Evidence for disulfide interaction in situ between two adjacent proteins in mammalian 60-S ribosomal subunits
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference23 articles.
1. Specific unmasking of ribosomal proteins under the influence of chelating agents and increased ionic strength
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4. A site of reversible conformational alteration in rat liver ribosomes
5. Effects of aminoacridines and related compounds on the conformation of rat-liver ribosomes
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1. Selective high-efficiency cross-linking of mammalian ribosomal proteins with cleavable thiol-directed heterobifunctional reagents: Separation and identification of contact sequences of neighboring proteins after CNBr fragmentation;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1986-08
2. Selective high-efficiency cross-linking of mammalian ribosomal proteins with cleavable thiol-directed heterobifunctional reagents: Identification and binding directions of major protein complexes;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1986-08
3. A class of cleavable heterobifunctional reagents for thiol-directed high-efficiency protein crosslinking: Synthesis and application to the analysis of protein contact sites in mammalian ribosomes;Analytical Biochemistry;1986-06
4. Location of the sulfhydryl groups involved in disulfide interaction between the neighboring proteins L6 and L29 in mammalian ribosomes. S-cleavage of the cyanylated proteins in polyacrylamide gels after separation by dodecylsulfate gel electrophoresis;European Journal of Biochemistry;1984-08
5. Isolation of the contact regions of the neighboring mammalian ribosomal proteins L6 and L29. Cyanogen bromide cleavage of the disulfide complex after preparative electrophoresis in non-oxidative polyacrylamide gels;European Journal of Biochemistry;1984-04
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