Splicing fidelity revisited

Charles C. Query, Maria M. Konarska

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Since the discovery of Prp16, a spliceosomal ATPase that alters the fidelity of splicing, many other ATPases associated with the spliceosome have been postulated to work similarly. The finding that Prp22, a DEAH-box ATPase, functions as a fidelity factor for the second step of splicing supports this hypothesis.

Original languageEnglish (US)
Pages (from-to)472-474
Number of pages3
JournalNature Structural and Molecular Biology
Volume13
Issue number6
DOIs
StatePublished - Jun 26 2006

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Adenosine Triphosphatases
Spliceosomes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Splicing fidelity revisited. / Query, Charles C.; Konarska, Maria M.

In: Nature Structural and Molecular Biology, Vol. 13, No. 6, 26.06.2006, p. 472-474.

Research output: Contribution to journalArticle

Query, Charles C. ; Konarska, Maria M. / Splicing fidelity revisited. In: Nature Structural and Molecular Biology. 2006 ; Vol. 13, No. 6. pp. 472-474.
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