Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins-Reference-Cited by-同舟云学术

Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins

Published:2016-01 Issue: Volume:208 Page:68-75
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Ricci Caterina,Ortore Maria Grazia^ORCID,Vilasi Silvia,Carrotta Rita,Mangione Maria Rosalia,Bulone Donatella^ORCID,Librizzi Fabio,Spinozzi Francesco,Burgio Giosalba,Amenitsch Heinz,San Biagio Pier Luigi

Funder

MIUR

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference36 articles.

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4. Crystal structure of wild-type chaperonin GroEL;Bartolucci;J. Mol. Biol.,2005

5. ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin;Clare;Cell,2012

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5. Inhibition of Aβ1–42 Fibrillation by Chaperonins: Human Hsp60 Is a Stronger Inhibitor than Its Bacterial Homologue GroEL;ACS Chemical Neuroscience;2019-07-12