Hypothesis: A combination of modifying factors induces misfolding and dysfunction of selected proteins in vivo

Progress in Biochemistry and Biophysics

Volumn 33, Issue 10, 2006, Pages 940-941

  He, Rong Qiao ^a   Chen, Lan ^a   Perrett, Sarah ^a   Wang, Chih Chen ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Combinative protein modification; Neurodegenerative diseases; Protein misfolding; Selective misfolding

Indexed keywords

EID: 33846332770     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (20)

1. Zhou J M. Prog Biochem Biophys, 2004, 31 (2): 95-105
2. Landrieu I, Lacosse L, Leroy A, et al. NMR analysis of a Tau phosphorylation pattern. J Am Chem Soc, 2006, 128 (11): 3575-3583
3. Phiel C J, Wilson C A, Lee V M, et al. GSK-3α regulates production of Alzheimer's disease amyloid-β peptides. Nature, 2003, 423 (6938): 435-439
4. Mitra N, Sinha S, Ramya T N, et al. N-linked oligosaccharides as outfitters for glycoprotein folding, form and function. Trends Biochem Sci., 2006, 31 (3): 156-163
5. Niemela O. Distribution of ethanol-induced protein adducts in vivo: relationship to tissue injury. Free Radic Biol Med, 2001, 31(12): 1533-1538
6. Chen F, David D, Ferrari A, et al. Posttranslational modifications of tau-role in human tauopathies and modeling in transgenic animals. Curr Drug Targets, 2004, 5 (6): 503-515
7. Kurono Y, Ichioka K, Ikeda K. Kinetics of the rapid modification of human serum albumin with trinitrobenzenesulfonate and localization of its site. J Pharm Sci, 1983, 72 (4): 432-435
8. Iberg N, Fluckiger R. Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites. Cell, 1986, 261 (29): 13542-13545
9. Gu W, Roeder R G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. J Pharm Sci, 1997, 90 (4): 595-606
10. Li M, Luo J, Brooks C L, et al. Acetylation of p53 inhibits its ubiquitination by Mdm2. J Biol Chem, 2002, 277 (52): 50607-50611
11. Schwartz D C, Hochstrasser M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci, 2003, 28 (6): 321-328
12. Barrett D M, Black S M, Todor H, et al. Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation. J Biol Chem, 2005, 280 (15): 14453-14461
13. Hess D T, Matsumoto A, Kim S O, et al. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol, 2005, 6 (2): 150-166
14. O'Brian C A, Chu F. Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission. Free Radic Res, 2005, 39 (5): 471-480
15. Dei R, Takeda A, Niwa H, et al. Lipid peroxidation and advanced glycation end products in the brain in normal aging and in Alzheimer's disease. Acta neuropathol (Berl), 2002, 104 (2): 113-122
16. Robertson L A, Moya K L, Breen K C. The potential role of tau protein O-glycosylation in Alzheimer's disease. J Alzheimers Dis, 2004, 6 (5): 489-495
17. Necula M, Kuret J. Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro. J Biol Chem, 2004, 279 (48): 49694-49703
18. Liu F, Iqbal K, Grundke-Iqbal I, et al. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc Natl Acad Sci USA, 2004, 101 (29): 10804-10809
19. Brooks C L, Gu W. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr Opin Cell Biol, 2003, 15 (2): 164-171
20. Hodara R, Norris E H, Giasson B I, et al. Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation. J Biol Chem, 2004, 279 (46): 47746-47753