Isolation of a peptide that inhibits the posttranslational arginylation of proteins in rat brain
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cellular and Molecular Neuroscience,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF02782502.pdf
Reference20 articles.
1. Bachmair A., Finley D., and Varshavsky A. (1986) In vivo half life of a protein is a function of its aminoterminal residue.Science 234, 179–234.
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3. Barra H. S., Rodriguez J. A., Arce C. A., and Caputto, R. (1973) A soluble preparation from rat brain that incorporates into its own proteins [14C] arginine by an RNase-sensitive system and [14C] tyrosine by an RNase-insensitive system.J. Neurochem. 20, 97–105.
4. Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding.Anal. Biochem. 72, 248–254.
5. Chakraborty G., and Nngoglia N. A. (1993) N-terminal arginylation and ubiquitin mediated proteolysis in nerve regeneration.Brain Res. Bull. 30, 439–445.
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2. Arginylation in a Partially Purified Fraction of 150k × g Supernatants of Axoplasm and Injured Vertebrate Nerves;Methods in Molecular Biology;2015
3. Posttranslational arginylation as a global biological regulator;Developmental Biology;2011-10
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