Multiple associated proteins regulate proteasome structure and function.

By D. S. Leggett, John Hanna, A. Borodovsky, B. Crosas, M. Schmidt, R. Baker, Thomas Walz, Hidde L. Ploegh, D. Finley. Molecules and Cells, 2002

667 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/237495cb51d4a10986fb0c848fb11c7a06a50623

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Citations in the corpus

A cryptic protease couples deubiquitination and degradation by the proteasome (2002, background): “Ubp6/USP14 is a DUB of unknown specificity that can associate with the proteasom”
A Protein Complex Network of Drosophila melanogaster (2011, background): “Consistent with yeast and human proteasome studies (Leggett et al., 2002; Wang et al., 2007), Rpn11—a proteasomal lid subunit—pulled down the majority of the proteasome components.”
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “Thus, it appears that the deubiquitinating enzyme Ubp6 binds proteasomes via Rpn1 (82, 83), and the ubiquitin ligase Hul5 binds proteasomes through Rpn2 (84).”
Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “cerevisiae, leads to accelerated protein degradation (59, 145).”
Proteasomes and their kin: proteases in the machine age (2004, background): “However, mass spectrometry coupled with new affinity-based purification strategies, which enable the retention of weakly bound components, have allowed the identification of many proteasome-bound protein”
The Logic of the 26S Proteasome. (2017, positive): “…Hul5 suppresses the phenotypic effects of Ubp6 deletion, Hul5 was proposed to counter Ubp6’s actions in deubiquitinating conjugates on the 26S (Leggett et al., 2002), by functioning as an ‘‘E4,’’ which elongates Ub chains on the substrate and thereby prolongs its association with the…”
Negative Staining and Image Classification – Powerful Tools in Modern Electron Microscopy (2004, methodology): “cerevisiae proteasome was prepared as described in (11).”
Protein interaction networks from yeast to human. (2004, background): “One gene, KIAA0368, is uncharacterized in the human genome, belonging to ‘uncharacterized conserved protein family’ KOG0915, although the yeast ortholog Ecm29 has been suggested to tether the core particle to the regulatory particle [75].”
Breaking the chains: structure and function of the deubiquitinases (2009, background): “The yeast homologue of USP14, Ubp6, becomes ∼300-fold more active on binding to the base of the 19S lid of the proteasom”
Complete subunit architecture of the proteasome regulatory particle (2012, neutral): “Additional ubiquitin shuttle receptors (Rad23, Ddi1 and Dsk2) are recruited to the base through interactions with Rpn1, which also binds a second, non-essential DUB, Ubp6 (ref”