Modulation of the Helicase Activity of eIF4A by eIF4B, eIF4H, and eIF4F
Open Access
- 1 August 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (33) , 30914-30922
- https://doi.org/10.1074/jbc.m100157200
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Further Characterization of the Helicase Activity of eIF4AJournal of Biological Chemistry, 2001
- The DEAD Box Protein eIF4A. 2. A Cycle of Nucleotide and RNA-Dependent Conformational ChangesBiochemistry, 1998
- The DEAD Box Protein eIF4A. 1. A Minimal Kinetic and Thermodynamic Framework Reveals Coupled Binding of RNA and NucleotideBiochemistry, 1998
- Kinetic Mechanism for the Sequential Binding of Two Single-Stranded Oligodeoxynucleotides to theEscherichia coliRep Helicase DimerBiochemistry, 1998
- Assays for Eukaryotic Translation Factors That Bind mRNAMethods, 1997
- Kinetic Measurement of the Step Size of DNA Unwinding by Escherichia coli UvrD HelicaseScience, 1997
- Improved Nearest-Neighbor Parameters for Predicting DNA Duplex StabilityBiochemistry, 1996
- Thermodynamic Parameters To Predict Stability of RNA/DNA Hybrid DuplexesBiochemistry, 1995
- Kinetics of Escherichia coli helicase II-catalyzed unwinding of fully duplex and nicked circular DNABiochemistry, 1993
- Dissociation of double stranded polynucleotide helical structures by eukaryotic initiation factors, as revealed by a novel assayBiochemistry, 1989