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Structure of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4 and characterization of its interaction with eIF4A

✍ Scribed by Waters, L C; Veverka, V; Böhm, M; Schmedt, T; Choong, P T; Muskett, F W; Klempnauer, K-H; Carr, M D


Book ID
110072302
Publisher
Nature Publishing Group
Year
2007
Tongue
English
Weight
319 KB
Volume
26
Category
Article
ISSN
0950-9232

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Structure of the APPL1 BAR-PH domain and
✍ Zhu, Guangyu (author);Chen, Jia (author);Liu, Jay (author);Brunzelle, Joseph S. 📂 Article 📅 2007 🏛 Nature Publishing Group 🌐 English ⚖ 433 KB

APPL1 is an effector of the small GTPase Rab5. Together, they mediate a signal transduction pathway initiated by ligand binding to cell surface receptors. Interaction with Rab5 is confined to the amino (N)-terminal region of APPL1. We report the crystal structures of human APPL1 N-terminal BAR-PH do