Characterization of the Region on Protein L7/L12 Involved in Binding to Ribosomal Particles
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1982.tb06974.x/fullpdf
Reference29 articles.
1. The Primary Structure of an Acidic Protein from 50-S Ribosomes of Escherichia coli which is Involved in GTP Hydrolysis Dependent on Elongation Factors G and T
2. 50-S Ribosomal Proteins. Purification and Partial Characterization of Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coli
3. Shape properties of proteins L7 and L12 from E. coli ribosomes
4. Small-angle X-ray scattering and crosslinking study of the proteins L7/L12 fromEscherichia coliribosomes
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1. Pivotal Role of the P1 N-terminal Domain in the Assembly of the Mammalian Ribosomal Stalk and in the Proteosynthetic Activity;Journal of Biological Chemistry;2001-01
2. A single-headed dimer of Escherichia coli ribosomal protein L7/L12 supports protein synthesis;Proceedings of the National Academy of Sciences;1998-04-14
3. Structure and Function of Escherichia Coli Ribosomal Protein L7/L12: Effect of Cross-Links and Deletions;The Translational Apparatus;1993
4. Structural and functional domains of Escherichia coli ribosomal protein L7/L12. The hinge region is required for activity.;Journal of Biological Chemistry;1993-01
5. The selective release of one of the two L7/L12 dimers from the Escherichia coli ribosome induced by a monoclonal antibody to the NH2-terminal region.;Journal of Biological Chemistry;1986-05
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