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Interaction of Bioactive Coomassie Brilliant Blue G with Protein: Insights from Spectroscopic Methods

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What this work says

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

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Quantitation of electrophoretically separated proteins in the submicrogram range by dye elution
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A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
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Principles of Fluorescence Spectroscopy
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Principles of Fluorescence Spectroscopy
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New Trends in Fluorescence Spectroscopy
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Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study
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Quantitative studies of the structure of proteins in solution by fourier-transform infrared spectroscopy
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Interaction of wogonin with bovine serum albumin
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Changes of serum albumin affinity for aspirin induced by fatty acid
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Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
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Interaction of BSA with proflavin: A spectroscopic approach
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Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin
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18β-Glycyrrhetinic acid interaction with bovine serum albumin
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Effect of temperature on the methotrexate – BSA interaction: Spectroscopic study
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Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy
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Interaction of the irisflorentin with bovine serum albumin: A fluorescence quenching study
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Human serum albumin interaction with paraquat studied using spectroscopic methods
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Rectification of excitation with bathochromic shift induced by intense absorption of organic ligands during emission measurement of Eu(III) complex
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Spectroscopic studies on the interaction of Congo Red with bovine serum albumin
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/s0065-3233(08)60640-3openalex-snapshot
Structure of Serum Albumin
inferredcites →https://doi.org/10.1017/s0033583502003815openalex-snapshot
What vibrations tell about proteins
inferredcites →https://doi.org/10.1021/bi00514a017openalex-snapshot
Thermodynamics of protein association reactions: forces contributing to stability
inferredcites →https://doi.org/10.1021/bi00642a024openalex-snapshot
Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin
inferredcites →https://doi.org/10.1021/j100546a014openalex-snapshot
Fluorescence quenching of indole and model micelle systems
inferredcites →https://doi.org/10.1073/pnas.0902531106openalex-snapshot
Systemic administration of an antagonist of the ATP-sensitive receptor P2X7 improves recovery after spinal cord injury
inferredcites →https://doi.org/10.1117/1.2747623openalex-snapshot
Human serum albumin and quercetin interactions monitored by time-resolved fluorescence: evidence for enhanced discrete rotamer conformations
inferredcites →https://doi.org/10.1126/science.2374930openalex-snapshot
Structure of Human Serum Albumin
inferredcites →https://doi.org/10.1159/000138988openalex-snapshot
Trityl Dyes Patent Blue V and Brilliant Blue G – Clinical Relevance and in vitro Analysis of the Function of the Outer Blood-Retinal Barrier
inferredcites →https://doi.org/10.1211/0022357991772079openalex-snapshot
Determination of the Affinity of Drugs toward Serum Albumin by Measurement of the Quenching of the Intrinsic Tryptophan Fluorescence of the Protein
inferredcites →https://doi.org/10.1248/bpb.25.695openalex-snapshot
Practical Aspects of the Ligand-Binding and Enzymatic Properties 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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Structural insights into the binding mode and conformational changes of BSA induced by bixin and crocin
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