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August 15, 1994Genes & DevelopmentOpen Access

The prespliceosome components SAP 49 and SAP 145 interact in a complex implicated in tethering U2 snRNP to the branch site.

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Authors

PCPatrick Champion-ArnaudBoston Children's HospitalRRRobin ReedHarvard University

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Cite This Study

Champion-Arnaud et al. (1994) studied this question.

synapsesocial.com/papers/6a9134dc9cd0eb66ad33f38fhttps://doi.org/10.1101/gad.8.16.1974
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Interaction of Mammalian Splicing Factor SF3a with U2 snRNP and Relation of Its 60-kD Subunit to Yeast PRP91993 · 151 citations
  2. 2Small Nuclear Ribonucleoprotein (RNP) U2 Contains Numerous Additional Proteins and Has a Bipartite RNP Structure Under Splicing Conditions1993 · 118 citations
  3. 3Presplicing complex formation requires two proteins and U2 snRNP.1988 · 113 citations
  4. 4A compensatory base change in human U2 snRNA can suppress a branch site mutation.1989 · 290 citations
  5. 5The U5 and U6 Small Nuclear RNAs as Active Site Components of the Spliceosome1993 · 352 citations