Biology, ICMB, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, UK
    Curr Opin Cell Biol 13:320-5. 2001
    ..Competition for the cap structure links translation and subsequent mRNA degradation, which may also involve multiple deadenylases...
  3. ncbi request reprint An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3'-->5' degradation
    Philip Mitchell
    Wellcome Trust Centre for Cell Biology, Institute for Cell and Molecular Biology, King s Buildings, University of Edinburgh, EH9 3JR, United Kingdom
    Mol Cell 11:1405-13. 2003
    ..We conclude that recognition of NMD substrates by the Upf surveillance complex can target mRNAs to rapid deadenylation and exosome-mediated degradation...
  4. pmc Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs
    Philip Mitchell
    Wellcome Trust Centre for Cell Biology, Institute for Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom
    Mol Cell Biol 23:6982-92. 2003
    ..We propose that Rrp47p functions as a substrate-specific nuclear cofactor for exosome activity in the processing of stable RNAs...
  5. pmc Functions of the exosome in rRNA, snoRNA and snRNA synthesis
    C Allmang
    Institute of Cell and Molecular Biology, University of Edinburgh, Swann Building, King s Buildings, Edinburgh EH9 3JR, UK
    EMBO J 18:5399-410. 1999
    ..We conclude that the exosome is involved in the processing of many RNA substrates and that different components can have distinct functions...
  6. ncbi request reprint mRNA stability in eukaryotes
    P Mitchell
    Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh, EH9 3JR, UK
    Curr Opin Genet Dev 10:193-8. 2000
    ..In yeast, the relationship between translation and mRNA turnover is clearer, but the mRNA decapping process has turned out to be unexpectedly complex...