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Article

Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells.

Traffic (Copenhagen, Denmark) - 1 Jan 2008

Tkach Johnny M, Glover John R

Abstract excerpt

Hsp104 is a molecular chaperone in yeast that restores solubility and activity to inactivated proteins after severe heat shock. We investigated the mechanisms that influence Hsp104 subcellular distribution in both unstressed and heat-shocked cells. In unstressed cells, Hsp104 and a green fluorescent protein-Hsp104 fusion protein were detected in both the nucleus and the cytoplasm. We demonstrate that a...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 17973656
DOI: 10.1111/j.1600-0854.2007.00666.x

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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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