Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis-Reference-Cited by-同舟云学术

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Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis

Published:2012-10-29 Issue:46 Volume:109 Page:18833-18838
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Nadler-Holly M.,Breker M.,Gruber R.,Azia A.,Gymrek M.,Eisenstein M.,Willison K. R.,Schuldiner M.,Horovitz A.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference33 articles.

1. Two Families of Chaperonin: Physiology and Mechanism

2. Chaperonins: two rings for folding

3. What distinguishes GroEL substrates from other Escherichia coli proteins?

4. A cytoplasmic chaperonin that catalyzes β-actin folding

5. TCP1 complex is a molecular chaperone in tubulin biogenesis

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