Investigation on PLK2 and PLK3 substrate recognition. | Biochim Biophys Acta;1824(12): 1366-73, 2012 Dec. | MEDLINE

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Investigation on PLK2 and PLK3 substrate recognition.

Salvi, M; Trashi, E; Cozza, G; Franchin, C; Arrigoni, G; Pinna, L A.

Affiliation

Salvi M; Department of Biomedical Sciences, University of Padova, Italy. mauro.salvi@unipd.it

Biochim Biophys Acta ; 1824(12): 1366-73, 2012 Dec.

Article in En | MEDLINE | ID: mdl-22828320

Subject(s)

Protein Serine-Threonine Kinases/metabolism; Amino Acid Sequence; Cells, Cultured; Humans; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Phosphorylation; Protein Interaction Domains and Motifs; Structural Homology, Protein; Substrate Specificity; Tumor Suppressor Proteins

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Serine-Threonine Kinases Limits: Humans Language: En Journal: Biochim Biophys Acta Year: 2012 Type: Article Affiliation country: Italy

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Serine-Threonine Kinases Limits: Humans Language: En Journal: Biochim Biophys Acta Year: 2012 Type: Article Affiliation country: Italy