RNA location and modeling of a WD40 repeat domain within the vault.

@article{Kong2000RNALA,
  title={RNA location and modeling of a WD40 repeat domain within the vault.},
  author={Lawrence B. Kong and Amara C. Siva and Valerie A. Kickhoefer and Leonard H. Rome and Phoebe L. Stewart},
  journal={RNA},
  year={2000},
  volume={6 6},
  pages={
          890-900
        }
}
The vault complex is a ubiquitous 13-MDa ribonucleoprotein assembly, composed of three proteins (TEP1, 240 kDa; VPARP, 193 kDa; and MVP, 100 kDa) that are highly conserved in eukaryotes and an untranslated RNA (vRNA). The vault has been shown to affect multidrug resistance in cancer cells, and one particular component, MVP, is thought to play a role in the transport of drug from the nucleus. To locate the position of the vRNA, vaults were treated with RNases, and cryo-electron microscopy (cryo… 

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TLDR
It is shown that while TEP1 is a component of the vault particle, vaults have no detectable telomerase activity, suggesting that TEP 1 may play a common role in some aspect of ribonucleoprotein structure, function, or assembly.
The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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