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WKP|Q47928733
(VIAF cluster)
(Authority/Source Record)
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20241120235922.0 |
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241120nneanz||abbn n and d |
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(WKP)Q47928733
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0000-0002-3754-6459
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orcid
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7402934380
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scopus
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(OCoLC)Q47928733
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100
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David L. Turner
‡9
es
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375
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1
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iso5218
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400
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ডেভিড এল টার্নার
‡c
গবেষক
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bn
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David L. Turner
‡c
British Portuguese chemist
‡9
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400
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David L. Turner
‡c
onderzoeker
‡9
nl
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670
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‡a
Author's 13 C and proton NMR studies of horse cytochrome c
|
670
|
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|
‡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
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|
|
‡a
Author's Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus
|
670
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|
|
‡a
Author's Evaluation of 13C and 1H Fermi contact shifts in horse cytochrome c. The origin of the anti-Curie effect
|
670
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|
|
‡a
Author's Four quartets. Application to two-dimensional NMR
|
670
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‡a
Author's Functional and Mechanistic Studies of Cytochromec3fromDesulfovibrio gigas: Thermodynamics of a “Proton Thruster” †
|
670
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‡a
Author's Functional properties of type I and type II cytochromes c3 from Desulfovibrio africanus
|
670
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|
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‡a
Author's High Yield of Methylophilus methylotrophus Cytochrome c″ by Coexpression with Cytochrome c Maturation Gene Cluster from Escherichia coli
|
670
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‡a
Author's Highly Selective Ligand Binding byMethylophilus methylotrophusCytochromec′′
|
670
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‡a
Author's Homotropic and heterotropic cooperativity in the tetrahaem cytochrome c3 from Desulfovibrio vulgaris
|
670
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‡a
Author's Homotropic and heterotropic interactions in cytochromes c
|
670
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‡a
Author's Homotropic and heterotropic interactions in cytochromes c(3) from sulphate reducing bacteria
|
670
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‡a
Author's Involvement of a labile axial histidine in coupling electron and proton transfer in Methylophilus methylotrophus cytochrome c "
|
670
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|
‡a
Author's Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motions
|
670
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|
|
‡a
Author's Metabolic and transcriptional analysis of acid stress in Lactococcus lactis, with a focus on the kinetics of lactic acid pools
|
670
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|
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‡a
Author's Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins.
|
670
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‡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
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‡a
Author's Pitfalls in assigning heme axial coordination by EPR
|
670
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‡a
Author's Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR.
|
670
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|
|
‡a
Author's Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.
|
670
|
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|
‡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
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|
|
‡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
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|
|
‡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
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|
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‡a
bindingofligandsoriginatessmallperturbationsonthemicroscopicthermodynamicpropertiesofamulticentreredoxprotein
‡A
Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
‡9
1
|
919
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|
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‡a
carbon13nmrstudiesoftheinfluenceofaxialligandorientationonhaemelectronicstructure
‡A
Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure
‡9
1
|
919
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|
|
‡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
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|
|
‡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
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‡a
crystallizationandpreliminary10raycharacterizationofcytochrome100fromtheobligatemethylotrophmethylophilusmethylotrophus
‡A
Crystallization and preliminary X-ray characterization of cytochrome c "from the obligate methylotroph Methylophilus methylotrophus
‡9
1
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919
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‡a
determinationofhaemelectronicstructureincytochromeb5andmetcyanomyoglobin
‡A
Determination of Haem Electronic Structure in Cytochrome b5 and Metcyanomyoglobin
‡9
1
|
919
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‡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
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|
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‡a
electrontransferbetweenmultihaemcytochromesc3fromdesulfovibrioafricanus
‡A
Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus
‡9
1
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919
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‡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
|