about
Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factorsThe hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutantConformational control of the binding of diatomic gases to cytochrome c'GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of Streptomyces lividansComplexes of horseradish peroxidase with formate, acetate, and carbon monoxideTyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes.A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure.Carbon Monoxide Gas Is Not Inert, but Global, in Its Consequences for Bacterial Gene Expression, Iron Acquisition, and Antibiotic ResistanceTyrosyl radicals in dehaloperoxidase: how nature deals with evolving an oxygen-binding globin to a biologically relevant peroxidase.Structural and spectroscopic characterisation of a heme peroxidase from sorghum.Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.Engineered silver nanoparticles are sensed at the plasma membrane and dramatically modify the physiology of Arabidopsis thaliana plants.A new method of identifying the site of tyrosyl radicals in proteins.Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin.Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily.Differentiated, Promoter-specific Response of [4Fe-4S] NsrR DNA Binding to Reaction with Nitric Oxide.Reduction of Cu(II) by lipid hydroperoxides: implications for the copper-dependent oxidation of low-density lipoprotein.Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases.The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: an EPR studyMorphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein.Nitrite binding to globins: linkage isomerism, EPR silence and reductive chemistry.Arabidopsis root K+-efflux conductance activated by hydroxyl radicals: single-channel properties, genetic basis and involvement in stress-induced cell death.'Super-reduced' iron under physiologically-relevant conditions.Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine.An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins.Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin.[The decomposition of the EPR spectra of multicomponent systems irradiated at 77 K into paramagnetic center signals of different natures]The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase.Superoxide activates uncoupling proteins by generating carbon-centered radicals and initiating lipid peroxidation: studies using a mitochondria-targeted spin trap derived from alpha-phenyl-N-tert-butylnitrone.Endogenous superoxide production and the nitrite/nitrate ratio control the concentration of bioavailable free nitric oxide in leaves.Mitochondrial dysfunction in patients with severe sepsis: an EPR interrogation of individual respiratory chain components.EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. Models for intermediates in the alkaline transition.Tyrosyl radicals in proteins: a comparison of empirical and density functional calculated EPR parameters.[Ascorbic acid radicals induced by the action of radiation in tissues from rat organs frozen at 77 K]Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys-Tyr Cross-Link in the Galactose 6-Oxidase Homologue GlxA.On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide.The reactivity of heme in biological systems: autocatalytic formation of both tyrosine-heme and tryptophan-heme covalent links in a single protein architecture.Protein-template-driven formation of polynuclear iron species.Nitrosyl heme production compared in endotoxemic and hemorrhagic shock.
P50
Q23923171-C91865AC-2653-4472-80E3-B59799E8335CQ27686943-0ECDE708-68ED-459D-B381-7C69D06B574AQ27698551-2FE8331A-4EC4-47AD-908A-8A5D538A68E1Q27701617-41242D6F-0E13-4C39-8932-4A255DD42311Q28301858-A0B8CE05-B1CF-4A38-94E8-9B5BE6C3C68FQ30486705-946EC1D9-FB8C-4C6A-AD3A-48B0BD64E977Q34480651-2E78627F-410F-4DAA-9E36-C3E8779E341EQ37040059-8077EA6A-7693-46C8-B823-612358FD983FQ37311472-D7C75E71-4B79-4169-9B59-454CEB98EAF0Q38685389-2A2020AE-9E76-43C2-AB14-98C235F706ABQ39539276-7C4F684F-4C27-40E0-A2BA-FACD3913D697Q40202471-34F9D9C6-F8C0-4AB8-8606-9FD43F320075Q40288984-CD3FB337-07BD-42E6-BD2D-47D6E5AED02EQ40423605-24D309F4-C977-4D28-8593-6F9B685644D2Q40650309-966B2C58-9656-4F81-BECF-43AB7019C098Q41038753-83F4C628-8FB0-46CB-96D1-E08DA8395E21Q41209583-A2FD6769-F542-41BF-A55B-F9C27FDA721CQ41859943-9D8DEC01-C8A9-46A8-9C70-191926E216C9Q41896706-DE5D9C09-5600-4167-8A57-10C3B221AEF3Q42037950-70CD049B-89A8-4A58-91E5-872132B1F760Q42106108-2CA95840-EE92-40AB-B70A-581126854E69Q43055406-F7C7C422-6F2B-460B-AFBA-79BDD95A6212Q43106823-E95CF454-0176-48D1-883D-558DC0844A38Q43183297-A4F0C600-329A-4DCC-881A-A70A9C962B64Q43503212-52BE094E-4F9C-4AD4-A146-375455A5F3DEQ43570165-4CE4E51E-3C0A-4003-BF8D-85B555AB8170Q43842616-A246DA1D-F31F-4AE2-8F3B-1BEE3B4949C2Q44131231-2E45BDAC-B14E-4A60-B75C-96945762B412Q44577588-33704ADF-6829-4035-A659-FE2412E5B81CQ44583900-8257A9E0-AD8B-49B0-A46B-852052869D6FQ44824200-C4CC3EF0-8279-4AB3-8271-B698E9323CAEQ45015616-EF1B9A83-8AEE-4CCE-9B3A-2FCE7F1CDA20Q45210980-EFE84CA8-B9CA-4ABC-8438-39DB92DE6B3DQ45917221-5786821D-53D7-42B3-9DF5-9690CDEFC83CQ46187239-67463F14-A41C-4AB1-9662-D022CB9E3AE5Q46373113-B0FFF500-7F85-40E0-9BAD-56F699C58C25Q46761880-9B2009AD-78DF-4907-BAA5-3817E012DF22Q46933933-401E1C10-B9AD-4819-9A2A-43ABE12427F3Q47268766-357EAC6C-BAC3-4B6A-A633-CC5F27059A89Q47882389-FEE77FEC-55FD-4B53-BFB8-0603303BF368
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Dimitri A Svistunenko
@ast
Dimitri A Svistunenko
@en
Dimitri A Svistunenko
@es
Dimitri A Svistunenko
@nl
Dimitri A Svistunenko
@sl
type
label
Dimitri A Svistunenko
@ast
Dimitri A Svistunenko
@en
Dimitri A Svistunenko
@es
Dimitri A Svistunenko
@nl
Dimitri A Svistunenko
@sl
prefLabel
Dimitri A Svistunenko
@ast
Dimitri A Svistunenko
@en
Dimitri A Svistunenko
@es
Dimitri A Svistunenko
@nl
Dimitri A Svistunenko
@sl
P106
P1960
_ua480UAAAAJ
P2038
Dimitri_Svistunenko
P21
P31
P496
0000-0001-8060-2738