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Proteostatic remodeling of small heat shock chaperones - crystallins by Ran-binding protein 2 and the peptidyl-prolyl <i>cis-trans</i> isomerase and chaperone activities of its cyclophilin domain

2024-01-30

Abstract excerpt

<h4>ABSTRACT</h4> Disturbances in phase transitions and intracellular partitions of nucleocytoplasmic shuttling substrates promote protein aggregation - a hallmark of neurodegenerative diseases. The modular Ran-binding protein 2 (Ranbp2) is a cytosolic molecular hub for rate-limiting steps of disassembly and phase transitions of Ran-GTP-bound protein ensembles exiting nuclear pores. Chaperones also play central r...

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Literature Corpus work
1c0fa4f8-838e-56ed-a225-586a3e395b76
DOI
10.1101/2024.01.26.577462
Open publication

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Proteostatic remodeling of small heat shock chaperones - crystallins by Ran-binding protein 2 and the peptidyl-prolyl <i>cis-trans</i> isomerase and chaperone activities of its cyclophilin domainDOI 10.1101/2024.01.26.577462
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