These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: The synthesis and proteasomal degradation of a model substrate Ub5DHFR.
    Author: Lam YA, Huang JW, Showole O.
    Journal: Methods Enzymol; 2005; 398():379-90. PubMed ID: 16275344.
    Abstract:
    The importance of substrate polyubiquitination in protein degradation has been established for many years. However, the many intricacies of substrate recognition and ubiquitination by E3 enzymes have greatly limited access to degradable substrate in vitro. Thus, detailed analysis of protein degradation using purified 26S proteasomes has been difficult. The ability to synthesize polyubiquitin chains in a test tube has provided a method to make large quantities of a specific polyubiquitinated substrate, Ub(5)DHFR. This chapter focuses on the synthesis and degradation of this model substrate.
    [Abstract] [Full Text] [Related] [New Search]