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Article

Structural basis for proteasome formation controlled by an assembly chaperone nas2.

Structure (London, England : 1993) - 6 May 2014

Satoh Tadashi, Saeki Yasushi, Hiromoto Takeshi, Wang Ying-Hui, Uekusa Yoshinori, Yagi Hirokazu, Yoshihara Hidehito, Yagi-Utsumi Maho, Mizushima Tsunehiro, Tanaka Keiji, Kato Koichi

Abstract excerpt

Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized...

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Share to Adenosine Triphosphatases
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 24685148
DOI: 10.1016/j.str.2014.02.014

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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