Chaperones

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References

  1. Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem. 2013;82:323-55. doi: 10.1146/annurev-biochem-060208-092442. PMID:23746257 doi:http://dx.doi.org/10.1146/annurev-biochem-060208-092442
  2. Ellis J. Proteins as molecular chaperones. Nature. 1987 Jul 30-Aug 5;328(6129):378-9. PMID:3112578 doi:http://dx.doi.org/10.1038/328378a0
  3. Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature. 1988 Apr 28;332(6167):800-5. PMID:3282178 doi:http://dx.doi.org/10.1038/332800a0
  4. Halperin L, Jung J, Michalak M. The many functions of the endoplasmic reticulum chaperones and folding enzymes. IUBMB Life. 2014 May 19. doi: 10.1002/iub.1272. PMID:24839203 doi:http://dx.doi.org/10.1002/iub.1272
  5. Gurard-Levin ZA, Quivy JP, Almouzni G. Histone chaperones: assisting histone traffic and nucleosome dynamics. Annu Rev Biochem. 2014 Jun 2;83:487-517. doi:, 10.1146/annurev-biochem-060713-035536. PMID:24905786 doi:http://dx.doi.org/10.1146/annurev-biochem-060713-035536
  6. Misra G, Ramachandran R. Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity. Biophys Chem. 2009 Jun;142(1-3):55-64. doi: 10.1016/j.bpc.2009.03.006. Epub 2009 , Mar 16. PMID:19339102 doi:http://dx.doi.org/10.1016/j.bpc.2009.03.006
  7. Ramachandran R. Exploring the positional importance of aromatic residues and lysine in the interactions of peptides with the Plasmodium falciparum Hsp70-1. Biochim Biophys Acta. 2011 Mar;1814(3):457. doi: 10.1016/j.bbapap.2010.11.010. PMID:21316608 doi:http://dx.doi.org/10.1016/j.bbapap.2010.11.010
  8. Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem. 2013;82:323-55. doi: 10.1146/annurev-biochem-060208-092442. PMID:23746257 doi:http://dx.doi.org/10.1146/annurev-biochem-060208-092442
  9. Meriin AB, Sherman MY. Role of molecular chaperones in neurodegenerative disorders. Int J Hyperthermia. 2005 Aug;21(5):403-19. PMID:16048838 doi:http://dx.doi.org/10.1080/02656730500041871
  10. Winklhofer KF, Tatzelt J. The role of chaperones in Parkinson's disease and prion diseases. Handb Exp Pharmacol. 2006;(172):221-58. PMID:16610362
  11. Jain MR, Ge WW, Elkabes S, Li H. Amyotrophic lateral sclerosis: Protein chaperone dysfunction revealed by proteomic studies of animal models. Proteomics Clin Appl. 2008 May 1;2(5):670-684. PMID:19578526 doi:http://dx.doi.org/10.1002/prca.200780023
  12. Qi L, Zhang XD. Role of chaperone-mediated autophagy in degrading Huntington's disease-associated huntingtin protein. Acta Biochim Biophys Sin (Shanghai). 2014 Feb;46(2):83-91. doi:, 10.1093/abbs/gmt133. Epub 2013 Dec 8. PMID:24323530 doi:http://dx.doi.org/10.1093/abbs/gmt133
  13. Paulson H. Machado-Joseph disease/spinocerebellar ataxia type 3. Handb Clin Neurol. 2012;103:437-49. doi: 10.1016/B978-0-444-51892-7.00027-9. PMID:21827905 doi:http://dx.doi.org/10.1016/B978-0-444-51892-7.00027-9
  14. Bailey CK, Andriola IF, Kampinga HH, Merry DE. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum Mol Genet. 2002 Mar 1;11(5):515-23. doi: 10.1093/hmg/11.5.515. PMID:11875046 doi:http://dx.doi.org/10.1093/hmg/11.5.515
  15. Chaudhuri TK, Paul S. Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J. 2006 Apr;273(7):1331-49. PMID:16689923 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05181.x
  16. Ebrahimi-Fakhari D, Saidi LJ, Wahlster L. Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies. Acta Neuropathol Commun. 2013 Dec 5;1(1):79. doi: 10.1186/2051-5960-1-79. PMID:24314025 doi:http://dx.doi.org/10.1186/2051-5960-1-79

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