Reference health
An O‐Centered Structure of the Trinuclear Copper Center in the Cys500Ser/Glu506Gln Mutant of CueO and Structural Changes in Low to High X‐Ray Dose Conditions
32/32 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
The 32 checked references that resolve
resolves10.1006/bbrc.2001.5474
CueO Is a Multi-copper Oxidase That Confers Copper Tolerance in Escherichia coli
resolves10.1074/jbc.M104122200
The Independent cue and cusSystems Confer Copper Tolerance during Aerobic and Anaerobic Growth inEscherichia coli
resolves10.1002/tcr.20125
Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
resolves10.1021/ja953621e
Chemical and Spectroscopic Definition of the Peroxide-Level Intermediate in the Multicopper Oxidases: Relevance to the Catalytic Mechanism of Dioxygen Reduction to Water
resolves10.1093/oxfordjournals.jbchem.a002942
A Novel Mixed Valence Form of Rhus vernicifera Laccase and Its Reaction with Dioxygen to Give a Peroxide Intermediate Bound to the Trinuclear Center
resolves10.1074/jbc.M808468200
Four-electron Reduction of Dioxygen by a Multicopper Oxidase, CueO, and Roles of Asp112 and Glu506 Located Adjacent to the Trinuclear Copper Center
resolves10.1021/bi0476836
Point Mutations at the Type I Cu Ligands, Cys457 and Met467, and at the Putative Proton Donor, Asp105, in <i>Myrothecium verrucaria</i> Bilirubin Oxidase and Reactions with Dioxygen
resolves10.1021/ja073905m
Spectroscopic and Kinetic Studies of Perturbed Trinuclear Copper Clusters: The Role of Protons in Reductive Cleavage of the O−O Bond in the Multicopper Oxidase Fet3p
resolves10.1074/jbc.274.46.32718
Spectroscopic and Kinetic Studies on the Oxygen-centered Radical Formed during the Four-electron Reduction Process of Dioxygen byRhus vernicifera Laccase
resolves10.1021/ja0114052
Nature of the Intermediate Formed in the Reduction of O<sub>2</sub> to H<sub>2</sub>O at the Trinuclear Copper Cluster Active Site in Native Laccase
resolves10.1021/ja046380w
Spectroscopic Demonstration of a Large Antisymmetric Exchange Contribution to the Spin-Frustrated Ground State of a <i>D</i><sub>3</sub> Symmetric Hydroxy-Bridged Trinuclear Cu(II) Complex: Ground-to-Excited State Superexchange Pathways
resolves10.1186/1472-6807-7-60
Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases
resolves10.1016/j.jmb.2008.11.024
The Structure of the Small Laccase from Streptomyces coelicolor Reveals a Link between Laccases and Nitrite Reductases
resolves10.1073/pnas.052710499
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in
<i>Escherichia coli</i>
resolves10.1016/j.jmb.2007.07.041
Structure and Function of the Engineered Multicopper Oxidase CueO from Escherichia coli—Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site
resolves10.1073/pnas.0902127106
Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase
resolves10.1016/j.febslet.2010.08.018
ATR‐FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase
resolves10.1021/ja00255a032
X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen
resolves10.1021/ja073947a
Electronic Structure of the Peroxy Intermediate and Its Correlation to the Native Intermediate in the Multicopper Oxidases: Insights into the Reductive Cleavage of the O−O Bond
resolves10.1073/pnas.0705137104
The two oxidized forms of the trinuclear Cu cluster in the multicopper oxidases and mechanism for the decay of the native intermediate
resolves10.1107/S0907444909011950
Structure of native laccase from<i>Trametes hirsuta</i>at 1.8 Å resolution
resolves10.1016/S0076-6879(97)76066-X
[20] Processing of X-ray diffraction data collected in oscillation mode
resolves10.1107/S0907444996012255
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
resolves10.1038/355472a0
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
resolves10.1093/nar/gkh398
MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes
What this badge says. CiteStamped means the CHECKABLE references of this
work were clean at the dated check: each resolved to a known work in a public registry, and none
carried a retraction notice at that time. It says nothing about the quality, findings,
or importance of the work itself, and nothing about references deposited without a DOI.
checked 2026-07-22 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record
Embed this badge
Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.
<a href="https://citestamp.com/citestamped/10.1002/anie.201107739"><img src="https://citestamp.com/citestamped/10.1002/anie.201107739/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[](https://citestamp.com/citestamped/10.1002/anie.201107739)