The lid that shapes the pot: structure and function of the chaperonin GroES
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference22 articles.
1. The crystal structure of the bacterial chaperonin GroEL at 2.8 å;Braig;Nature,1994
2. Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy;Chen;Nature,1994
3. How chaperonins tell wrong from right;Saibil;Nat. Struct. Biol,1994
4. Cooperativity in ATP hydrolysis by GroEL is increased by GroES;Gray;FEBS Lett,1991
5. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala;Yifrach;J. Mol. Biol,1994
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2. TEM and STEM-EDS evaluation of metal nanoparticle encapsulation in GroEL/GroES complexes according to the reaction mechanism of chaperonin;Microscopy;2020-11-11
3. Chaperonin—Co-chaperonin Interactions;Subcellular Biochemistry;2014-12-09
4. Urease inactivation by an unusual GroES chaperonin;Science China Chemistry;2014-02-20
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