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An alternate mode of binding of the polyphenol quercetin with serum albumins when complexed with Cu(II)
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Zwischenmolekulare Energiewanderung und Fluoreszenz
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Binding of quercetin with human serum albumin: A critical spectroscopic study
inferredcites →https://doi.org/10.1002/chir.20794openalex-snapshot
Interactions between quercetin and Warfarin for albumin binding: A new eye on food/drug interference
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How to measure and predict the molar absorption coefficient of a protein
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Hidden Markov models that use predicted local structure for fold recognition: Alphabets of backbone geometry
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Combining local-structure, fold-recognition, and new fold methods for protein structure prediction
inferredcites →https://doi.org/10.1002/prot.20008openalex-snapshot
Evaluation of local structure alphabets based on residue burial
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SAM-T04: What is new in protein-structure prediction for CASP6
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Agonist–PPARγ interactions: Molecular modeling study with docking approach
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Inhibitory Effect of Quercetin Metabolites and Their Related Derivatives on Copper Ion-Induced Lipid Peroxidation in Human Low-Density Lipoprotein
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Influence of Metal Ions on Flavonoid Protection against Asbestos-Induced Cell Injury
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Interaction of Iron with Polyphenolic Compounds: Application to Antioxidant Characterization
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Principles of Fluorescence Spectroscopy
inferredcites →https://doi.org/10.1007/bf02708293openalex-snapshot
Fluorescence spectroscopic studies on binding of a flavonoid antioxidant quercetin to serum albumins
inferredcites →https://doi.org/10.1007/s00775-009-0486-8openalex-snapshot
DNA binding and oxidative DNA damage induced by a quercetin copper(II) complex: potential mechanism of its antitumor properties
inferredcites →https://doi.org/10.1016/0003-9861(80)90268-4openalex-snapshot
Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinamide fluorescence quenching
inferredcites →https://doi.org/10.1016/0006-2952(83)90262-9openalex-snapshot
Flavonoids, a class of natural products of high pharmacological potency
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Influence of the oral administration of excess copper on the immune response
inferredcites →https://doi.org/10.1016/0300-9084(91)90022-sopenalex-snapshot
Chlorpheniramine binding to human serum albumin by fluorescence quenching measurements
inferredcites →https://doi.org/10.1016/0308-8146(96)00065-9openalex-snapshot
Analysis and health effects of flavonoids
inferredcites →https://doi.org/10.1016/j.aca.2006.11.006openalex-snapshot
Interaction between quercetin–copper(II) complex and DNA with the use of the Neutral Red dye fluorophor probe
inferredcites →https://doi.org/10.1016/j.bmc.2005.12.034openalex-snapshot
Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR, and molecular modeling
inferredcites →https://doi.org/10.1016/j.colsurfb.2006.11.044openalex-snapshot
Hydrolytic cleavage of DNA by quercetin manganese(II) complexes
inferredcites →https://doi.org/10.1016/j.ejmech.2006.12.037openalex-snapshot
The consequences of scoring docked ligand conformations using free energy correlations
inferredcites →https://doi.org/10.1016/j.febslet.2011.09.005openalex-snapshot
Complex formation of rutin and quercetin with copper alters the mode of inhibition of Ribonuclease A
inferredcites →https://doi.org/10.1016/j.jlumin.2011.12.063openalex-snapshot
Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins
inferredcites →https://doi.org/10.1016/j.jpba.2004.08.021openalex-snapshot
Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin
inferredcites →https://doi.org/10.1016/j.jpba.2007.10.016openalex-snapshot
Probing the binding of morin to human serum albumin by optical spectroscopy
inferredcites →https://doi.org/10.1016/j.jphotochem.2004.05.017openalex-snapshot
The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods
inferredcites →https://doi.org/10.1016/j.molstruc.2004.11.081openalex-snapshot
Copper(II)–Quercetin complexes in aqueous solutions: spectroscopic and kinetic properties
inferredcites →https://doi.org/10.1016/j.molstruc.2006.03.051openalex-snapshot
Antioxidant flavonoids bind human serum albumin
inferredcites →https://doi.org/10.1016/j.molstruc.2008.04.050openalex-snapshot
Synthesis, characterization and investigation of antioxidant activity of cobalt–quercetin complex
inferredcites →https://doi.org/10.1016/j.molstruc.2008.08.008openalex-snapshot
Antioxidant property of quercetin–Cr(III) complex: The role of Cr(III) ion
inferredcites →https://doi.org/10.1016/j.saa.2008.07.004openalex-snapshot
Spectrometric and voltammetric studies of the interaction between quercetin and bovine serum albumin using warfarin as site marker with the aid of chemometrics
inferredcites →https://doi.org/10.1016/s0006-291x(02)02667-0openalex-snapshot
The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study
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Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods
inferredcites →https://doi.org/10.1016/s0026-895x(25)10691-3openalex-snapshot
The Characterization of Two Specific Drug Binding Sites on Human Serum Albumin
inferredcites →https://doi.org/10.1016/s0026-895x(25)10855-9openalex-snapshot
Further Characterization of Specific Drug Binding Sites on Human Serum Albumin
inferredcites →https://doi.org/10.1016/s0031-6997(24)01472-8openalex-snapshot
The Effects of Plant Flavonoids on Mammalian Cells:Implications for Inflammation, Heart Disease, and Cancer
inferredcites →https://doi.org/10.1016/s0031-6997(25)06849-8openalex-snapshot
Molecular aspects of ligand binding to serum albumin.
inferredcites →https://doi.org/10.1016/s0031-9422(00)00235-1openalex-snapshot
Advances in flavonoid research since 1992
inferredcites →https://doi.org/10.1016/s0162-0134(02)00469-5openalex-snapshot
Spectroscopic and structural study of complexes of quercetin with Al(III)
inferredcites →https://doi.org/10.1016/s0167-4838(01)00287-4openalex-snapshot
Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling
inferredcites →https://doi.org/10.1016/s0361-9230(01)00454-3openalex-snapshot
Copper in disorders with neurological symptoms: Alzheimer’s, Menkes, and Wilson diseases
inferredcites →https://doi.org/10.1016/s1386-1425(99)00284-xopenalex-snapshot
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inferredcites →https://doi.org/10.1021/bi00514a017openalex-snapshot
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inferredcites →https://doi.org/10.1021/bi00772a015openalex-snapshot
Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
inferredcites →https://doi.org/10.1021/bm900961eopenalex-snapshot
Site-Selective Binding of Human Serum Albumin by Palmatine: Spectroscopic Approach
inferredcites →https://doi.org/10.1021/ja01176a030openalex-snapshot
A Spectrophotometric Investigation of the Interaction of Iodine with Aromatic Hydrocarbons
inferredcites →https://doi.org/10.1021/jf050061mopenalex-snapshot
Covalent Binding of the Flavonoid Quercetin to Human Serum Albumin
inferredcites →https://doi.org/10.1021/jf060986hopenalex-snapshot
Iron Chelation by the Powerful Antioxidant Flavonoid Quercetin
inferredcites →https://doi.org/10.1021/np960040+openalex-snapshot
Natural Polyphenols (Vegetable Tannins) as Drugs: Possible Modes of Action
inferredcites →https://doi.org/10.1023/a:1007152927167openalex-snapshot
Antioxidative and anti-tumour activities of solid quercetin metal(II) complexes
inferredcites →https://doi.org/10.1023/a:1009238732287openalex-snapshot
Prooxidant action of aluminum Ion – Stimulation of iron-mediated lipid peroxidation by aluminum
inferredcites →https://doi.org/10.1023/a:1021254104012openalex-snapshot
Copper Chaperones for Cytochrome c Oxidase and Human Disease
inferredcites →https://doi.org/10.1038/358209a0openalex-snapshot
Atomic structure and chemistry of human serum albumin
inferredcites →https://doi.org/10.1042/bj3301173openalex-snapshot
Structural dependence of flavonoid interactions with Cu2+ ions: implications for their antioxidant properties
inferredcites →https://doi.org/10.1080/07391102.2002.10506804openalex-snapshot
Interaction of AZT with Human Serum Albumin Studied by Capillary Electrophoresis, FTIR and CD Spectroscopic Methods
inferredcites →https://doi.org/10.1093/protein/12.6.439openalex-snapshot
Crystal structure of human serum albumin at 2.5 Å resolution
inferredcites →https://doi.org/10.1093/toxsci/16.2.249openalex-snapshot
Influence of the Oral Administration of Excess Copper on the Immune Response
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.01049.xopenalex-snapshot
Preliminary Crystallographic Studies of Four Crystal forms of Serum Albumin
inferredcites →https://doi.org/10.1111/j.1440-1681.2008.04969.xopenalex-snapshot
COPPER AND ANGIOGENESIS: UNRAVELLING A RELATIONSHIP KEY TO CANCER PROGRESSION
inferredcites →https://doi.org/10.1177/108705710000500501openalex-snapshot
Fluorescence Polarization and Anisotropy in High Throughput Screening: Perspectives and Primer
inferredcites →https://doi.org/10.1179/135100004225003897openalex-snapshot
Antioxidant properties of complexes of flavonoids with metal ions
inferredcites →https://doi.org/10.1186/1472-6807-3-6openalex-snapshot
Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
inferredcites →https://doi.org/10.1562/2006-02-23-ra-811openalex-snapshot
Binding of Warfarin Influences the Acid‐Base Equilibrium of H242 in Sudlow Site I of Human Serum Albumin
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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