VIAF

Virtual International Authority File

Search

Leader 00000nz a2200037n 45 0
001 WKP|Q47928733 (VIAF cluster) (Authority/Source Record)
003 WKP
005 20241120235922.0
008 241120nneanz||abbn n and d
035 ‎‡a (WKP)Q47928733‏
024 ‎‡a 0000-0002-3754-6459‏ ‎‡2 orcid‏
024 ‎‡a 7402934380‏ ‎‡2 scopus‏
035 ‎‡a (OCoLC)Q47928733‏
100 0 ‎‡a David L. Turner‏ ‎‡9 es‏ ‎‡9 sl‏ ‎‡9 ast‏
375 ‎‡a 1‏ ‎‡2 iso5218‏
400 0 ‎‡a ডেভিড এল টার্নার‏ ‎‡c গবেষক‏ ‎‡9 bn‏
400 0 ‎‡a David L. Turner‏ ‎‡c British Portuguese chemist‏ ‎‡9 en‏
400 0 ‎‡a David L. Turner‏ ‎‡c onderzoeker‏ ‎‡9 nl‏
670 ‎‡a Author's 13 C and proton NMR studies of horse cytochrome c‏
670 ‎‡a Author's 13 C-NMR studies of horse ferrocytochrome c‏
670 ‎‡a Author's 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states‏
670 ‎‡a Author's 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c‏
670 ‎‡a Author's A difference method for the reduction of “auto” peaks in autocorrelation spectra‏
670 ‎‡a Author's A New Pathway for Mannitol Metabolism in Yeasts Suggests a Link to the Evolution of Alcoholic Fermentation‏
670 ‎‡a Author's An approach to understanding conformational mobility in peptides and proteins‏
670 ‎‡a Author's An integrated view of redox and catalytic properties of B-type PpDyP from Pseudomonas putida MET94 and its distal variants‏
670 ‎‡a Author's An unusual conformation of the methionine haem ligand in cytochrome cL established by two-dimensional 1H-NMR‏
670 ‎‡a Author's Assignment of the redox potentials to the four haems in Desulfovibrio vulgaris cytochrome c 3 by 2D-NMR‏
670 ‎‡a Author's Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein‏
670 ‎‡a Author's Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure‏
670 ‎‡a Author's Carbon flux analysis by 13C nuclear magnetic resonance to determine the effect of CO2 on anaerobic succinate production by Corynebacterium glutamicum‏
670 ‎‡a Author's Characterization of the haem environment in Methylophilus methylotrophus ferricytochrome c "by 1H-NMR.‏
670 ‎‡a Author's Characterization of the improved sensitivity obtained using a flow method for oxygenating and mixing cell suspensions in NMR‏
670 ‎‡a Author's Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome‏
670 ‎‡a Author's Constrained peptide analogues of transforming growth factor-alpha residues cysteine 21-32 are mitogenically active. Use of proline mimetics to enhance biological potency.‏
670 ‎‡a Author's Crystallization and preliminary X-ray characterization of cytochrome c "from the obligate methylotroph Methylophilus methylotrophus‏
670 ‎‡a Author's Determination of Haem Electronic Structure in Cytochrome b5 and Metcyanomyoglobin‏
670 ‎‡a Author's Determination of the magnetic properties and orientation of the heme axial ligands of PpcA from Geobacter metallireducens by paramagnetic NMR‏
670 ‎‡a Author's Determination of the orientation of the axial ligands and of the magnetic properties of the haems in the tetrahaem ferricytochrome from Shewanella frigidimarina‏
670 ‎‡a Author's Distance dependence of interactions between charged centres in proteins with common structural features‏
670 ‎‡a Author's Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus‏
670 ‎‡a Author's Evaluation of 13C and 1H Fermi contact shifts in horse cytochrome c. The origin of the anti-Curie effect‏
670 ‎‡a Author's Four quartets. Application to two-dimensional NMR‏
670 ‎‡a Author's Functional and Mechanistic Studies of Cytochromec3fromDesulfovibrio gigas: Thermodynamics of a “Proton Thruster” †‏
670 ‎‡a Author's Functional properties of type I and type II cytochromes c3 from Desulfovibrio africanus‏
670 ‎‡a Author's High Yield of Methylophilus methylotrophus Cytochrome c″ by Coexpression with Cytochrome c Maturation Gene Cluster from Escherichia coli‏
670 ‎‡a Author's Highly Selective Ligand Binding byMethylophilus methylotrophusCytochromec′′‏
670 ‎‡a Author's Homotropic and heterotropic cooperativity in the tetrahaem cytochrome c3 from Desulfovibrio vulgaris‏
670 ‎‡a Author's Homotropic and heterotropic interactions in cytochromes c‏
670 ‎‡a Author's Homotropic and heterotropic interactions in cytochromes c(3) from sulphate reducing bacteria‏
670 ‎‡a Author's Involvement of a labile axial histidine in coupling electron and proton transfer in Methylophilus methylotrophus cytochrome c "‏
670 ‎‡a Author's Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motions‏
670 ‎‡a Author's Metabolic and transcriptional analysis of acid stress in Lactococcus lactis, with a focus on the kinetics of lactic acid pools‏
670 ‎‡a Author's Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins.‏
670 ‎‡a Author's Paramagnetic NMR shifts in cyanoferricytochrome c‏
670 ‎‡a Author's pH Dependence of Structural and Functional Properties of Oxidized Cytochromec "fromMethylophilus methylotrophus‏
670 ‎‡a Author's Pitfalls in assigning heme axial coordination by EPR‏
670 ‎‡a Author's Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR.‏
670 ‎‡a Author's Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.‏
670 ‎‡a Author's Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances‏
670 ‎‡a Author's Redox- and pH-linked conformational changes in triheme cytochrome PpcA from Geobacter sulfurreducens‏
670 ‎‡a Author's Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.‏
670 ‎‡a Author's Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774‏
670 ‎‡a Author's Relationship between protein stabilization and protein rigidification induced by mannosylglycerate‏
670 ‎‡a Author's Relative importance of driving force and electrostatic interactions in the reduction of multihaem cytochromes by small molecules‏
670 ‎‡a Author's Replacement of the methionine axial ligand in cytochrome c‏
670 ‎‡a Author's Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure‏
670 ‎‡a Author's Revision of the haem-core architecture in the tetraheam cytochrome c from Desulfovibrio baculatus by two-dimensional 1H NMR‏
670 ‎‡a Author's Solution structure and dynamics of the outer membrane cytochrome OmcF from Geobacter sulfurreducens‏
670 ‎‡a Author's Solution structure of a mutant of the triheme cytochrome PpcA from Geobacter sulfurreducens sheds light on the role of the conserved aromatic residue F15‏
670 ‎‡a Author's Solution structure of Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3: structural basis for functional cooperativity‏
670 ‎‡a Author's Solution structure of plantaricin C, a novel lantibiotic.‏
670 ‎‡a Author's Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor‏
670 ‎‡a Author's Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris‏
670 ‎‡a Author's Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity‏
670 ‎‡a Author's Stereospecificity of Corynebacterium glutamicum 2,3-butanediol dehydrogenase and implications for the stereochemical purity of bioproduced 2,3-butanediol‏
670 ‎‡a Author's Structural and functional characterization of cytochrome c 3 from D. desulfuricans ATCC 27774 by 1 H-NMR‏
670 ‎‡a Author's Structural determinants of protein stabilization by solutes. The important of the hairpin loop in rubredoxins.‏
670 ‎‡a Author's Structural evidence for a proton transfer pathway coupled with haem reduction of cytochrome c″ from Methylophilus methylotrophus‏
670 ‎‡a Author's Structural studies of Desulfovibrio vulgaris ferrocytochrome c3 by two-dimensional NMR‏
670 ‎‡a Author's Structure-function relationship in type II cytochrome c‏
670 ‎‡a Author's Structure-function relationship in type II cytochrome c(3) from Desulfovibrio africanus: a novel function in a familiar heme core‏
670 ‎‡a Author's Structure of Escherichia coli Flavodiiron Nitric Oxide Reductase‏
670 ‎‡a Author's Symmetry and Phase-Selected NMR Spectra of Liquid Crystalline Samples‏
670 ‎‡a Author's Synthesis, conformational properties, and antibody recognition of peptides containing beta-turn mimetics based on alpha-alkylproline derivatives‏
670 ‎‡a Author's The Conformation of the Monensin-A-Sodium Complex in Solution Determined from Self-consistent NOE Distance Constraints‏
670 ‎‡a Author's The lactate dehydrogenases encoded by the ldh and ldhB genes in Lactococcus lactis exhibit distinct regulation and catalytic properties - comparative modeling to probe the molecular basis‏
670 ‎‡a Author's The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif‏
670 ‎‡a Author's Thermodynamic and kinetic characterisation of individual haems in multicentre cytochromes c3‏
670 ‎‡a Author's Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans‏
670 ‎‡a Author's Thermodynamic and kinetic characterization of two methyl-accepting chemotaxis heme sensors from Geobacter sulfurreducens reveals the structural origin of their functional difference‏
670 ‎‡a Author's Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3.‏
670 ‎‡a Author's Tuning of functional heme reduction potentials in Shewanella fumarate reductases‏
670 ‎‡a Author's Two‐dimensional J spectroscopy: Proton‐coupled carbon‐13 NMR‏
670 ‎‡a Author's Two-dimensional NMR studies of electron transfer in cytochrome c3‏
670 ‎‡a Author's Two-dimensional nuclear magnetic resonance of paramagnetic metalloproteins.‏
909 ‎‡a (orcid) 0000000237546459‏ ‎‡9 1‏
909 ‎‡a (scopus) 7402934380‏ ‎‡9 1‏
919 ‎‡a solutionstructureofdesulfovibriovulgarishildenboroughferrocytochromec3structuralbasisforfunctionalcooperativity‏ ‎‡A Solution structure of Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3: structural basis for functional cooperativity‏ ‎‡9 1‏
919 ‎‡a solutionstructureofplantaricin100anovellantibiotic‏ ‎‡A Solution structure of plantaricin C, a novel lantibiotic.‏ ‎‡9 1‏
919 ‎‡a solutionstructureofthemegftgfalpha4450chimericgrowthfactor‏ ‎‡A Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor‏ ‎‡9 1‏
919 ‎‡a solutionstructuresoftetrahaemferricytochromec3fromdesulfovibriovulgaris‏ ‎‡A Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris‏ ‎‡9 1‏
919 ‎‡a solutionstructuresoftetrahaemferricytochromec3fromdesulfovibriovulgarishildenboroughanditsk45qmutantthemolecularbasisofcooperativity‏ ‎‡A Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity‏ ‎‡9 1‏
919 ‎‡a stereospecificityofcorynebacteriumglutamicum23butanedioldehydrogenaseandimplicationsforthestereochemicalpurityofbioproduced23butanediol‏ ‎‡A Stereospecificity of Corynebacterium glutamicum 2,3-butanediol dehydrogenase and implications for the stereochemical purity of bioproduced 2,3-butanediol‏ ‎‡9 1‏
919 ‎‡a structuralandfunctionalcharacterizationofcytochrome1003from500desulfuricansatcc27774by1hnmr‏ ‎‡A Structural and functional characterization of cytochrome c 3 from D. desulfuricans ATCC 27774 by 1 H-NMR‏ ‎‡9 1‏
919 ‎‡a structuraldeterminantsofproteinstabilizationbysolutestheimportantofthehairpinloopinrubredoxins‏ ‎‡A Structural determinants of protein stabilization by solutes. The important of the hairpin loop in rubredoxins.‏ ‎‡9 1‏
919 ‎‡a structuralevidenceforaprotontransferpathwaycoupledwithhaemreductionofcytochrome100frommethylophilusmethylotrophus‏ ‎‡A Structural evidence for a proton transfer pathway coupled with haem reduction of cytochrome c″ from Methylophilus methylotrophus‏ ‎‡9 1‏
919 ‎‡a structuralstudiesofdesulfovibriovulgarisferrocytochromec3by2dimensionalnmr‏ ‎‡A Structural studies of Desulfovibrio vulgaris ferrocytochrome c3 by two-dimensional NMR‏ ‎‡9 1‏
919 ‎‡a structurefunctionrelationshipintype2cytochrome100‏ ‎‡A Structure-function relationship in type II cytochrome c‏ ‎‡9 1‏
919 ‎‡a structurefunctionrelationshipintype2cytochrome1003fromdesulfovibrioafricanusanovelfunctioninafamiliarhemecore‏ ‎‡A Structure-function relationship in type II cytochrome c(3) from Desulfovibrio africanus: a novel function in a familiar heme core‏ ‎‡9 1‏
919 ‎‡a structureofescherichiacoliflavodiironnitricoxidereductase‏ ‎‡A Structure of Escherichia coli Flavodiiron Nitric Oxide Reductase‏ ‎‡9 1‏
919 ‎‡a symmetryandphaseselectednmrspectraofliquidcrystallinesamples‏ ‎‡A Symmetry and Phase-Selected NMR Spectra of Liquid Crystalline Samples‏ ‎‡9 1‏
919 ‎‡a synthesisconformationalpropertiesandantibodyrecognitionofpeptidescontainingbetaturnmimeticsbasedonalphaalkylprolinederivatives‏ ‎‡A Synthesis, conformational properties, and antibody recognition of peptides containing beta-turn mimetics based on alpha-alkylproline derivatives‏ ‎‡9 1‏
919 ‎‡a conformationofthemonensinasodiumcomplexinsolutiondeterminedfromselfconsistentnoedistanceconstraints‏ ‎‡A The Conformation of the Monensin-A-Sodium Complex in Solution Determined from Self-consistent NOE Distance Constraints‏ ‎‡9 1‏
919 ‎‡a lactatedehydrogenasesencodedbytheldhandldhbgenesinlactococcuslactisexhibitdistinctregulationandcatalyticpropertiescomparativemodelingtoprobethemolecularbasis‏ ‎‡A The lactate dehydrogenases encoded by the ldh and ldhB genes in Lactococcus lactis exhibit distinct regulation and catalytic properties - comparative modeling to probe the molecular basis‏ ‎‡9 1‏
919 ‎‡a solutionstructureofatetrahemecytochromefromshewanellafrigidimarinarevealsanovelfamilystructuralmotif‏ ‎‡A The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif‏ ‎‡9 1‏
919 ‎‡a thermodynamicandkineticcharacterisationofindividualhaemsinmulticentrecytochromesc3‏ ‎‡A Thermodynamic and kinetic characterisation of individual haems in multicentre cytochromes c3‏ ‎‡9 1‏
919 ‎‡a thermodynamicandkineticcharacterizationoftrihaemcytochromec3fromdesulfuromonasacetoxidans‏ ‎‡A Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans‏ ‎‡9 1‏
919 ‎‡a thermodynamicandkineticcharacterizationof2methylacceptingchemotaxishemesensorsfromgeobactersulfurreducensrevealsthestructuraloriginoftheirfunctionaldifference‏ ‎‡A Thermodynamic and kinetic characterization of two methyl-accepting chemotaxis heme sensors from Geobacter sulfurreducens reveals the structural origin of their functional difference‏ ‎‡9 1‏
919 ‎‡a thermodynamiccharacterizationofatetrahaemcytochromeisolatedfromafacultativeaerobicbacteriumshewanellafrigidimarinaaputativeredoxmodelforflavocytochromec3‏ ‎‡A Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3.‏ ‎‡9 1‏
919 ‎‡a tuningoffunctionalhemereductionpotentialsinshewanellafumaratereductases‏ ‎‡A Tuning of functional heme reduction potentials in Shewanella fumarate reductases‏ ‎‡9 1‏
919 ‎‡a 2dimensionaljspectroscopyprotoncoupledcarbon13nmr‏ ‎‡A Two‐dimensional J spectroscopy: Proton‐coupled carbon‐13 NMR‏ ‎‡9 1‏
919 ‎‡a 2dimensionalnmrstudiesofelectrontransferincytochromec3‏ ‎‡A Two-dimensional NMR studies of electron transfer in cytochrome c3‏ ‎‡9 1‏
919 ‎‡a 2dimensionalnuclearmagneticresonanceofparamagneticmetalloproteins‏ ‎‡A Two-dimensional nuclear magnetic resonance of paramagnetic metalloproteins.‏ ‎‡9 1‏
919 ‎‡a 13100andprotonnmrstudiesofhorsecytochrome100‏ ‎‡A 13 C and proton NMR studies of horse cytochrome c‏ ‎‡9 1‏
919 ‎‡a 13100nmrstudiesofhorseferrocytochrome100‏ ‎‡A 13 C-NMR studies of horse ferrocytochrome c‏ ‎‡9 1‏
919 ‎‡a 13candprotonnmrstudiesofhorsecytochrome100systematicassignmentofmethylandmethineresonancesinbothoxidationstates‏ ‎‡A 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states‏ ‎‡9 1‏
919 ‎‡a 1hand13cnmrinvestigationofredoxstatedependentandtemperaturedependentconformationchangesinhorsecytochrome100‏ ‎‡A 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c‏ ‎‡9 1‏
919 ‎‡a differencemethodforthereductionofautopeaksinautocorrelationspectra‏ ‎‡A A difference method for the reduction of “auto” peaks in autocorrelation spectra‏ ‎‡9 1‏
919 ‎‡a newpathwayformannitolmetabolisminyeastssuggestsalinktotheevolutionofalcoholicfermentation‏ ‎‡A A New Pathway for Mannitol Metabolism in Yeasts Suggests a Link to the Evolution of Alcoholic Fermentation‏ ‎‡9 1‏
919 ‎‡a approachtounderstandingconformationalmobilityinpeptidesandproteins‏ ‎‡A An approach to understanding conformational mobility in peptides and proteins‏ ‎‡9 1‏
919 ‎‡a integratedviewofredoxandcatalyticpropertiesofbtypeppdypfrompseudomonasputidamet94anditsdistalvariants‏ ‎‡A An integrated view of redox and catalytic properties of B-type PpDyP from Pseudomonas putida MET94 and its distal variants‏ ‎‡9 1‏
919 ‎‡a unusualconformationofthemethioninehaemligandincytochrome150establishedby2dimensional1hnmr‏ ‎‡A An unusual conformation of the methionine haem ligand in cytochrome cL established by two-dimensional 1H-NMR‏ ‎‡9 1‏
919 ‎‡a assignmentoftheredoxpotentialstothe4haemsindesulfovibriovulgariscytochrome1003by2dnmr‏ ‎‡A Assignment of the redox potentials to the four haems in Desulfovibrio vulgaris cytochrome c 3 by 2D-NMR‏ ‎‡9 1‏
919 ‎‡a bindingofligandsoriginatessmallperturbationsonthemicroscopicthermodynamicpropertiesofamulticentreredoxprotein‏ ‎‡A Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein‏ ‎‡9 1‏
919 ‎‡a carbon13nmrstudiesoftheinfluenceofaxialligandorientationonhaemelectronicstructure‏ ‎‡A Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure‏ ‎‡9 1‏
919 ‎‡a carbonfluxanalysisby13cnuclearmagneticresonancetodeterminetheeffectofco2onanaerobicsuccinateproductionbycorynebacteriumglutamicum‏ ‎‡A Carbon flux analysis by 13C nuclear magnetic resonance to determine the effect of CO2 on anaerobic succinate production by Corynebacterium glutamicum‏ ‎‡9 1‏
919 ‎‡a characterizationofthehaemenvironmentinmethylophilusmethylotrophusferricytochrome100by1hnmr‏ ‎‡A Characterization of the haem environment in Methylophilus methylotrophus ferricytochrome c "by 1H-NMR.‏ ‎‡9 1‏
919 ‎‡a characterizationoftheimprovedsensitivityobtainedusingaflowmethodforoxygenatingandmixingcellsuspensionsinnmr‏ ‎‡A Characterization of the improved sensitivity obtained using a flow method for oxygenating and mixing cell suspensions in NMR‏ ‎‡9 1‏
919 ‎‡a conformationalcomponentinthecoupledtransferofmultipleelectronsandprotonsinamonomerictetrahemecytochrome‏ ‎‡A Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome‏ ‎‡9 1‏
919 ‎‡a constrainedpeptideanaloguesoftransforminggrowthfactoralpharesiduescysteine2132aremitogenicallyactiveuseofprolinemimeticstoenhancebiologicalpotency‏ ‎‡A Constrained peptide analogues of transforming growth factor-alpha residues cysteine 21-32 are mitogenically active. Use of proline mimetics to enhance biological potency.‏ ‎‡9 1‏
919 ‎‡a crystallizationandpreliminary10raycharacterizationofcytochrome100fromtheobligatemethylotrophmethylophilusmethylotrophus‏ ‎‡A Crystallization and preliminary X-ray characterization of cytochrome c "from the obligate methylotroph Methylophilus methylotrophus‏ ‎‡9 1‏
919 ‎‡a determinationofhaemelectronicstructureincytochromeb5andmetcyanomyoglobin‏ ‎‡A Determination of Haem Electronic Structure in Cytochrome b5 and Metcyanomyoglobin‏ ‎‡9 1‏
919 ‎‡a determinationofthemagneticpropertiesandorientationofthehemeaxialligandsofppcafromgeobactermetallireducensbyparamagneticnmr‏ ‎‡A Determination of the magnetic properties and orientation of the heme axial ligands of PpcA from Geobacter metallireducens by paramagnetic NMR‏ ‎‡9 1‏
919 ‎‡a determinationoftheorientationoftheaxialligandsandofthemagneticpropertiesofthehaemsinthetetrahaemferricytochromefromshewanellafrigidimarina‏ ‎‡A Determination of the orientation of the axial ligands and of the magnetic properties of the haems in the tetrahaem ferricytochrome from Shewanella frigidimarina‏ ‎‡9 1‏
919 ‎‡a distancedependenceofinteractionsbetweenchargedcentresinproteinswithcommonstructuralfeatures‏ ‎‡A Distance dependence of interactions between charged centres in proteins with common structural features‏ ‎‡9 1‏
919 ‎‡a electrontransferbetweenmultihaemcytochromesc3fromdesulfovibrioafricanus‏ ‎‡A Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus‏ ‎‡9 1‏
919 ‎‡a evaluationof13cand1hfermicontactshiftsinhorsecytochrome100theoriginoftheanticurieeffect‏ ‎‡A Evaluation of 13C and 1H Fermi contact shifts in horse cytochrome c. The origin of the anti-Curie effect‏ ‎‡9 1‏
919 ‎‡a 4quartetsapplicationto2dimensionalnmr‏ ‎‡A Four quartets. Application to two-dimensional NMR‏ ‎‡9 1‏
919 ‎‡a functionalandmechanisticstudiesofcytochromec3fromdesulfovibriogigasthermodynamicsofaprotonthruster‏ ‎‡A Functional and Mechanistic Studies of Cytochromec3fromDesulfovibrio gigas: Thermodynamics of a “Proton Thruster” †‏ ‎‡9 1‏
919 ‎‡a functionalpropertiesoftype1andtype2cytochromesc3fromdesulfovibrioafricanus‏ ‎‡A Functional properties of type I and type II cytochromes c3 from Desulfovibrio africanus‏ ‎‡9 1‏
919 ‎‡a highyieldofmethylophilusmethylotrophuscytochrome100bycoexpressionwithcytochrome100maturationgeneclusterfromescherichiacoli‏ ‎‡A High Yield of Methylophilus methylotrophus Cytochrome c″ by Coexpression with Cytochrome c Maturation Gene Cluster from Escherichia coli‏ ‎‡9 1‏
919 ‎‡a highlyselectiveligandbindingbymethylophilusmethylotrophuscytochromec‏ ‎‡A Highly Selective Ligand Binding byMethylophilus methylotrophusCytochromec′′‏ ‎‡9 1‏
919 ‎‡a homotropicandheterotropiccooperativityinthetetrahaemcytochromec3fromdesulfovibriovulgaris‏ ‎‡A Homotropic and heterotropic cooperativity in the tetrahaem cytochrome c3 from Desulfovibrio vulgaris‏ ‎‡9 1‏
919 ‎‡a homotropicandheterotropicinteractionsincytochromes100‏ ‎‡A Homotropic and heterotropic interactions in cytochromes c‏ ‎‡9 1‏
919 ‎‡a homotropicandheterotropicinteractionsincytochromes1003fromsulphatereducingbacteria‏ ‎‡A Homotropic and heterotropic interactions in cytochromes c(3) from sulphate reducing bacteria‏ ‎‡9 1‏
919 ‎‡a involvementofalabileaxialhistidineincouplingelectronandprotontransferinmethylophilusmethylotrophuscytochrome100‏ ‎‡A Involvement of a labile axial histidine in coupling electron and proton transfer in Methylophilus methylotrophus cytochrome c "‏ ‎‡9 1‏
919 ‎‡a mannosylglyceratestabilizesstaphylococcalnucleasewithrestrictionofslowβsheetmotions‏ ‎‡A Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motions‏ ‎‡9 1‏
919 ‎‡a metabolicandtranscriptionalanalysisofacidstressinlactococcuslactiswithafocusonthekineticsoflacticacidpools‏ ‎‡A Metabolic and transcriptional analysis of acid stress in Lactococcus lactis, with a focus on the kinetics of lactic acid pools‏ ‎‡9 1‏
919 ‎‡a obtainingligandgeometriesfromparamagneticshiftsinlowspinhaemproteins‏ ‎‡A Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins.‏ ‎‡9 1‏
919 ‎‡a paramagneticnmrshiftsincyanoferricytochrome100‏ ‎‡A Paramagnetic NMR shifts in cyanoferricytochrome c‏ ‎‡9 1‏
919 ‎‡a phdependenceofstructuralandfunctionalpropertiesofoxidizedcytochromecfrommethylophilusmethylotrophus‏ ‎‡A pH Dependence of Structural and Functional Properties of Oxidized Cytochromec "fromMethylophilus methylotrophus‏ ‎‡9 1‏
919 ‎‡a pitfallsinassigninghemeaxialcoordinationbyepr‏ ‎‡A Pitfalls in assigning heme axial coordination by EPR‏ ‎‡9 1‏
919 ‎‡a proteinstabilizationbycompatiblesoluteseffectofdiglycerolphosphateonthedynamicsofdesulfovibriogigasrubredoxinstudiedbynmr‏ ‎‡A Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR.‏ ‎‡9 1‏
919 ‎‡a protonassisted2electrontransferinnaturalvariantsoftetrahemecytochromesfromdesulfomicrobiumsp‏ ‎‡A Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.‏ ‎‡9 1‏
919 ‎‡a protonnmrstudiesofhorseferricytochrome100completionoftheassignmentofthewellresolvedhyperfineshiftedresonances‏ ‎‡A Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances‏ ‎‡9 1‏
919 ‎‡a redoxandphlinkedconformationalchangesintrihemecytochromeppcafromgeobactersulfurreducens‏ ‎‡A Redox- and pH-linked conformational changes in triheme cytochrome PpcA from Geobacter sulfurreducens‏ ‎‡9 1‏
919 ‎‡a redoxbehaviourofthehaemdomainofflavocytochromec3fromshewanellafrigidimarinaprobedbynmr‏ ‎‡A Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.‏ ‎‡9 1‏
919 ‎‡a redoxlinkedconformationalchangesincytochromec3fromdesulfovibriodesulfuricansatcc27774‏ ‎‡A Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774‏ ‎‡9 1‏
919 ‎‡a relationshipbetweenproteinstabilizationandproteinrigidificationinducedbymannosylglycerate‏ ‎‡A Relationship between protein stabilization and protein rigidification induced by mannosylglycerate‏ ‎‡9 1‏
919 ‎‡a relativeimportanceofdrivingforceandelectrostaticinteractionsinthereductionofmultihaemcytochromesbysmallmolecules‏ ‎‡A Relative importance of driving force and electrostatic interactions in the reduction of multihaem cytochromes by small molecules‏ ‎‡9 1‏
919 ‎‡a replacementofthemethionineaxialligandincytochrome100‏ ‎‡A Replacement of the methionine axial ligand in cytochrome c‏ ‎‡9 1‏
919 ‎‡a replacementofthemethionineaxialligandincytochrome100550byalysineeffectsonthehaemelectronicstructure‏ ‎‡A Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure‏ ‎‡9 1‏
919 ‎‡a revisionofthehaemcorearchitectureinthetetraheamcytochrome100fromdesulfovibriobaculatusby2dimensional1hnmr‏ ‎‡A Revision of the haem-core architecture in the tetraheam cytochrome c from Desulfovibrio baculatus by two-dimensional 1H NMR‏ ‎‡9 1‏
919 ‎‡a solutionstructureanddynamicsoftheoutermembranecytochromeomcffromgeobactersulfurreducens‏ ‎‡A Solution structure and dynamics of the outer membrane cytochrome OmcF from Geobacter sulfurreducens‏ ‎‡9 1‏
919 ‎‡a solutionstructureofamutantofthetrihemecytochromeppcafromgeobactersulfurreducensshedslightontheroleoftheconservedaromaticresiduef15‏ ‎‡A Solution structure of a mutant of the triheme cytochrome PpcA from Geobacter sulfurreducens sheds light on the role of the conserved aromatic residue F15‏ ‎‡9 1‏
946 ‎‡a b‏ ‎‡9 1‏
996 ‎‡2 ISNI|0000000039001482
996 ‎‡2 NSK|000804036
996 ‎‡2 BAV|495_267066
996 ‎‡2 NYNYRILM|183534
996 ‎‡2 ISNI|0000000445077458
996 ‎‡2 ISNI|0000000399347049
996 ‎‡2 LC|n 85067474
996 ‎‡2 ISNI|000000039633391X
996 ‎‡2 NII|DA02988127
996 ‎‡2 SUDOC|184044596
996 ‎‡2 NLA|000035040113
996 ‎‡2 LC|nb2008026208
996 ‎‡2 ISNI|0000000073991598
996 ‎‡2 LC|nb2014019193
996 ‎‡2 BNE|XX970581
996 ‎‡2 BNF|17981772
996 ‎‡2 ISNI|0000000044636749
996 ‎‡2 ISNI|0000000516672757
996 ‎‡2 LC|nb2001032582
996 ‎‡2 BIBSYS|90857916
996 ‎‡2 ISNI|000000038357380X
996 ‎‡2 NUKAT|n 2017025862
996 ‎‡2 PTBNP|350972
996 ‎‡2 LC|no2020132490
996 ‎‡2 LC|n 80010341
996 ‎‡2 ISNI|0000000063273277
996 ‎‡2 J9U|987007438789305171
996 ‎‡2 LC|n 87935199
996 ‎‡2 SUDOC|092738133
996 ‎‡2 ISNI|0000000442641738
996 ‎‡2 NII|DA12774334
996 ‎‡2 DNB|170543196
996 ‎‡2 ISNI|0000000026618504
996 ‎‡2 DNB|1225942004
996 ‎‡2 ISNI|0000000042514406
996 ‎‡2 LC|nb2005016939
996 ‎‡2 NLA|000035589413
996 ‎‡2 BNF|12426964
996 ‎‡2 ISNI|0000000041887454
996 ‎‡2 NUKAT|nx2023543191
996 ‎‡2 NKC|jo20191050086
996 ‎‡2 LC|n 2005068884
996 ‎‡2 LC|n 86860613
996 ‎‡2 LC|n 86860612
996 ‎‡2 CAOONL|ncf10975213
996 ‎‡2 ISNI|0000000383950775
996 ‎‡2 NII|DA04470108
996 ‎‡2 LIH|LNB:BE_t_8;=BZ
996 ‎‡2 LC|no2006006520
996 ‎‡2 ISNI|0000000498231711
996 ‎‡2 PTBNP|1562563
996 ‎‡2 SUDOC|234706279
996 ‎‡2 LC|n 79068016
996 ‎‡2 LNB|LNC10-000266328
996 ‎‡2 LC|n 89653656
996 ‎‡2 DNB|173448135
996 ‎‡2 BNF|14468487
996 ‎‡2 BIBSYS|90161984
996 ‎‡2 LNB|LNC10-000036677
996 ‎‡2 DNB|118939491
996 ‎‡2 ISNI|0000000050289122
996 ‎‡2 DBC|87097969040969
996 ‎‡2 NII|DA06002483
996 ‎‡2 J9U|987007356377105171
996 ‎‡2 LC|n 88606761
996 ‎‡2 ISNI|0000000494124521
996 ‎‡2 ISNI|0000000040091606
996 ‎‡2 NTA|071647945
996 ‎‡2 CAOONL|ncf10065040
996 ‎‡2 LC|n 81087973
996 ‎‡2 ISNI|0000000138855969
996 ‎‡2 NUKAT|n 2006106918
996 ‎‡2 LC|nr 90020716
996 ‎‡2 SUDOC|272752304
996 ‎‡2 SUDOC|081988168
996 ‎‡2 ISNI|0000000050789135
996 ‎‡2 NUKAT|n 95002492
996 ‎‡2 BIBSYS|2108174
996 ‎‡2 DNB|102375984
996 ‎‡2 ISNI|000000002736223X
996 ‎‡2 RERO|A012385847
996 ‎‡2 BNF|13548680
996 ‎‡2 LIH|LNB:BK_f_3;=BM
996 ‎‡2 LC|n 2017020922
996 ‎‡2 ISNI|0000000050775980
996 ‎‡2 RERO|A003915426
996 ‎‡2 RERO|A003915425
996 ‎‡2 DNB|1145304338
996 ‎‡2 NKC|utb20191023232
996 ‎‡2 NKC|ola2012719409
996 ‎‡2 ISNI|0000000046334795
996 ‎‡2 SUDOC|035526106
996 ‎‡2 DNB|1015385850
996 ‎‡2 ISNI|000000006151169X
996 ‎‡2 ISNI|0000000082111601
996 ‎‡2 DNB|1030192553
996 ‎‡2 LC|n 88156124
996 ‎‡2 LC|n 96062273
996 ‎‡2 LC|no2008169303
996 ‎‡2 ISNI|0000000026526802
996 ‎‡2 SUDOC|254251579
996 ‎‡2 LC|nb2016023893
996 ‎‡2 LC|no2022027947
996 ‎‡2 DNB|1263037100
996 ‎‡2 DNB|1118644239
996 ‎‡2 CAOONL|ncf12027764
996 ‎‡2 SUDOC|276743660
996 ‎‡2 J9U|987007456659905171
996 ‎‡2 DNB|1183698496
996 ‎‡2 SUDOC|15877065X
996 ‎‡2 DNB|1025823222
996 ‎‡2 CAOONL|ncf11936088
996 ‎‡2 BNF|14412676
996 ‎‡2 ISNI|0000000436809645
996 ‎‡2 NLA|000035968321
996 ‎‡2 LC|n 85155254
996 ‎‡2 BNF|14600730
996 ‎‡2 LC|nb 98016882
996 ‎‡2 N6I|vtls000082679
996 ‎‡2 LC|nb2005017869
996 ‎‡2 SUDOC|033400415
996 ‎‡2 NTA|371710812
996 ‎‡2 SUDOC|073714577
996 ‎‡2 LC|n 82000019
996 ‎‡2 ISNI|0000000052234846
996 ‎‡2 BNF|17985721
996 ‎‡2 LC|no2004076032
996 ‎‡2 PLWABN|9814283095205606
996 ‎‡2 CAOONL|ncf12130248
996 ‎‡2 LC|n 81121855
996 ‎‡2 RERO|A022022024
996 ‎‡2 NTA|408692251
996 ‎‡2 J9U|987007383306205171
996 ‎‡2 NTA|068370571
996 ‎‡2 NTA|312651503
996 ‎‡2 J9U|987012798159505171
996 ‎‡2 BIBSYS|90141392
996 ‎‡2 NUKAT|n 2022075288
996 ‎‡2 ISNI|0000000035936950
996 ‎‡2 NTA|136063861
996 ‎‡2 NTA|074744224
996 ‎‡2 BNF|15819482
996 ‎‡2 NKC|pna2015857972
996 ‎‡2 ISNI|0000000043732560
996 ‎‡2 NTA|339721170
996 ‎‡2 LC|no2020071470
996 ‎‡2 J9U|987007269177005171
996 ‎‡2 LC|n 84213886
996 ‎‡2 CAOONL|ncf11948080
996 ‎‡2 ISNI|0000000048645300
996 ‎‡2 ISNI|0000000496243065
996 ‎‡2 J9U|987007426179305171
996 ‎‡2 SUDOC|050814079
996 ‎‡2 NII|DA12933278
996 ‎‡2 LC|nb2014005326
996 ‎‡2 LC|n 78031551
996 ‎‡2 SUDOC|067735320
996 ‎‡2 J9U|987007437839105171
996 ‎‡2 LC|nb2013000746
996 ‎‡2 ISNI|0000000078938331
996 ‎‡2 LC|n 83204907
996 ‎‡2 LC|no2017026187
996 ‎‡2 SUDOC|171837959
996 ‎‡2 SUDOC|030026792
996 ‎‡2 ISNI|0000000496837701
996 ‎‡2 ISNI|0000000035942963
996 ‎‡2 NDL|001223528
996 ‎‡2 NTA|074512714
996 ‎‡2 CAOONL|ncf10027038
996 ‎‡2 JPG|500124274
996 ‎‡2 JPG|500124275
996 ‎‡2 LC|nb 99008638
996 ‎‡2 LC|n 88156119
996 ‎‡2 NDL|00853604
996 ‎‡2 NTA|267564686
996 ‎‡2 LC|nb2018004586
996 ‎‡2 ISNI|0000000083896404
996 ‎‡2 ISNI|0000000083275691
996 ‎‡2 ISNI|0000000118331949
996 ‎‡2 LC|no2012155420
996 ‎‡2 LC|n 79110674
996 ‎‡2 ISNI|000000040339333X
996 ‎‡2 RERO|A022953892
996 ‎‡2 SUDOC|255677324
996 ‎‡2 CAOONL|ncf10237389
996 ‎‡2 NUKAT|n 2020031145
996 ‎‡2 NKC|xx0181495
996 ‎‡2 ISNI|0000000081693638
996 ‎‡2 J9U|987007420754805171
996 ‎‡2 DNB|1338005235
996 ‎‡2 NUKAT|n 2010077889
996 ‎‡2 BNF|12466993
996 ‎‡2 NTA|42268144X
996 ‎‡2 LC|no2022044862
996 ‎‡2 LC|nb2016018789
996 ‎‡2 ISNI|0000000043314473
996 ‎‡2 LC|n 79007063
996 ‎‡2 RERO|A022279804
996 ‎‡2 LC|nb 99082355
996 ‎‡2 NUKAT|nx2023166994
996 ‎‡2 NTA|073685550
996 ‎‡2 SUDOC|273899724
996 ‎‡2 ISNI|0000000117569701
996 ‎‡2 LC|n 2007012415
996 ‎‡2 LC|no2022086543
996 ‎‡2 CAOONL|ncf12101505
996 ‎‡2 PLWABN|9810585305105606
996 ‎‡2 ISNI|000000002150409X
996 ‎‡2 LC|n 94085616
996 ‎‡2 DNB|1223468267
996 ‎‡2 SUDOC|258246804
996 ‎‡2 LC|no 93031921
996 ‎‡2 J9U|987007423677705171
996 ‎‡2 J9U|987007272201105171
996 ‎‡2 SUDOC|074322141
996 ‎‡2 LC|no2008087498
996 ‎‡2 ISNI|0000000047245487
996 ‎‡2 LC|n 86861433
996 ‎‡2 NUKAT|n 2009098151
996 ‎‡2 SUDOC|088613836
996 ‎‡2 ISNI|000000004304627X
996 ‎‡2 BNF|13194654
996 ‎‡2 ISNI|0000000021846823
996 ‎‡2 LC|n 2013070001
996 ‎‡2 J9U|987007294191405171
996 ‎‡2 ISNI|0000000050370967
996 ‎‡2 NKC|ntk2011617745
996 ‎‡2 DNB|1147191514
996 ‎‡2 LC|n 96121565
996 ‎‡2 RERO|A012430716
996 ‎‡2 ISNI|0000000067171964
996 ‎‡2 NUKAT|n 2005129159
996 ‎‡2 ISNI|0000000038208342
996 ‎‡2 CAOONL|ncf11468116
996 ‎‡2 ISNI|0000000063593596
996 ‎‡2 ISNI|000000007594906X
996 ‎‡2 ISNI|000000002913867X
996 ‎‡2 SUDOC|263498492
996 ‎‡2 ISNI|0000000053043523
996 ‎‡2 LC|no2019123323
996 ‎‡2 LC|n 2024045063
996 ‎‡2 ISNI|0000000416606875
996 ‎‡2 DNB|1252651589
996 ‎‡2 LC|nb2005017884
996 ‎‡2 LC|nb2005017885
996 ‎‡2 NLA|000035175647
996 ‎‡2 LC|nb2005017882
996 ‎‡2 LC|nb2005017883
996 ‎‡2 LC|n 2020021263
996 ‎‡2 NLA|000035042023
997 ‎‡a 0 0 lived 0 0‏ ‎‡9 1‏