A comparative study of the characteristics of eIF-2 and eIF-2-ancillary factor activities from yeast Saccharomyces cerevisiae and rabbit reticulocytes.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Purification and properties of eukaryotic initiation factor 2 and its ancillary protein factor (Co-eIF-2A) from yeast Saccharomyces cerevisiae.
2. Protein synthesis in rabbit reticulocytes XXI. Purification and properties of a protein factor (Co-EIF-1) which stimulates Met-tRNAf binding to EIF-1.
3. Protein synthesis in rabbit reticulocytes. Demonstration of the requirements for eIF-2 and Co-eIF-2A for peptide chain initiation using immune sera.
4. Protein synthesis in rabbit reticulocytes. A study of the mechanism of interreaction of fluorescently labeled co-eIF-2A with eIF-2 using fluorescence polarization.
5. Protein synthesis in rabbit reticulocytes. Co-eIF-2A reverses mRNA inhibition of ternary complex (Met-tRNAf.eIF-2.GTP) formation by eIF-2.
Cited by 14 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Minimum Requirements for the Function of Eukaryotic Translation Initiation Factor 2;Genetics;2001-05-01
2. Biochemical Analysis of the eIF2βγ Complex Reveals a Structural Function for eIF2α in Catalyzed Nucleotide Exchange;Journal of Biological Chemistry;2001-01
3. Purification and Kinetic Analysis of eIF2B fromSaccharomyces cerevisiae;Journal of Biological Chemistry;2000-08
4. The highly acidic C-terminal region of the yeast initiation factor subunit 2 α (eIF-2 α) contains casein kinase phosphorylation sites and is essential for maintaining normal regulation of GCN4;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1995-04
5. The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon;Molecular and Cellular Biology;1992-01
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