Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta (Q24563795)

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S Caplan

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D Mertens

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G Hynes

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Z Pitluk

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Y Kashi

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K Harrison-Lavoie

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S Stevenson

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C Brown

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B Barrell

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

29 March 1994

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published in

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volume

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issue

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page(s)

2743-7

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cites work

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24 March 2017

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The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

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27 September 2017

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27 September 2017

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Random-clone strategy for genomic restriction mapping in yeast

27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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The Role of Tyrosine Protein Phosphorylation in Lymphocyte Activation

27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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30 May 2018

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30 May 2018

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30 May 2018

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Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

30 May 2018

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A cytoplasmic chaperonin that catalyzes beta-actin folding

30 May 2018

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Is yeast TCP1 a chaperonin?

30 May 2018

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Molecular chaperones: the plant connection

30 May 2018

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28 November 2018

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Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). I. Initial characterization

28 November 2018

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PubMed

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inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

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https://pubmed.ncbi.nlm.nih.gov/7908441