CstF64: Cell Cycle Regulation and Functional Role in 3' End Processing of Replication-Dependent Histone mRNAs
出版年份 2014 全文链接
标题
CstF64: Cell Cycle Regulation and Functional Role in 3' End Processing of Replication-Dependent Histone mRNAs
作者
关键词
-
出版物
MOLECULAR AND CELLULAR BIOLOGY
Volume 34, Issue 23, Pages 4272-4284
出版商
American Society for Microbiology
发表日期
2014-09-30
DOI
10.1128/mcb.00791-14
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- CstF-64 supports pluripotency and regulates cell cycle progression in embryonic stem cells through histone 3′ end processing
- (2014) Bradford A. Youngblood et al. NUCLEIC ACIDS RESEARCH
- The human cap-binding complex is functionally connected to the nuclear RNA exosome
- (2013) Peter Refsing Andersen et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Polyadenylation site–induced decay of upstream transcripts enforces promoter directionality
- (2013) Evgenia Ntini et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- A Subset of Histone H2B Genes Produces Polyadenylated mRNAs under a Variety of Cellular Conditions
- (2013) Vijayalakshmi Kari et al. PLoS One
- Overlapping and distinct functions of CstF64 and CstF64 in mammalian mRNA 3' processing
- (2013) C. Yao et al. RNA
- Interaction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization
- (2012) Minyou Zhang et al. BIOCHEMISTRY
- A Complex Containing the CPSF73 Endonuclease and Other Polyadenylation Factors Associates with U7 snRNP and Is Recruited to Histone Pre-mRNA for 3'-End Processing
- (2012) X.-C. Yang et al. MOLECULAR AND CELLULAR BIOLOGY
- The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination
- (2012) N. Krishnan et al. MOLECULAR AND CELLULAR BIOLOGY
- Genome-wide Analysis of Pre-mRNA 3′ End Processing Reveals a Decisive Role of Human Cleavage Factor I in the Regulation of 3′ UTR Length
- (2012) Georges Martin et al. Cell Reports
- Drosophilahistone locus bodies form by hierarchical recruitment of components
- (2011) Anne E. White et al. JOURNAL OF CELL BIOLOGY
- FLASH Is Required for the Endonucleolytic Cleavage of Histone Pre-mRNAs but Is Dispensable for the 5' Exonucleolytic Degradation of the Downstream Cleavage Product
- (2011) X.-c. Yang et al. MOLECULAR AND CELLULAR BIOLOGY
- The PolyA tail length of yeast histone mRNAs varies during the cell cycle and is influenced by Sen1p and Rrp6p
- (2011) S. Beggs et al. NUCLEIC ACIDS RESEARCH
- Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure
- (2011) M. Moreno-Morcillo et al. RNA
- Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila
- (2011) B. D. Burch et al. RNA
- Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function
- (2010) Marc-David Ruepp et al. MOLECULAR BIOLOGY OF THE CELL
- The 68 kDa subunit of mammalian cleavage factor I interacts with the U7 small nuclear ribonucleoprotein and participates in 3′-end processing of animal histone mRNAs
- (2010) Marc-David Ruepp et al. NUCLEIC ACIDS RESEARCH
- Induced G1 cell-cycle arrest controls replication-dependent histone mRNA 3′ end processing through p21, NPAT and CDK9
- (2010) J Pirngruber et al. ONCOGENE
- CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 3′-end processing
- (2009) Judith Pirngruber et al. EMBO REPORTS
- A Core Complex of CPSF73, CPSF100, and Symplekin May Form Two Different Cleavage Factors for Processing of Poly(A) and Histone mRNAs
- (2009) Kelly D. Sullivan et al. MOLECULAR CELL
- FLASH, a Proapoptotic Protein Involved in Activation of Caspase-8, Is Essential for 3′ End Processing of Histone Pre-mRNAs
- (2009) Xiao-cui Yang et al. MOLECULAR CELL
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreDiscover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversation