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A biophysical probe on the binding of 2-mercaptothioazoline to bovine hemoglobin

https://doi.org/10.1007/s11356-018-3405-0
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1 of 37 checkable references need attention · checked 2026-07-23

At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.

2 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

References needing attention

does not resolve to a known work10.1254/jjp.58.201
The 36 checked references that resolve
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Electrochemical studies of rutin interacting with hemoglobin and determination of hemoglobin
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Interaction of toxic azo dyes with heme protein: Biophysical insights into the binding aspect of the food additive amaranth with human hemoglobin
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Influence of Dietary Iodine on Drug-induced Hypothyroidism in the Rat
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resolves10.1021/ie0306729
Decomposition of 2-Mercaptothiazoline in an Aqueous Solution by Ozonation with UV Radiation
resolves10.1021/ie040091z
Kinetics of Ozonation of 2-Mercaptothiazoline in an Electroplating Solution
resolves10.1016/j.chemosphere.2004.02.001
Decomposition of 2-mercaptothiazoline in aqueous solution by ozonation
resolves10.1016/j.jhazmat.2010.04.110
Toxic interaction mechanism between oxytetracycline and bovine hemoglobin
resolves10.1080/00387010.2017.1334001
Mechanism of the toxicological interactions of decabrominated diphenyl ether with hemoglobin
resolves10.1016/S0043-1354(97)00332-1
Analysis of the ozonation of 2-mercaptobenzothiazole in water and tannery wastewater using sum parameters, liquid- and gas chromatography and capillary electrophoresis
resolves10.1021/ci3001277
ZINC: A Free Tool to Discover Chemistry for Biology
resolves10.3389/fchem.2016.00050
A Study of the Interaction of Bovine Hemoglobin with Synthetic Dyes Using Spectroscopic Techniques and Molecular Docking
resolves10.1016/j.jphotobiol.2016.08.031
Probing the binding of anticancer drug topotecan with human hemoglobin: Structural and thermodynamic studies
resolves10.1021/bi00745a021
Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale
resolves10.1002/bio.2510
A probe to study the toxic interaction of tartrazine with bovine hemoglobin at the molecular level
resolves10.1016/j.saa.2014.09.051
Studies of the interaction between FNC and human hemoglobin: A spectroscopic analysis and molecular docking
resolves10.1016/j.fct.2013.04.048
Investigation on the interaction of the toxicant, gentian violet, with bovine hemoglobin
resolves10.1038/physci231064a0
Synchronized Excitation of Fluorescence Emission Spectra
resolves10.1016/j.fct.2011.09.011
Binding of Sudan II and Sudan IV to bovine serum albumin: Comparison studies
resolves10.1002/jcc.21256
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resolves10.1038/185416a0
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resolves10.1016/j.saa.2011.04.078
Multiple and sequential charge transfer interactions occurring in situ: A redox reaction of thiazolidine-2-thione with 2,3-dichloro-5,6-dicyano-1,4-benzoquinone
resolves10.1016/j.saa.2010.11.019
In vitro simulation of the chemical scenario of the action of an anti-thyroid drug: Charge transfer interaction of thiazolidine-2-thione with iodine
resolves10.1021/bi00514a017
Thermodynamics of protein association reactions: forces contributing to stability
resolves10.1016/j.jcis.2017.02.035
Binding interaction of sodium-N-dodecanoyl sarcosinate with hemoglobin and myoglobin: Physicochemical and spectroscopic studies with molecular docking analysis
resolves10.1016/j.ijbiomac.2012.05.013
Characterization of diadzein–hemoglobin binding using optical spectroscopy and molecular dynamics simulations
resolves10.1016/j.jphotobiol.2014.01.001
Exploring the biophysical aspects and binding mechanism of thionine with bovine hemoglobin by optical spectroscopic and molecular docking methods
resolves10.1016/j.electacta.2008.03.055
Investigation of adsorption and inhibitive effect of 2-mercaptothiazoline on corrosion of mild steel in hydrochloric acid media
resolves10.1006/abio.2000.4880
Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
resolves10.1007/s11356-015-5035-0
Molecular mechanism of copper–zinc superoxide dismutase activity change exposed to N-acetyl-l-cysteine-capped CdTe quantum dots-induced oxidative damage in mouse primary hepatocytes and nephrocytes
resolves10.1016/j.etap.2017.06.008
Study on the interaction between typical phthalic acid esters (PAEs) and human haemoglobin (hHb) by molecular docking
resolves10.1021/j100809a020
OXYGEN QUENCHING OF FLUORESCENCE IN SOLUTION: AN EXPERIMENTAL STUDY OF THE DIFFUSION PROCESS
resolves10.1007/s11356-018-1378-7
Probing the toxic mechanism of bisphenol A with acid phosphatase at the molecular level
resolves10.1021/jp904004w
Probing the Interaction of Magnetic Iron Oxide Nanoparticles with Bovine Serum Albumin by Spectroscopic Techniques
resolves10.1016/j.fct.2013.12.047
Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin
The 2 references without a DOI — listed, not checked
no DOI — not checkedNaeeminejad S, Assaran Darban R, Beigoli S, Saberi MR, Chamani J (2016) Studying the interaction between three synthesized heterocyclic sulfonamide compounds with hemoglobin by spectroscopy and molecular modeling techniques. J Biomol Struct Dyn 35:1–18
no DOI — not checkedZhang H, Liu Y, Liu R, Liu C, Chen Y (2014) Molecular mechanism of lead-induced superoxide dismutase inactivation in zebrafish livers. J Phys Chem B 118:14820–14826
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.

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