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Article

Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48.

Scientific reports - 14 Jul 2017

Esaki Masatoshi, Islam Md Tanvir, Tani Naoki, Ogura Teru

Abstract excerpt

Yeast Cdc48 is a well-conserved, essential chaperone of ATPases associated with diverse cellular activity (AAA) proteins, which recognizes substrate proteins and modulates their conformations to carry out many cellular processes. However, the fundamental mechanisms underlying the diverse pivotal roles of Cdc48 remain unknown. Almost all AAA proteins form a ring-shaped structure with a conserved aromatic amino...

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Share to Adenosine Triphosphatases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28710470
DOI: 10.1038/s41598-017-05806-y
PMCID: PMC5511170

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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