Now showing items 1-4 of 4

    • Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites. 

      Collette, JR; Fernández-Golbano, IM; Geli, MI; Giblin, JP; Grötsch, H; Idrissi, FZ; Lemmon, Sandra K; ... (9 authors) (EMBO J, 2010-09-01)
      Myosins-I are conserved proteins that bear an N-terminal motor head followed by a Tail Homology 1 (TH1) lipid-binding domain. Some myosins-I have an additional C-terminal extension (C(ext)) that promotes Arp2/3 complex-dependent ...
    • Domain-oriented edge-based alignment of protein interaction networks. 

      Guo, X; Hartemink, Alexander J (Bioinformatics, 2009-06-15)
      MOTIVATION: Recent advances in high-throughput experimental techniques have yielded a large amount of data on protein-protein interactions (PPIs). Since these interactions can be organized into networks, and since separate ...
    • DOMINE: a comprehensive collection of known and predicted domain-domain interactions. 

      Tasneem, Asba; Yellaboina, Sailu; Zaykin, Dmitri V; Raghavachari, Balaji; Jothi, Raja (Nucleic acids research, 2011-01)
      DOMINE is a comprehensive collection of known and predicted domain-domain interactions (DDIs) compiled from 15 different sources. The updated DOMINE includes 2285 new domain-domain interactions (DDIs) inferred from experimentally ...
    • Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain. 

      D'Andrea, AD; Kim, H; Wang, S; Wojtaszek, JL; Wu, Qinglin; Zhou, Pei (Nucleic Acids Res, 2014-12-16)
      FAAP20 is an integral component of the Fanconi anemia core complex that mediates the repair of DNA interstrand crosslinks. The ubiquitin-binding capacity of the FAAP20 UBZ is required for recruitment of the Fanconi anemia ...