ArticleMethods in enzymology2019
Engineered disulfide crosslinking to measure conformational changes in the 26S proteasome.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- Mapping Interaction of Assembly Factor Rpn14 With the Proteasome Base Reveals a Bipartite Interface and Implies Ordered Remodeling of Intersubunit Contacts During Proteasome Biogenesis.Journal of molecular biology · 2026Article
- Proteasomal conformation controls unfolding ability.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Proteasome subunit α1 overexpression preferentially drives canonical proteasome biogenesis and enhances stress tolerance in yeast.Scientific reports · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The 26S proteasome is a multisubunit ATP-dependent peptidase complex mediating most regulated protein degradation in eukaryotes. The proteasome undergoes several coordinated conformational changes during catalysis that activate it for substrate processing and functionally couple distinct enzymatic activities during substrate degradation. Understanding the impact of substrate interactions and individual ATP binding events on these conformational changes is currently a major bottleneck in the study of proteasome function. Here, we describe a simple biochemical reporter based on engineered disulfide crosslinking for measuring the conformational distribution of the Saccharomyces cerevisiae 26S proteasome. We demonstrate its use to investigate the impact of ATP analogs and proteasome inhibitors on proteasome conformational equilibria. This reporter allows simultaneous and rapid comparison of multiple treatments or conditions on the steady-state conformational distribution of the proteasome and can be readily extended to the study of other multisubunit complexes for which multiple conformational states are known at near-atomic resolution.
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Registered trials
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