| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871678 | FEBS Letters | 2011 | 7 Pages |
Abstract
⺠Fe65 directly interacts with the intracellular domains of LRP1 (LICD) and APP (AICD). ⺠Fe65/LICD interaction depends on tyrosine phosphorylation in the 2nd NPVY motif. ⺠Mutations of two Fe65 arginines impair complex formation with phosphorylated LICD. ⺠Fe65-PTB1 and Fe65-PTB2 are flexibly linked and can interact as independent modules.
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Authors
Wilfried Klug, Andreas Dietl, Bernd Simon, Irmgard Sinning, Klemens Wild,