Mária Deák - Concepedia

Concepedia

Author

Mária Deák

MRC Protein Phosphorylation and Ubiquitylation Unit

Also Known As

D.M.F. Van Aalten, M Deak, M. Deak, M. Deák, Maria DEAK, Maria Deak, Maria Deák, Mária Deák, Mária Deák

117

Publications

17.7K

Citations

69

H-Index

122

Concepts

All Affiliations

MRC Protein Phosphorylation and Ubiquitylation Unit University of Dundee École Polytechnique Fédérale de Lausanne Nestlé (Switzerland)Hungarian Academy of Sciences

MD

About

Mária Deák is an author at MRC Protein Phosphorylation and Ubiquitylation Unit specializing in medicine, cell signaling, and signal transduction.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	48	57	10.5K
2	Natural Sciences	38	43	6.9K
3	Biochemistry	24	27	4.7K
4	Engineering	7	7	982
5	Health Sciences	2	2	97

Mária Deák

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99

Publications

17.7K

Citations

69

H-Index

	Year	Citations
LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1 José M. Lizcano, Olga Göransson, Rachel Toth, The EMBO Journal	2004	1.4K
Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activationofCREB Mária Deák The EMBO Journal Stress-activated Protein Kinase-1Molecular PhysiologySignal TransductionSignaling PathwayNutrient Signalling	1998	981
PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65 Chandana Kondapalli, Agne Kazlauskaite, Ning Zhang, Open Biology MitophagyMolecular BiologyInsect Pink1Synaptic SignalingOxidative Stress	2012	922
3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase Dario R. Alessi, Mária Deák, Antonio Casamayor, Current Biology Protein FunctionSignal TransductionSignaling Pathway3-Phosphoinositide-dependent Protein Kinase-1Cellular Biochemistry	1997	743
Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities Simon DOWLER, A Currie, David G. CAMPBELL, Biochemical Journal	2000	518
LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity Mahaboobi Jaleel, R. Jeremy Nichols, Mária Deák, Biochemical Journal MitophagyMolecular BiologySignaling PathwayLrrk2 ActivityAutophagy	2007	510
The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases Alberto C. Vitari, Mária Deák, Nick Morrice, Biochemical Journal	2005	496
Identification of Protor as a novel Rictor-binding component of mTOR complex-2 Laura R. Pearce, Xu Huang, Jérôme Boudeau, Biochemical Journal	2007	447
PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2 Anudharan Balendran, Antonio Casamayor, Mária Deák, Current Biology Signal TransductionBiochemistryCarboxyl TerminusNatural SciencesPdk2 Activity	1999	441
14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization R. Jeremy Nichols, Nicolas Dzamko, Nicholas A. Morrice, Biochemical Journal Neurodegenerative DiseasesMitophagySignal Transduction14-3-3 BindingSignaling Pathway	2010	397

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