Modulation of RNA Condensation by the DEAD-Box Protein eIF4A
- 9 January 2020
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 180 (3), 411-426.e16
- https://doi.org/10.1016/j.cell.2019.12.031
Abstract
No abstract availableKeywords
Funding Information
- Howard Hughes Medical Institute
- National Institutes of Health
- National Institutes of Health
- Canadian Institutes of Health Research
This publication has 97 references indexed in Scilit:
- Fiji: an open-source platform for biological-image analysisNature Methods, 2012
- Dimerization of oskar 3′ UTRs promotes hitchhiking for RNA localization in the Drosophila oocyteRNA, 2011
- The DEAD-Box Protein Ded1 Modulates Translation by the Formation and Resolution of an eIF4F-mRNA ComplexMolecular Cell, 2011
- The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1Genes & Development, 2011
- The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1Journal of Bone and Joint Surgery, 2011
- ParaspecklesCold Spring Harbor Perspectives in Biology, 2010
- ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwindingProceedings of the National Academy of Sciences of the United States of America, 2008
- Recruitment of the RNA Helicase RHAU to Stress Granules via a Unique RNA-binding DomainJournal of Biological Chemistry, 2008
- Targeting of Aberrant mRNAs to Cytoplasmic Processing BodiesCell, 2006
- Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4ANature Chemical Biology, 2006