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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzymeStructure of the human protein kinase CK2 catalytic subunit CK2α' and interaction thermodynamics with the regulatory subunit CK2βEnzymatic activity with an incomplete catalytic spine: insights from a comparative structural analysis of human CK2α and its paralogous isoform CK2α'A subnanomolar fluorescent probe for protein kinase CK2 interaction studiesStructural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunityA Note of Caution on the Role of Halogen Bonds for Protein Kinase/Inhibitor Recognition Suggested by High- And Low-Salt CK2α Complex StructuresCrystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 A resolution. An example of strong asymmetry between subunitsCrystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolutionCrystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.Primary and secondary interactions between CK2alpha and CK2beta lead to ring-like structures in the crystals of the CK2 holoenzyme.Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights.Structural Hypervariability of the Two Human Protein Kinase CK2 Catalytic Subunit Paralogs Revealed by Complex Structures with a Flavonol- and a Thieno[2,3-d]pyrimidine-Based Inhibitor.Structural basis of the constitutive activity of protein kinase CK2.Exploring the intramolecular phosphorylation sites in human Chk2.Biochemical characterization of CK2alpha and alpha' paralogues and their derived holoenzymes: evidence for the existence of a heterotrimeric CK2alpha'-holoenzyme forming trimeric complexes.Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis.Crystallization and preliminary crystallographic analysis of Arabidopsis thaliana EDS1, a key component of plant immunity, in complex with its signalling partner SAG101.Characterization of CK2 holoenzyme variants with regard to crystallization.Insights from soft X-rays: the chlorine and sulfur sub-structures of a CK2alpha/DRB complex.Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity.Biochemical characterization of the recombinant human Drosophila homologues Timekeeper and Andante involved in the Drosophila circadian oscillator.Purification and characterization of the CK2alpha'-based holoenzyme, an isozyme of CK2alpha: a comparative analysis.Unexpected Binding Mode of a Potent Indeno[1,2-b]indole-Type Inhibitor of Protein Kinase CK2 Revealed by Complex Structures with the Catalytic Subunit CK2α and Its Paralog CK2α'.A π-Halogen Bond of Dibenzofuranones with the Gatekeeper Phe113 in Human Protein Kinase CK2 Leads to Potent Tight Binding Inhibitors.Evidence for aggregation of protein kinase CK2 in the cell: a novel strategy for studying CK2 holoenzyme interaction by BRET(2).Development of a high-throughput screening-compatible assay to identify inhibitors of the CK2α/CK2β interaction.Protein kinase CK2: a catalyst for biology, medicine and structural biochemistry.The Structure of an Inverting GH43 β-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic ResiduesCrystallization and preliminary X-ray analysis of a family 51 glycoside hydrolase, the α-L-arabinofuranosidase fromGeobacillus stearothermophilusT-6Crystallization and preliminary characterization of crystals ofR-alcohol dehydrogenase fromLactobacillus brevisCrystallization, preliminary X-ray analysis of a native and selenomethionineD-hydantoinase fromThermusspExpression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea maysCrystallization and preliminary X-ray analysis of a hydantoinase from Artrobacter aurescens DSM 3745Crystallization and Preliminary Characterization of Crystals of d-2-hydroxyisocaproate Dehydrogenase from Lactobacillus caseiAn EDS1 heterodimer signalling surface enforces timely reprogramming of immunity genes in ArabidopsisCrystal structure of highly glycosylated human leukocyte elastase in complex with an S2' site binding inhibitorMutation of recombinant catalytic subunit alpha of the protein kinase CK2 that affects catalytic efficiency and specificityThe 'regulatory' beta-subunit of protein kinase CK2 negatively influences p53-mediated allosteric effects on Chk2 activationImproved protein-crystal identification by using 2,2,2-trichloroethanol as a fluorescence enhancer
P50
Q24291728-4021BDAE-83C7-46B6-A8E7-132699892282Q27666529-F919ED05-8E9D-45E4-B96A-5D02B739CA46Q27670730-D39A6949-7FB5-4751-BBE3-1ED7CB83A151Q27682639-A1E4FD2D-8102-4904-A661-FCB796853174Q27687934-1B52CC2F-3F21-4FD2-B1E7-ACD6DF8DC694Q27700826-B640B6D8-8AAC-4B1D-B01F-A7F9832C09F4Q27729824-9F3C5196-E7F2-4B78-9FB3-1921EC83A558Q27736799-9F0E472D-4095-4186-A183-271A816B527AQ34465858-754BC72D-D32E-440D-B7DD-DE6EC798371FQ36334422-FA3A0C55-7CAE-4CC6-99B3-BF8A31DB3427Q37456255-5C631D8D-FF9F-4150-97BC-C66604A2C131Q37731310-F6B1FAE3-06E5-49ED-9862-F8809E9A2754Q37805186-7C4397DC-C12B-48F8-999E-D1C2B405D995Q39936706-E419E4D4-A0B3-4C7C-84C6-3FB03F5CECB2Q39968855-B00A7D10-9B6C-4C98-9CA3-72C4C94ECAEAQ42001223-766E434D-BEAE-4DD6-A696-00C451894DEEQ42091338-F1C2F51F-1E81-477E-AEA2-09A2A439CFBAQ43876367-3DB61CD8-879A-4448-B082-B49377632A30Q44387770-434F6953-FF44-4C31-AD0F-23D92B73DF6EQ45290258-1E5E70B6-C405-4188-8CD7-D3BC303A3BF4Q46493049-C1441D37-5CDC-4A4F-92B7-0F7843ED0F84Q46840853-00F4FA76-D485-4132-902B-3F05FDBD2F90Q46915739-021F5E82-3B57-4EEF-AFD9-D7F580BCE864Q47162634-71A2B09C-1330-47E7-9DF7-EEEE1F0141B7Q49804565-4A7542BB-50DA-4011-9092-AC74CE3536BEQ51061573-5E24A22E-2415-4961-9122-3496B7A341DFQ54321258-793E3456-4927-4803-9E49-0F95A1F32249Q54574128-5C17261C-3D79-483E-B770-5F3D60D96DF3Q57013549-53C05441-5E43-4635-A472-7D8D15CCAF9FQ57013575-15FC955A-1A7E-4F75-8196-6033D4F7E025Q57013594-7BA83203-5CF4-485E-8DCC-931EB24BC231Q57013598-40B794B5-5EEF-4098-AD23-961A0C9ED7C0Q57013614-2C22DF9A-AE81-4BEB-93E2-1AF422AE98BAQ57013627-51FFFF7A-DC91-484A-BBAC-D29C9F94ED7DQ57013689-219AF02A-C4FA-465E-B3A5-91B4EA52C4C3Q61795890-0947528D-052C-435D-9EAB-B9AD73EEDD5FQ63471185-BBA838B1-DA52-4FE2-9EAE-151ADF41E97CQ73790241-2675F87A-9B0B-43D2-B4DD-4F0FD10DE36DQ81820554-8D655694-439B-4CFD-BC39-ABB5D4280E09Q88540582-9FCB835E-8D2A-48B8-8E99-0163F1B6F831
P50
description
onderzoeker
@nl
researcher ORCID: 0000-0002-0183-6315
@en
name
Karsten Niefind
@ast
Karsten Niefind
@en
Karsten Niefind
@es
Karsten Niefind
@nl
Karsten Niefind
@sl
type
label
Karsten Niefind
@ast
Karsten Niefind
@en
Karsten Niefind
@es
Karsten Niefind
@nl
Karsten Niefind
@sl
prefLabel
Karsten Niefind
@ast
Karsten Niefind
@en
Karsten Niefind
@es
Karsten Niefind
@nl
Karsten Niefind
@sl
P106
P21
P31
P496
0000-0002-0183-6315