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The structure-function relationship of oncogenic LMTK3

Elucidating signaling driven by lemur tyrosine kinase 3 (LMTK3) could help drug development. Here, we solve the crystal structure of LMTK3 kinase domain to 2.1Å resolution, determine its consensus motif and phosphoproteome, unveiling in vitro and in vivo LMTK3 substrates. Via high-throughput homogen...

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Dades bibliogràfiques
Publicat a:Sci Adv
Autors principals: Ditsiou, Angeliki, Cilibrasi, Chiara, Simigdala, Nikiana, Papakyriakou, Athanasios, Milton-Harris, Leanne, Vella, Viviana, Nettleship, Joanne E., Lo, Jae Ho, Soni, Shivani, Smbatyan, Goar, Ntavelou, Panagiota, Gagliano, Teresa, Iachini, Maria Chiara, Khurshid, Sahir, Simon, Thomas, Zhou, Lihong, Hassell-Hart, Storm, Carter, Philip, Pearl, Laurence H., Owen, Robin L., Owens, Raymond J., Roe, S. Mark, Chayen, Naomi E., Lenz, Heinz-Josef, Spencer, John, Prodromou, Chrisostomos, Klinakis, Apostolos, Stebbing, Justin, Giamas, Georgios
Format: Artigo
Idioma:Inglês
Publicat: American Association for the Advancement of Science 2020
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC7673765/
https://ncbi.nlm.nih.gov/pubmed/33188023
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1126/sciadv.abc3099
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