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Cryo-electron microscopy snapshots of the spliceosome: structural insights into a dynamic ribonucleoprotein machine

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NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 24, 期 10, 页码 791-799

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NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3463

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资金

  1. UK Medical Research Council [MC_U105184330]
  2. European Research Council [693087-SPLICE3D]
  3. EMBO
  4. Marie Sklodowska-Curie fellowships
  5. MRC [MC_U105184330] Funding Source: UKRI
  6. Medical Research Council [MC_U105184330] Funding Source: researchfish

向作者/读者索取更多资源

The spliceosome excises introns from pre-messenger RNAs using an RNA-based active site that is cradled by a dynamic protein scaffold. A recent revolution in cryo-electron microscopy (cryo-EM) has led to near-atomic-resolution structures of key spliceosome complexes that provide insight into the mechanism of activation, splice site positioning, catalysis, protein rearrangements and ATPase-mediated dynamics of the active site. The cryo-EM structures rationalize decades of observations from genetic and biochemical studies and provide a molecular framework for future functional studies.

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