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

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Chaperone-driven proteasome assembly.
    Author: Rosenzweig R, Glickman MH.
    Journal: Biochem Soc Trans; 2008 Oct; 36(Pt 5):807-12. PubMed ID: 18793141.
    Abstract:
    Assembly of the 34-subunit, 2.5 MDa 26S proteasome is a carefully choreographed intricate process. It starts with formation of a seven-membered alpha-ring that serves as a template for assembly of the complementary beta-ring-forming 'half-proteasomes'. Dimerization results in a latent 20S core particle that can serve further as a platform for 19S regulatory particle attachment and formation of the biologically active 26S proteasome for ubiquitin-dependent proteolysis. Both general and dedicated proteasome assembly chaperones regulate the efficiency and outcome of critical steps in proteasome biogenesis, and in complex association.
    [Abstract] [Full Text] [Related] [New Search]