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...

Πλήρης περιγραφή

Αποθηκεύτηκε σε:
Λεπτομέρειες βιβλιογραφικής εγγραφής
Τόπος έκδοσης:Sci Adv
Κύριοι συγγραφείς: 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
Μορφή: Artigo
Γλώσσα:Inglês
Έκδοση: American Association for the Advancement of Science 2020
Θέματα:
Research Articles
Διαθέσιμο Online: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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