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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Cleavage stimulation factor, 3' pre-RNA, subunit 2, 64kDa

CstF-64, Cstf2
This gene encodes a nuclear protein with an RRM (RNA recognition motif) domain. The protein is a member of the cleavage stimulation factor (CSTF) complex that is involved in the 3' end cleavage and polyadenylation of pre-mRNAs. Specifically, this protein binds GU-rich elements within the 3'-untranslated region of mRNAs. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on CstF-64
Characterization of a cleavage stimulation factor, 3' pre-RNA, subunit 2, 64 kDa (CSTF2) as a therapeutic target for lung cancer.
GeneRIF
Daigo et al., Tokyo, Japan. In Clin Cancer Res, 2011
CSTF2 is likely to play an important role in lung carcinogenesis and be a prognostic biomarker in the clinic.
Interactions of CstF-64, CstF-77, and symplekin: implications on localisation and function.
GeneRIF
Schümperli et al., Bern, Switzerland. In Mol Biol Cell, 2011
nuclear accumulation of CstF-64 depends on binding to CstF-77 not symplekin; interaction between CstF-64/CstF-64Tau and CstF-77 are important for maintenance of nuclear levels of CstF complex components and intracellular localization, stability, function
The hinge domain of the cleavage stimulation factor protein CstF-64 is essential for CstF-77 interaction, nuclear localization, and polyadenylation.
GeneRIF
MacDonald et al., Lubbock, United States. In J Biol Chem, 2010
The Hinge domain is necessary for CstF-64 interaction with CstF-77 and consequent nuclear localization.
Transcription elongation factor ELL2 directs immunoglobulin secretion in plasma cells by stimulating altered RNA processing.
Impact
GeneRIF
Milcarek et al., Pittsburgh, United States. In Nat Immunol, 2009
ELL2 and CstF-64 tracked together with RNA polymerase II across the Igh mu- and gamma-gene segments
Characterization of Rous sarcoma virus polyadenylation site use in vitro.
GeneRIF
McNally et al., Milwaukee, United States. In Virology, 2008
The inactivity of the RSV poly(A) site was at least in part due to poor CstF binding since tethering CstF to the RSV substrate activated polyadenylation.
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