Protein Kinase CK2 Mutants Defective in Substrate Recognition
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Quinalizarin as a potent, selective and cell-permeable inhibitor of protein kinase CK2Structural features underlying the selectivity of the kinase inhibitors NBC and dNBC: role of a nitro group that discriminates between CK2 and DYRK1AHematopoietic lineage cell specific protein 1 associates with and down-regulates protein kinase CK2.The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.Phosphorylation-dependent kinase-substrate cross-linkingCystic fibrosis transmembrane regulator fragments with the Phe508 deletion exert a dual allosteric control over the master kinase CK2.Using bacteria to determine protein kinase specificity and predict target substratesThe Development of CK2 Inhibitors: From Traditional Pharmacology to in Silico Rational Drug Design.Involvement of asparagine 118 in the nucleotide specificity of the catalytic subunit of protein kinase CK2.Casein kinases as potential therapeutic targets.Protein kinase CK2 modulates HSJ1 function through phosphorylation of the UIM2 domain.Urolithin as a converging scaffold linking ellagic acid and coumarin analogues: design of potent protein kinase CK2 inhibitors.Aberrant signalling by protein kinase CK2 in imatinib-resistant chronic myeloid leukaemia cells: biochemical evidence and therapeutic perspectives.Establishing the stability and reversibility of protein pyrophosphorylation with synthetic peptides.De novo mutations in CSNK2A1 are associated with neurodevelopmental abnormalities and dysmorphic features.Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2').Unique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme.A novel splicing variant encoding putative catalytic alpha subunit of maize protein kinase CK2.Isolation of a CK2α subunit and the holoenzyme from the mussel Mytilus galloprovincialis and construction of the CK2α and CK2β cDNAs.Phosphorylation of cystic fibrosis transmembrane conductance regulator (CFTR) serine-511 by the combined action of tyrosine kinases and CK2: the implication of tyrosine-512 and phenylalanine-508.Ser/Thr phosphorylation of hematopoietic specific protein 1 (HS1)Unique features of HIV-1 Rev protein phosphorylation by protein kinase CK2 (‘casein kinase-2’)Basic Residues in the 74-83 and 191-198 Segments of Protein Kinase CK2 Catalytic Subunit are Implicated in Negative but not in Positive Regulation by the beta-SubunitTyrosineVersusSerine/Threonine Phosphorylation by Protein Kinase Casein Kinase-2
P2860
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P2860
Protein Kinase CK2 Mutants Defective in Substrate Recognition
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Mai 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в травні 1996
@uk
name
Protein Kinase CK2 Mutants Defective in Substrate Recognition
@en
Protein Kinase CK2 Mutants Defective in Substrate Recognition
@nl
type
label
Protein Kinase CK2 Mutants Defective in Substrate Recognition
@en
Protein Kinase CK2 Mutants Defective in Substrate Recognition
@nl
prefLabel
Protein Kinase CK2 Mutants Defective in Substrate Recognition
@en
Protein Kinase CK2 Mutants Defective in Substrate Recognition
@nl
P2093
P2860
P356
P1476
Protein kinase CK2 mutants def ...... ification and kinetic analysis
@en
P2093
P2860
P304
10595-10601
P356
10.1074/JBC.271.18.10595
P407
P577
1996-05-01T00:00:00Z