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Sökning: WFRF:(Wahlestedt C) > Liang Z.

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1.
  • Katayama, S, et al. (författare)
  • Antisense transcription in the mammalian transcriptome
  • 2005
  • Ingår i: Science (New York, N.Y.). - : American Association for the Advancement of Science (AAAS). - 1095-9203 .- 0036-8075. ; 309:5740, s. 1564-1566
  • Tidskriftsartikel (refereegranskat)abstract
    • Antisense transcription (transcription from the opposite strand to a protein-coding or sense strand) has been ascribed roles in gene regulation involving degradation of the corresponding sense transcripts (RNA interference), as well as gene silencing at the chromatin level. Global transcriptome analysis provides evidence that a large proportion of the genome can produce transcripts from both strands, and that antisense transcripts commonly link neighboring “genes” in complex loci into chains of linked transcriptional units. Expression profiling reveals frequent concordant regulation of sense/antisense pairs. We present experimental evidence that perturbation of an antisense RNA can alter the expression of sense messenger RNAs, suggesting that antisense transcription contributes to control of transcriptional outputs in mammals.
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  • Thormeyer, D, et al. (författare)
  • Characterization of lacZ complementation deletions using membrane receptor dimerization
  • 2003
  • Ingår i: BioTechniques. - : Future Science Ltd. - 0736-6205 .- 1940-9818. ; 34:2, s. 346-
  • Tidskriftsartikel (refereegranskat)abstract
    • We describe the screening of lacZ deletions in mammalian cells and the discovery of a novel pair of lacZ deletions that can undergo α-complementation only when they are fused to peptides that interact with each other. The two lacZ deletions, ΔN 11-75 and ΔC 82-1023, were first characterized by fusing to two small interacting peptides and were then further analyzed by fusing to three membrane receptors (G protein-coupled receptors α2cAR and D2DRL and receptor tyrosine kinase insulin receptor) that were known to form homodimers in the membrane. Histochemical and quantitative FACS® assays demonstrated that the novel deletions have much lower level of association with each other, thus offering a much lower background in monitoring membrane protein interactions compared to previously published lacZ deletions. Furthermore, our method has the exciting potential to monitor simultaneously membrane receptor dimerization and localization to the cell surface of living cells.
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