Area of research
Molecular Biology · Cell Biology
Research interest
Research focused on Kinase and Casein kinase 2, with related work in Protein subunit, Cancer, Cell biology. Notable publications include 'Protein kinase CK2: a potential therapeutic target for diverse human diseases', 'Re-evaluation of protein kinase CK2 pleiotropy: new insights provided by a phosphoproteomics analysis of CK2 knockout cells', and 'Role of CK2 inhibitor CX-4945 in anti-cancer combination therapy – potential clinical relevance'.
Targeting the E1 ubiquitin-activating enzyme (UBA1) improves elexacaftor/tezacaftor/ivacaftor efficacy towards F508del and rare misfolded CFTR mutants
Protein kinase CK2: a potential therapeutic target for diverse human diseases
Targeting CK2 in cancer: a valuable strategy or a waste of time?
How can a traffic light properly work if it is always green? The paradox of CK2 signaling
Role of CK2 inhibitor CX-4945 in anti-cancer combination therapy – potential clinical relevance
“Janus” efficacy of CX-5011: CK2 inhibition and methuosis induction by independent mechanisms
Activity of CK2α protein kinase is required for efficient replication of some HPV types
Protein Kinase CK2 Subunits Differentially Perturb the Adhesion and Migration of GN11 Cells: A Model of Immature Migrating Neurons
The protein kinase CK2 contributes to the malignant phenotype of cholangiocarcinoma cells
A Journey through the Cytoskeleton with Protein Kinase CK2
Dependence of HSP27 cellular level on protein kinase CK2 discloses novel therapeutic strategies
Re-evaluation of protein kinase CK2 pleiotropy: new insights provided by a phosphoproteomics analysis of CK2 knockout cells
Generation and quantitative proteomics analysis of CK2α/α’(−/−) cells
Exploring the CK2 Paradox: Restless, Dangerous, Dispensable
Polo-like kinase 2 modulates α-synuclein protein levels by regulating its mRNA production
Design, validation and efficacy of bisubstrate inhibitors specifically affecting ecto-CK2 kinase activity
Quantitative analysis of a phosphoproteome readily altered by the protein kinase CK2 inhibitor quinalizarin in HEK-293T cells
Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants