sameAs
P1855
Three-dimensional structure of the free radical protein of ribonucleotide reductaseA method to find tissue-specific novel sites of selective adenosine deamination.SegH and Hef: two novel homing endonucleases whose genes replace the mobC and mobE genes in several T4-related phagesRestoring proper radical generation by azide binding to the iron site of the E238A mutant R2 protein of ribonucleotide reductase from Escherichia coliStructural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductasesCrystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenesA metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductaseHigh-resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states--an unusual flavodoxin. Structural biologyStructural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP ConesAutocatalytic generation of dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the dopa-208 proteinBinding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate bindingA new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductaseCrystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteinsDistribution, sequence homology, and homing of group I introns among T-even-like bacteriophages: evidence for recent transfer of old intronsTrisodium phosphonoformate, a new antiviral compoundEfficient growth inhibition of Bacillus anthracis by knocking out the ribonucleotide reductase tyrosyl radical.Ribonucleotide reductase modularity: Atypical duplication of the ATP-cone domain in Pseudomonas aeruginosaTwo proteins mediate class II ribonucleotide reductase activity in Pseudomonas aeruginosa: expression and transcriptional analysis of the aerobic enzymesBiochemical Characterization of the Split Class II Ribonucleotide Reductase from Pseudomonas aeruginosaThe origin and evolution of ribonucleotide reductionThe ribonucleotide reductase jigsaw puzzle: a large piece falls into place.Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F.RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to Genbank.Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron center.Generation and electron paramagnetic resonance spin trapping detection of thiyl radicals in model proteins and in the R1 subunit of Escherichia coli ribonucleotide reductase.A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H. Combined x-ray diffraction and EPR/ENDOR studies.Localization and characterization of two nucleotide-binding sites on the anaerobic ribonucleotide reductase from bacteriophage T4.New paramagnetic species formed at the expense of the transient tyrosyl radical in mutant protein R2 F208Y of Escherichia coli ribonucleotide reductase.Ribonucleotide reduction - horizontal transfer of a required function spans all three domains.Subunit and small-molecule interaction of ribonucleotide reductases via surface plasmon resonance biosensor analysesCarboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: kinetic analysis of inhibition studies.Ribonucleotide reductase. A virtual playground for electron transfer reactions.Use of structural phylogenetic networks for classification of the ferritin-like superfamily.Discovery of antimicrobial ribonucleotide reductase inhibitors by screening in microwell formatThiols in redox mechanism of ribonucleotide reductase.A metagenomics transect into the deepest point of the Baltic Sea reveals clear stratification of microbial functional capacitiesThe Crystal Structure of Thermotoga maritima Class III Ribonucleotide Reductase Lacks a Radical Cysteine Pre-Positioned in the Active SiteInsertion of a homing endonuclease creates a genes-in-pieces ribonucleotide reductase that retains function.A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD geneProtein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene.
P50
Q22061880-2A5074CD-54F8-4D33-BE07-6BB611A90AB7Q24536298-338E4FB1-4118-4C2E-9031-7AE05F3A084CQ24812579-08964862-8E8B-478D-B119-5C6F89D17A8CQ27631516-EA0E2E5F-A617-4F7B-9CFA-6E799532498BQ27635227-4DB0ECF1-E363-4F9E-B248-6FF0342125F1Q27637422-A515D809-00C4-4327-96C5-270BB2D00E71Q27640784-EC69F80B-BAAB-441B-8760-542D2143AE84Q27664408-A894830C-28C7-4BE2-934B-FB99B27EAD8AQ27704771-93EC0BBE-ED84-4AC9-9B0A-85195E0A7F86Q27732006-E716EACA-72F0-48D8-8665-EC20F93C65D7Q27744341-AA27DD71-324D-4338-859C-BF8619F2F6A4Q27748304-29B35919-A0BB-4EC9-B442-21BE09083E4AQ27764908-0B7746ED-65BF-4E29-ABB2-0B818F135ED5Q28250982-888491FC-D8AE-4CCF-9B78-537C2F5B19B7Q28321928-C5F0FAC1-9B3E-46E4-9AF5-3A91BF18C859Q28386930-9EFF0F26-5364-439C-9F16-1BCCF0C8CDFFQ28492584-333D91E3-007B-4F15-897D-2F84B9AC8C2DQ28492748-35C21A2A-8097-42A2-A70B-EAA6771F4BDCQ28546909-70A51406-403E-4166-B106-0D924626ED3AQ28649971-C5B5907B-2143-4895-9F96-CEE430238C2DQ30194064-2F82A8D4-A4DD-42EA-9E9C-E12A0AD65EF0Q30194064-FB6D4951-44A8-4736-94AE-C186D11F2B49Q30421091-5E10C31D-8E5C-4636-94BF-CCBB893DF5C8Q30967498-46C166D4-A447-4300-BB38-777D3348A7A6Q31021399-DACC1D4F-700B-4ABB-8963-F60C53B27E73Q31032678-C6EFCCC7-66EB-4652-AFB7-A8C1CEA2360FQ31139122-9D67A10E-7558-4B5E-8EEF-8E5B2B05441CQ32023627-78FC588C-9058-44F5-9FF8-CA6AA70AB2C2Q32061682-6F98CF4C-0ACD-4FE1-A74D-4EDC76FF10BBQ33767059-21A6D532-15D7-4865-B6A9-2790CD5147E8Q33967620-9B8688A7-F3FE-4052-819B-A28E48C2D560Q34108189-08689663-0D20-44A6-9828-6E0B2A563340Q34147845-7049740D-F2C6-457A-B6DF-F51A6AD139CEQ34246786-3056B38A-2A78-4321-B32A-2C4872D5B2CEQ34292119-DA1BF2ED-B6DA-4DE0-B849-0DE1ACEB6300Q34555725-D908C792-E2F9-4B83-92CE-E97EF610ABFDQ35005286-ADAEC71A-3F02-424A-8BB0-F2CDFB46BA36Q35683551-5785512B-0130-430D-ADE4-3B836D7F238DQ35748580-FFD5AE25-816F-46B0-B8F5-982F8697EF3FQ36061742-D699463C-37E8-462C-91AF-78398C88B953
P50
description
Swedish biochemist
@en
Zweeds academicus
@nl
académica sueca
@ast
bithchemiceoir Sualannach
@ga
name
Britt-Marie Sjöberg
@ast
Britt-Marie Sjöberg
@ca
Britt-Marie Sjöberg
@en
Britt-Marie Sjöberg
@es
Britt-Marie Sjöberg
@fi
Britt-Marie Sjöberg
@fr
Britt-Marie Sjöberg
@ga
Britt-Marie Sjöberg
@it
Britt-Marie Sjöberg
@nl
Britt-Marie Sjöberg
@sl
type
label
Britt-Marie Sjöberg
@ast
Britt-Marie Sjöberg
@ca
Britt-Marie Sjöberg
@en
Britt-Marie Sjöberg
@es
Britt-Marie Sjöberg
@fi
Britt-Marie Sjöberg
@fr
Britt-Marie Sjöberg
@ga
Britt-Marie Sjöberg
@it
Britt-Marie Sjöberg
@nl
Britt-Marie Sjöberg
@sl
prefLabel
Britt-Marie Sjöberg
@ast
Britt-Marie Sjöberg
@ca
Britt-Marie Sjöberg
@en
Britt-Marie Sjöberg
@es
Britt-Marie Sjöberg
@fi
Britt-Marie Sjöberg
@fr
Britt-Marie Sjöberg
@ga
Britt-Marie Sjöberg
@it
Britt-Marie Sjöberg
@nl
Britt-Marie Sjöberg
@sl
P106
P108
P21
P27
P31
P496
0000-0001-5953-3360
P5463
Sjöberg_Britt-Marie
P569
1944-01-01T00:00:00Z