On the public citation graph

Structural Insights into the Initiation of Free Radical Formation in the Class Ib Ribonucleotide Reductases in Mycobacteria

https://doi.org/10.2139/ssrn.4808936
0 signed · 54 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/jcc.20084openalex-extracted
UCSF Chimera—A visualization system for exploratory research and analysis
inferredcites →https://doi.org/10.1002/jcc.21303openalex-extracted
Crystal contacts as nature's docking solutions
inferredcites →https://doi.org/10.1007/11560500_15openalex-extracted
Detection of Protein Assemblies in Crystals
inferredcites →https://doi.org/10.1007/s00018-005-5514-4openalex-extracted
Flavodoxins: sequence, folding, binding, function and beyond
inferredcites →https://doi.org/10.1007/s00775-019-01703-zopenalex-extracted
Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access
inferredcites →https://doi.org/10.1007/s00775-020-01782-3openalex-extracted
The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron
inferredcites →https://doi.org/10.1016/j.bpj.2013.10.017openalex-extracted
Strong Ionic Hydrogen Bonding Causes a Spectral Isotope Effect in Photoactive Yellow Protein
inferredcites →https://doi.org/10.1016/j.febslet.2004.05.059openalex-extracted
Crystal structure of the biologically active form of class Ib ribonucleotide reductase small subunit from Mycobacterium tuberculosis
inferredcites →https://doi.org/10.1016/j.jbc.2021.101137openalex-extracted
The periodic table of ribonucleotide reductases
inferredcites →https://doi.org/10.1016/j.jmb.2006.03.035openalex-extracted
The First Holocomplex Structure of Ribonucleotide Reductase Gives New Insight into its Mechanism of Action
inferredcites →https://doi.org/10.1016/j.jmb.2007.05.022openalex-extracted
Inference of Macromolecular Assemblies from Crystalline State
inferredcites →https://doi.org/10.1016/j.tube.2011.03.004openalex-extracted
Structural biology of Mycobacterium tuberculosis proteins: The Indian efforts
inferredcites →https://doi.org/10.1016/s0969-2126(01)00628-1openalex-extracted
Crystal Structure of Manganese Catalase from Lactobacillus plantarum
inferredcites →https://doi.org/10.1016/s0969-2126(97)00259-1openalex-extracted
Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding
inferredcites →https://doi.org/10.1021/acs.biochem.6b00699openalex-extracted
Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus
inferredcites →https://doi.org/10.1021/acs.chemrev.7b00650openalex-extracted
Same Substrate, Many Reactions: Oxygen Activation in Flavoenzymes
inferredcites →https://doi.org/10.1021/acs.inorgchem.3c04163openalex-extracted
Class Ib Ribonucleotide Reductases: Activation of a Peroxido-MnIIMnIII to Generate a Reactive Oxo-MnIIIMnIV Oxidant
inferredcites →https://doi.org/10.1021/acs.jpclett.1c00814openalex-extracted
Two Distinct Oxygen-Radical Conformations in the X-ray Free Electron Laser Structures of Photosystem II
inferredcites →https://doi.org/10.1021/bi011429lopenalex-extracted
Crystal Structure of the Di-iron/Radical Protein of Ribonucleotide Reductase from Corynebacterium ammoniagenes,
inferredcites →https://doi.org/10.1021/bi101881dopenalex-extracted
Escherichia coli Class Ib Ribonucleotide Reductase Contains a Dimanganese(III)-Tyrosyl Radical Cofactor in Vivo
inferredcites →https://doi.org/10.1021/bi981380sopenalex-extracted
Structure of Salmonella typhimurium nrdF Ribonucleotide Reductase in Its Oxidized and Reduced Forms,
inferredcites →https://doi.org/10.1021/cb400757hopenalex-extracted
Crystal Structure of Bacillus cereus Class Ib Ribonucleotide Reductase Di-iron NrdF in Complex with NrdI
inferredcites →https://doi.org/10.1021/ed076p759.1openalex-extracted
An Introduction to Hydrogen Bonding (Jeffrey, George A.)
inferredcites →https://doi.org/10.1021/ja1036995openalex-extracted
A Tyrosyl−Dimanganese Coupled Spin System is the Native Metalloradical Cofactor of the R2F Subunit of the Ribonucleotide Reductase of Corynebacterium ammoniagenes
inferredcites →https://doi.org/10.1021/ja109712qopenalex-extracted
Multiscale Simulation Reveals Multiple Pathways for H2 and O2 Transport in a [NiFe]-Hydrogenase
inferredcites →https://doi.org/10.1021/ja312457topenalex-extracted
Mechanism of Assembly of the Dimanganese-Tyrosyl Radical Cofactor of Class Ib Ribonucleotide Reductase: Enzymatic Generation of Superoxide Is Required for Tyrosine Oxidation via a Mn(III)Mn(IV) Intermediate
inferredcites →https://doi.org/10.1021/ja401342sopenalex-extracted
Function of the Diiron Cluster ofEscherichia coliClass Ia Ribonucleotide Reductase in Proton-Coupled Electron Transfer
inferredcites →https://doi.org/10.1038/345593a0openalex-extracted
Three-dimensional structure of the free radical protein of ribonucleotide reductase
inferredcites →https://doi.org/10.1038/s41467-019-10568-4openalex-extracted
Convergent allostery in ribonucleotide reductase
inferredcites →https://doi.org/10.1073/pnas.0510977103openalex-extracted
The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
inferredcites →https://doi.org/10.1073/pnas.0536684100openalex-extracted
Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-Å x-ray data
inferredcites →https://doi.org/10.1073/pnas.0807348105openalex-extracted
NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
inferredcites →https://doi.org/10.1074/jbc.m104103200openalex-extracted
Oxygen Access to the Active Site of Cholesterol Oxidase through a Narrow Channel Is Gated by an Arg-Glu Pair
inferredcites →https://doi.org/10.1074/jbc.m110.186841openalex-extracted
Superoxide Is Produced by the Reduced Flavin in Mitochondrial Complex I
inferredcites →https://doi.org/10.1074/jbc.m117.783092openalex-extracted
Glutamate 52-β at the α/β subunit interface of Escherichia coli class Ia ribonucleotide reductase is essential for conformational gating of radical transfer
inferredcites →https://doi.org/10.1107/s0021889807021206openalex-extracted
Phaser crystallographic software
inferredcites →https://doi.org/10.1107/s0907444904019158openalex-extracted
Coot : model-building tools for molecular graphics
inferredcites →https://doi.org/10.1107/s0907444911001314openalex-extracted
REFMAC 5 for the refinement of macromolecular crystal structures
inferredcites →https://doi.org/10.1107/s0907444912001308openalex-extracted
Towards automated crystallographic structure refinement with phenix.refine
inferredcites →https://doi.org/10.1107/s0907444913012274openalex-extracted
Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography
inferredcites →https://doi.org/10.1111/j.1742-4658.2010.07815.xopenalex-extracted
High‐resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states – an unusual flavodoxin
inferredcites →https://doi.org/10.1126/science.1190187openalex-extracted
Structural Basis for Activation of Class Ib Ribonucleotide Reductase
inferredcites →https://doi.org/10.1126/science.1650033openalex-extracted
Mechanism of Assembly of the Tyrosyl Radical-Dinuclear Iron Cluster Cofactor of Ribonucleotide Reductase
inferredcites →https://doi.org/10.1126/science.aba6794openalex-extracted
Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex
inferredcites →https://doi.org/10.1128/jb.00185-08openalex-extracted
NrdI Essentiality for Class Ib Ribonucleotide Reduction in Streptococcus pyogenes
inferredcites →https://doi.org/10.1128/jb.01409-08openalex-extracted
Function and Regulation of Class I Ribonucleotide Reductase-Encoding Genes in Mycobacteria
inferredcites →https://doi.org/10.1146/annurev.biochem.67.1.71openalex-extracted
RIBONUCLEOTIDE REDUCTASES
inferredcites →https://doi.org/10.1146/annurev.biochem.75.103004.142443openalex-extracted
Ribonucleotide Reductases
inferredcites →https://doi.org/10.1371/journal.pcbi.1002708openalex-extracted
CAVER 3.0: A Tool for the Analysis of Transport Pathways in Dynamic Protein Structures
inferredcites →https://doi.org/10.3389/fcimb.2014.00052openalex-extracted
Ribonucleotide reductases: essential enzymes for bacterial life
inferredcites →https://doi.org/10.3389/fmolb.2020.598912openalex-extracted
N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position
inferredcites →https://doi.org/10.7554/elife.07141openalex-extracted
Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli
inferredcites →https://doi.org/10.7554/elife.31502openalex-extracted
3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound
inferredcites →https://doi.org/10.7554/elife.79226openalex-extracted
Redox-controlled reorganization and flavin strain within the ribonucleotide reductase R2b–NrdI complex monitored by serial femtosecond crystallography
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.