Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10763047 | Biochemical and Biophysical Research Communications | 2011 | 6 Pages |
Abstract
⺠MAL has a bipartite NLS that binds to Impα in an extended conformation. ⺠Mutational analyses verified the functional significance of MAL-Impα interactions. ⺠Induced folding and NLS-masking by G-actins inhibit nuclear import of MAL.
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Authors
Hidemi Hirano, Yoshiyuki Matsuura,