Mycobacterial chaperonins: the tail wags the dog
Author:
Affiliation:
1. ImmunoBiology Limited; Babraham Research Campus Cambridge UK
2. The European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI); Hinxton Cambridge UK
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/350/1/20/19128360/350-1-20.pdf
Reference30 articles.
1. A novel nucleoid-associated protein of Mycobacterium tuberculosis is a sequence homolog of GroEL;Basu;Nucleic Acids Res,2009
2. Platensimycin activity against mycobacterial beta-ketoacyl-ACP synthases;Brown;PLoS ONE,2009
3. The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases;Canova;J Bacteriol,2009
4. Chaperonin nomenclature;Coates;Mol Microbiol,1993
5. The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function;Fan;Mol Microbiol,2012
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1. Beyond copper: examining the significance of His-mutations in mycobacterial GroEL1 HRCT for Ni(ii) complex stability and formation;Dalton Transactions;2024
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3. Mycobacterial chaperonins in cellular proteostasis: Evidence for chaperone function of Cpn60.1 and Cpn60.2‐mediated protein folding;Molecular Microbiology;2023-06-23
4. Histidine-Rich C-Terminal Tail of Mycobacterial GroEL1 and Its Copper Complex─The Impact of Point Mutations;Inorganic Chemistry;2023-04-24
5. Chaperonin: Co-chaperonin Interactions;Subcellular Biochemistry;2022-12-16
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