Chaperone protein ClpB

From Proteopedia

References

1. ↑ Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029
2. ↑ Wortmann SB, Wevers RA. CLPB Deficiency PMID:27891836
3. ↑ Wortmann SB, Zietkiewicz S, Kousi M, Szklarczyk R, Haack TB, Gersting SW, Muntau AC, Rakovic A, Renkema GH, Rodenburg RJ, Strom TM, Meitinger T, Rubio-Gozalbo ME, Chrusciel E, Distelmaier F, Golzio C, Jansen JH, van Karnebeek C, Lillquist Y, Lucke T, Ounap K, Zordania R, Yaplito-Lee J, van Bokhoven H, Spelbrink JN, Vaz FM, Pras-Raves M, Ploski R, Pronicka E, Klein C, Willemsen MA, de Brouwer AP, Prokisch H, Katsanis N, Wevers RA. CLPB mutations cause 3-methylglutaconic aciduria, progressive brain atrophy, intellectual disability, congenital neutropenia, cataracts, movement disorder. Am J Hum Genet. 2015 Feb 5;96(2):245-57. doi: 10.1016/j.ajhg.2014.12.013. Epub, 2015 Jan 15. PMID:25597510 doi:http://dx.doi.org/10.1016/j.ajhg.2014.12.013
4. ↑ Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell. 2003 Oct 17;115(2):229-40. PMID:14567920