about
The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ionsHigh-resolution structural analysis of a novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducensStructures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: towards understanding the mechanism of the closure of the interdomain cleftStructures of complexes of octahaem cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens with sulfite and cyanideCovalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activityExpression, purification, crystallization and preliminary crystallographic analysis of a thermostable DNA ligase from the archaeonThermococcus sibiricusHigh-syn conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis MR-1 uridine phosphorylase in the free form and in complex with uridineElucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ionsConcerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzymeNADP-Dependent Aldehyde Dehydrogenase from Archaeon Pyrobaculum sp.1860: Structural and Functional Features.Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris.Site-directed mutagenesis of the base recognition loop of ribonuclease from Bacillus intermedius (binase).Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism.Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.Structural study of the X-ray-induced enzymatic reaction of octahaem cytochrome C nitrite reductase.Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties.Atomic Resolution Crystal Structure of NAD(+)-Dependent Formate Dehydrogenase from Bacterium Moraxella sp. C-1.Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens.Hepatitis C virus RNA-dependent RNA polymerase: study on the inhibition mechanism by pyrogallol derivatives.Substrate specificity of thymidine phosphorylase of E. coli: role of hydroxyl groups.Structure of native laccase from Trametes hirsuta at 1.8 A resolution.Chemoenzymatic synthesis of cytokinins from nucleosides: ribose as a blocking group.Purification, biochemical characterization, and structure of recombinant endo-1,4-β-xylanase XylE.Substrate specificity of Escherichia coli thymidine phosphorylase.Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducensStructure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyiDetermination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerasesMechanism of Ca2+-induced inhibition of Escherichia coli inorganic pyrophosphataseKey role of barstar Cys-40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstarComparative study of binase and barnase: experience in chimeric ribonucleasesPhysicochemical characterization of uridine phosphorylase from Shewanella oneidensis MR-1
P50
Q27638898-FDBA3412-92E7-4C21-A14D-892E97DF99EBQ27655236-A78C4B9C-4050-47B9-9A27-D389C4304B24Q27658478-866AED7C-FBCE-4683-8F2D-252C79AD4FEAQ27665006-32658D8E-8D41-4A00-A0DD-635E683C9634Q27676913-B510539E-5636-4263-BBC5-7871B95D6C98Q27677005-E6B4490B-2291-4ADE-B345-9ADDCB907F48Q27696322-0A5DFB51-8E54-41E1-A020-73ACDD8D11D3Q27700111-458F509D-1A88-4870-AAA5-DE0142BF1C0FQ27704052-6A1A89CF-9C1D-481E-9E4E-1E6758474C0CQ30354828-3197A077-E679-4D23-9E82-A3E2028473ABQ34328835-AA157B55-7F8C-4298-B6CA-78BA0E5A78CCQ38359067-A4D704D7-28B5-4948-8936-1180A99578DFQ38805051-4509FD8C-F6B9-487E-B28E-13344270214EQ40254725-989D0F94-E5DA-4E3E-9E48-C02CDDA7C827Q40971405-561B95C3-A9A4-4ACB-9874-8C3D06C5DB9BQ41766777-71F5463F-D362-4EE2-BE74-B31A24222BDBQ41870705-1AEE1A23-1AD0-44F3-B8C0-8BC2735B5591Q42949106-FF8DD19E-E4F2-4390-A9A3-7D4A98743DEDQ43031897-7DBB5C4C-44D2-4908-972F-12C9E42FF2CDQ46251542-C711AA51-3630-4E0B-A7CF-17FCB39292AAQ47734390-47411443-F86D-4813-B6F4-96BBB0DB91D5Q52665536-94AEFE38-DEB0-4F8A-AA67-647FCC2F0ED0Q54323391-5D8D45EE-314E-491D-9B88-9CE31FDA0E85Q54446514-5E82599F-473B-451B-B544-C40719CC774FQ57090941-47A5A0D6-F84A-4959-A6E9-2F637648ED46Q57463694-BA7FBAFA-53A6-412C-A228-0A274DE070E7Q73268387-776B1589-2A26-4952-8ACA-A077AA2900F9Q73598000-EF8FF59F-C795-4CEB-93E8-1413B8BAD82DQ74643821-632D9166-4D24-4886-906B-4F76D3F1067EQ77492360-0E35BD0B-030C-4B93-B187-22BAC9915B57Q87307974-BF9ED78F-13BB-422F-AEB0-150B67A41A6C
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0001-7718-4336
@en
name
Konstantin M Polyakov
@ast
Konstantin M Polyakov
@nl
Konstantin Michailowitsch Poljakow
@de
Konstantin Polyakov
@en
Константин Михайлович Поляков
@ru
type
label
Konstantin M Polyakov
@ast
Konstantin M Polyakov
@nl
Konstantin Michailowitsch Poljakow
@de
Konstantin Polyakov
@en
Константин Михайлович Поляков
@ru
altLabel
Konstantin M Polyakov
@en
Konstantin Mikhaylovich Polyakov
@en
Konstantin Poljakow
@de
prefLabel
Konstantin M Polyakov
@ast
Konstantin M Polyakov
@nl
Konstantin Michailowitsch Poljakow
@de
Konstantin Polyakov
@en
Константин Михайлович Поляков
@ru
P106
P21
P31
P496
0000-0001-7718-4336