Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871265 | FEBS Letters | 2012 | 6 Pages |
Abstract
⺠We modified tau by N-homocysteinylation (0.15, 1.5 and 15 mM). ⺠We found that 25 Lys residues are particularly susceptible to modification in the presence of 15 mM tHcy. ⺠Binding of tau to MTP is inhibited upon modification, depending on the degree of N-homocysteinylation. ⺠N-Hcy-tau species, compared to unmodified tau, change the assembly parameters, critical concentration and morphology of MTP.
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Authors
Oveis Karima, Gholamhossein Riazi, Sirus Khodadadi, Hassan Aryapour, Mohammad Ali Nasiri Khalili, Leila Yousefi, Ali Akbar Moosavi-Movahedi,