Protein misfolding and disease

Progress in Biochemistry and Biophysics

Volumn 27, Issue 6, 2000, Pages 583-584

  Zhou, Jun Mei ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Disease; Prion; Protein misfolding; Quality control; Therapeutic agents

Indexed keywords

EID: 21944455864     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (31)

1. Ellgaard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science, 1999, 286 (5446): 1882-1888
2. Lindahl T, Wood R D. Quality control by DNA repair. Science, 1999, 286 (5446): 1897-1905
3. Ibba M, Soll D. Quality control mechanism during translation. Science, 1999, 286 (5446): 1893-1897
4. Wickner S, Maurizi M R, Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science, 1999, 286 (5446): 1888-1893
5. Teter S A, Houry W A, Ang D, et al. Polypeptide flux through bacterial HSP 70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell, 1999, 97: 755-765
6. Ewalt K A, Hendrick J P, Houry W A, et al. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell, 1997, 90: 491-500
7. Goldberg A L. Degradation of abnormal proteins in Escherichia coli. Proc Natl Acad Sci USA, 1972, 69: 422-426
8. Gottesman S, Maurizi M R. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol Rev, 1992, 56: 592-621
9. Deuerling E, Schulze-Specking A, Tomoyasu T, et al. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature, 1999, 400: 693-696
10. Beuron F, Maurizi M R, Belnap D M, et al. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J Struct Biol, 1998, 123: 248-259
11. Hiller M M, Finger A, Schweiger M, et al. ER Degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science, 1996, 273: 1725-1728
12. Hershko A, Ciechanover A. The ubiquitin system. Annu Rev Biochem, 1998, 67: 425-479
13. Gottesman S, Winkner S, Maurizi M R. Protein quality control: triage by chaperones and proteases. Genes Dev, 1997, 11: 815-823
14. Taubes G. Misfolding the way to disease. Science, 1996, 271 (5255): 1493-1495
15. Perrett S. Misshapes and misfits: protein misfolding and disease. Chemistry & Industry, 1998, 18: 389-393
16. Jackson G S, Hosszu L L P, Power A, et al. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformation. Science, 1999, 283 (5409): 1935-1937
17. Prusiner S B. Prion diseases and the BSE crisis. Science, 1998, 278 (5336): 245-251
18. Balter M. Prions: a lone killer or a vital accomplice? Science, 1999, 286 (5440): 660-662
19. Hardy J. The alzheimer family of diseases: many etiologies, one pathogenesis? Proc Natl Acad Sci USA, 1997, 94: 2095-2097
20. Selkoe D J. Alzheimer's disease: genotypes, phenotype, and treatments. Science, 1997, 275: 630-631
21. Vassar R. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science, 1999, 286: 735-741
22. Haass C, Strooper B D. The presenilins in Alzheimer's disease-proteolysis holds the key. Science, 1999, 286 (5441): 916-919
23. Spillantini M G. α-Synuclein in Lewy bodies. Nature, 1997, 388: 839-840
24. Polymeropoulos M H, Lavedent C, Leroy, E, et al. Mutation in the α4-Synuclein gene identified in families with Parkinson's disease. Science, 1997, 276: 2045-2047
25. Bullock A N, Henckel J, DeDecker B S, et al. Thermodynamic stability of wild-type and mutant p53 core domains. Proc Natl Acad Sci USA, 1997, 94: 14338-14342
26. Janciauskiene S, Carlemalm E, Eriksson S. In vitro amyloid fibril formation from alpha 1-antitrypsin. Biol Chem, 1995, 376: 103-109
27. Tagliavini F, McArthur R A, Canciani B, et al. Effectiveness of anthracycline against experimental prion disease in syrian hamsters. Science, 1997, 276 (5315): 1119-1121
28. Caughey B, Race R E. Potent inhibition of scrapie-associated PrP accumulation by congo red. J Neurochem, 1992, 59: 768-771
29. Ingrosso L, Ladogana A, Pocchiari M. Congo red prolongs the incubation period in scrapie-infected hamsters. J Virol, 1995, 69: 506-508
30. Foster B A, Coffey H A, Morin M J, et al. Pharmacological rescue of mutant p53 conformation and function. Science, 1999, 286 (5449): 2507-2510
31. Pennisi E. Bracing p53 for the war on cancer. Scenice, 1999, 286 (5449): 2431