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Chirascan Citations (10k+ and counting)

Recommended Publications

Chirascan in Biotherapeutic Development Citations:

  1. Barnett, Balakrishnan, Chennamsetty, Hoffman, Bongers, Tao, Huang, et al. 2019.
    “Probing the Tryptophan Environment in Therapeutic Proteins: Implications for Higher Order Structure on Tryptophan Oxidation.”
    Journal of Pharmaceutical Sciences 108: 1944–52.
    https://doi.org/10.1016/j.xphs.2018.12.027.
    Keywords: Automated Circular Dichroism, Higher Order Structure, Tertiary Structure, Biotherapeutic Antibodies
  2. Barnett, Balakrishnan, Chennamsetty, Meengs, Meyer, Bongers, Ludwig, et al. 2018.
    “Enhanced Precision of Circular Dichroism Spectral Measurements Permits Detection of Subtle Higher Order Structural Changes in Therapeutic Proteins.”
    Journal of Pharmaceutical Sciences 107: 2559–69.
    https://doi.org/10.1016/j.xphs.2018.06.007.
    Keywords: Automated Circular Dichroism, Higher Order Structure, Tertiary Structure, Biotherapeutic Antibodies.
  3. Bommana, Chai, Schöneich, Weiss, and Majumdar. 2018.
    “Understanding the Increased Aggregation Propensity of a Light-Exposed IgG1 Monoclonal Antibody Using Hydrogen Exchange Mass Spectrometry, Biophysical Characterization, and Structural Analysis.”
    Journal of Pharmaceutical Sciences 107: 1498–1511.
    https://doi.org/10.1016/j.xphs.2018.01.017.
    Keywords: Automated Circular Dichroism, Higher Order Structure, Tertiary Structure, Biotherapeutic Antibodies.
  4. Bönisch, Sellmann, Maresch, Halbig, Becker, Toleikis, Hock, and Rüker. 2017.
    “Novel CH1:CL Interfaces That Enhance Correct Light Chain Pairing in Heterodimeric Bispecific Antibodies.”
    Protein Engineering, Design and Selection 30: 685–96.
    https://doi.org/10.1093/protein/gzx044.
    Keywords: Bispecific Antibodies, Interface Mutations.
  5. Egbu, van der Walle, Brocchini, and Williams. 2020.
    “Inhibiting the Fibrillation of a GLP-1-like Peptide.”
    International Journal of Pharmaceutics 574 (January): 118923.
    https://doi.org/10.1016/j.ijpharm.2019.118923.
    Keywords: Therapeutic Peptides, Formulation, Fibrillation, Excipients.
  6. Hickey, Toprani, Kaur, Mishra, Goel, Oganesyan, Lees, Sitrin, Joshi, and Volkin. 2018.
    “Analytical Comparability Assessments of 5 Recombinant CRM 197 Proteins From Different Manufacturers and Expression Systems.”
    Journal of Pharmaceutical Sciences 107: 1806–19.
    https://doi.org/10.1016/j.xphs.2018.03.002.
    Keywords: Conjugate
    Vaccines, Higher Order Structure, 6-Cell Turret, Thermal Denaturation.
  7. Hutterer, Polozova, Kuhns, McBride, Cao, and Liu. 2019.
    “Assessing Analytical and Functional Similarity of Proposed
    Amgen Biosimilar ABP 980 to Trastuzumab.”
    BioDrugs 33: 321–33.
    https://doi.org/10.1007/s40259-019-00350-9.
    Keywords: Biosimilars, Antibody Therapeutics, Tertiary Structure, Higher Order Structure.
  8. Jeong, Jeong, Son, Kwon, Jung, Song, Hwang, and Lee. 2018.
    “Comprehensive Physicochemical and Biological Characterization of the Proposed Biosimilar Darbepoetin Alfa, LBDE, and Its Originator Darbepoetin Alfa, NESP ®.”
    BioDrugs 32: 153–68.
    https://doi.org/10.1007/s40259-018-0272-7.
    Keywords: Biosimilars, Higher Order Structure, Tertiary Structure.
  9. J. Lee, Kang, Bae, Kim, Lee, Lim, Choo, and Chang. 2018.
    “Evaluation of Analytical Similarity between Trastuzumab
    Biosimilar CT-P6 and Reference Product Using Statistical Analyses.”
    MAbs 10: 547–71.
    https://doi.org/10.1080/19420862.2018.1440170. 
    Keywords: Biosimilars, Antibody Therapeutics, Higher Order Structure.
  10. K. H. Lee, Lee, Bae, Kim, Kang, Kim, Lee, et al. 2018.
    “Analytical Similarity Assessment of Rituximab Biosimilar CT-P10
    to Reference Medicinal Product.”
    MAbs 10: 380–96.
    https://doi.org/10.1080/19420862.2018.1433976.
    Keywords: Biosimilars, Antibody Therapeutics, Higher Order Structure.
  11. Liu, Eris, Li, Cao, and Kuhns. 2016.
    “Assessing Analytical Similarity of Proposed Amgen Biosimilar ABP 501 to Adalimumab.”
    BioDrugs 30: 321–38.
    https://doi.org/10.1007/s40259-016-0184-3.
    Keywords: Higher Order Structure, Biotherapeutics, Biosimilar.
  12. McAvan, Bowsher, Powell, O’Hara, Spitali, Goodacre, and Doig. 2020.
    “Raman Spectroscopy to Monitor Post-Translational Modifications and Degradation in Monoclonal Antibody Therapeutics.”
    Analytical Chemistry 92:10381–89.
    https://doi.org/10.1021/acs.analchem.0c00627.
    Keywords: Automated Circular Dichroism, Higher Order Structure, Tertiary Structure, Biotherapeutic Antibodies.
  13. Miao, Fan, Zhao, Ding, Liu, Wang, and Tan. 2017.
    “Physicochemical and Biological Characterization of the Proposed Biosimilar Tocilizumab.”
    BioMed Research International 2017: 1–13.
    https://doi.org/10.1155/2017/4926168.
    Keywords: Higher Order Structure, Biotherapeutics, Biosimilar.
  14. Rowe, Flynn, Wooten, Noufer, Cancel, Zhang, Subramony, Pechenov, and Wang. 2018.
    “Submicron Aggregation of Chemically Denatured Monoclonal Antibody.”
    Molecular Pharmaceutics 15: 4710–21.
    https://doi.org/10.1021/acs.molpharmaceut.8b00690. 
    Keywords: Antibody Therapeutics, Aggregation, Secondary Structure.
  15. Saricay, de Kort, Yigit-Gercek, and Dirksen. 2021.
    “A Multi-Angular View on the Impact of Protein Unfolding on Biophysical Structural Data.”
    Analytical Biochemistry 630 (October): 114331.
    https://doi.org/10.1016/j.ab.2021.114331.
    Keywords: Antibodies, Antibody Drug Conjugates, Higher Order Structure.
  16. Shah, Singh, and Mallela. 2018.
    “Effect of Chemical Oxidation on the Higher Order Structure, Stability, Aggregation, and Biological Function of Interferon Alpha-2a: Role of Local Structural Changes Detected by 2D NMR.”
    Pharmaceutical Research 35: 232.
    https://doi.org/10.1007/s11095-018-2518-y.
    Keywords: Far- and Near-UV, Higher Order Structure of a biotherapeutic, Stability assessed by chemical unfolding.
  17. Singh, Bandi, Jones, and Mallela. 2017.
    “Effect of Polysorbate 20 and Polysorbate 80 on the Higher-Order Structure of a Monoclonal Antibody and Its Fab and Fc Fragments Probed Using 2D Nuclear Magnetic Resonance Spectroscopy.”
    Journal of Pharmaceutical Sciences 106: 3486–98.
    https://doi.org/10.1016/j.xphs.2017.08.011.
    Keywords: Antibodies, Excipients, Higher Order Structure, Thermal Denaturation.
  18. Toughiri, Wu, Ruiz, Huang, Crissman, Dickey, Froning, Conner, Cujec, and Demarest. 2016.
    “Comparing Domain Interactions within Antibody Fabs with Kappa and Lambda Light Chains.”
    MAbs 8: 1276–85
    https://doi.org/10.1080/19420862.2016.1214785.
    Keywords: Automated Circular Dichroism, Chemical Denaturation, Stability, Antibody Therapeutics.

Chirascan in Citations from Academia:

  1. Al-Ahmady, Al-Jamal, Bossche, Bui, Drake, Mason, and Kostarelos. 2012.
    “Lipid-Peptide Vesicle Nanoscale Hybrids for Triggered Drug Release by Mild Hyperthermia in Vitro and in Vivo.”
    ACS Nano 6: 9335–46.
    https://doi.org/10.1021/nn302148p.
    Keywords: Amphiphilic Peptides, Liposomes, Thermal Denaturation,
    Continuous Multi-Wavelength T-Ramp, Global Thermodynamic Analysis.
  2. Berdnikova, Sosnin, Fedorova, and Ihmels. 2018.
    “Governing the DNA-Binding Mode of Styryl Dyes by the Length of Their Alkyl Substituents-from Intercalation to Major Groove Binding.”
    Organic and Biomolecular Chemistry 16:
    545–54.
    https://doi.org/10.1039/c7ob02736b.
    Keywords: DNA; Dyes; Ligand Binding; Linear Dichroism; Couette Cell.
  3. Elmer-Dixon and Bowler. 2017.
    “Site A-Mediated Partial Unfolding of Cytochrome c on Cardiolipin Vesicles Is Species-Dependent and Does Not Require Lys72.”
    Biochemistry 56: 4830–39.
    https://doi.org/10.1021/acs.biochem.7b00694.
    Keywords: Chemical Unfolding, Scanning Fluorescence
    Monochromator, Titrator, Cytochrome c, Heme Soret Band; Lipid Vesicles; Protein Mutants.
  4. Elmer-Dixon and Bowler. 2018.
    “Electrostatic Constituents of the Interaction of Cardiolipin with Site A of Cytochrome C.”
    Biochemistry 57:5683–95.
    https://doi.org/10.1021/acs.biochem.8b00704.
    Keywords: Protein-Lipid Vesicle-Interaction, Near-UV
    and UV/Vis CD, Fluorescence, Chemical Unfolding.
  5. Grunér, Paananen, Szilvay, and Linder. 2017.
    “The Dynamics of Multimer Formation of the Amphiphilic Hydrophobin Protein HFBII.”
    Colloids and Surfaces B: Biointerfaces 155 (July): 111–17.
    https://doi.org/10.1016/j.colsurfb.2017.03.057.
  6. Hedegaard, Derbas, Lind, Kasimova, Christensen, Michaelsen, Campbell, et al. 2018.
    “Fluorophore Labeling of a Cell-Penetrating Peptide Significantly Alters the Mode and Degree of Biomembrane Interaction.”
    Scientific Reports 8:6327.
    https://doi.org/10.1038/s41598-018-24154-z.
    Keywords: Cell-penetrating Peptides, Induced Folding, Lipid Vesicles.
  7. Hughes, Longo, Phillips-Jones, and Hussain. 2017.
    “Characterisation of the Selective Binding of Antibiotics Vancomycin and Teicoplanin by the VanS Receptor Regulating Type A Vancomycin Resistance in the Enterococci.”
    Biochimica et Biophysica Acta - General Subjects 1861: 1951–59.
    https://doi.org/10.1016/j.bbagen.2017.05.011.
  8. Jana, Jung, and Sheves. 2020.
    “The Chirality Origin of Retinal-Carotenoid Complex in Gloeobacter Rhodopsin: A Temperature-Dependent Excitonic Coupling.”
    Scientific Reports 10: 13992.
    https://doi.org/10.1038/s41598-020-70697-5.
    Keywords: Rhodopsins, UV/Vis CD, Retinal Proteins, Exciton Coupling.
  9. Kries, Kellner, Kamileen, and O’Connor. 2017.
    “Inverted Stereocontrol of Iridoid Synthase in Snapdragon.”
    Journal of Biological Chemistry 292: 14659–67.
    https://doi.org/10.1074/jbc.M117.800979.
  10. Kriznik, Libiad, Le Cordier, Boukhenouna, Toledano, and Rahuel-Clermont. 2020.
    “Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.”
    ACS Catalysis 10: 3326–39.
    https://doi.org/10.1021/acscatal.9b04471.
    Keywords: Redox Enzymes, Stopped-Flow, Kinetics, Fluorescence, Far- and Near-UV CD.
  11. Lei and Bowler. 2018.
    “Humanlike Substitutions to Ω-Loop D of Yeast Iso-1-Cytochrome c Only Modestly Affect Dynamics and Peroxidase Activity.”
    Journal of Inorganic Biochemistry 183 (February): 146–56.
    https://doi.org/10.1016/j.jinorgbio.2018.02.022.
    Keywords: Chemical Unfolding; Protein Mutants; Titrator;
    Stopped-Flow (SX20).
  12. Liu, Shen, Li, Gong, Chen, Chen, and Cai. 2017.
    “Ratiometric Fluorescence Sensor for the MicroRNA Determination by Catalyzed Hairpin Assembly.”
    ACS Sensors 2: 1430–34.
    https://doi.org/10.1021/acssensors.7b00313.
    Keywords: DNA, Biosensor, microRNA, G-Quadruplex.
  13. Narang, Singh, and Mukhopadhyay. 2017.
    “Stepwise Unfolding of Human β2-Microglobulin into a Disordered Amyloidogenic Precursor at Low PH.”
    European Biophysics Journal 46: 65–76.
    https://doi.org/10.1007/s00249-016-1138-x.
    Keywords: Aggregation Kinetics, Amyloid Fibrils, Thermal Denaturation, Mutants, Stopped-Flow.
  14. Nejat Dehkordi and Akerman. 2018.
    “Interaction of DNA with Water Soluble Complex of Nickle and Formation of DNA Cross-Links.”
    Chemico-Biological Interactions 282 (February): 55–62.
    https://doi.org/10.1016/j.cbi.2018.01.007.
    Keywords: DNA, Intercalating Ligand, Linear Dichroism, Couette Cell, Organometallic Complex.
  15. Nwaji, Mack, and Nyokong. 2018.
    “Photophysical and Strong Optical Limiting Properties of Ball-Type Phthalocyanines Dimers and Their Monomeric Analogues.”
    Journal of Photochemistry and Photobiology A: Chemistry 352
    (February): 73–85.
    https://doi.org/10.1016/j.jphotochem.2017.10.045.
    Keywords: Optical Materials, Magnetic Circular Dichroism, Small Molecules.
  16. Perez-Riba, Komives, Main, and Itzhaki. 2019.
    “Decoupling a Tandem-Repeat Protein: Impact of Multiple Loop Insertions on a Modular Scaffold.”
    Scientific Reports 9: 15439.
    https://doi.org/10.1038/s41598-019-49905-4.
    Keywords: Peptides, Chemical Denaturation, Titration.
  17. Qin, Song, Dai, Chan, Chan, and Guo. 2018.
    “Single‐Turnover Kinetics Reveal a Distinct Mode of Thiamine Diphosphate‐Dependent Catalysis in Vitamin K Biosynthesis.”
    ChemBioChem 19: 1514–22.
    https://doi.org/10.1002/cbic.201800143.
    Keywords: Stopped-Flow, Enzyme Kinetics, Reaction Intermediates, Biosynthesis.
  18. Raasakka, Myllykoski, Laulumaa, Lehtimäki, Härtlein, Moulin, Kursula, and Kursula. 2015.
    “Determinants of Ligand Binding and Catalytic Activity in the Myelin Enzyme 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase.”
    Scientific Reports 5: 16520.
    https://doi.org/10.1038/srep16520.
    Keywords: Protein Mutants, Thermal Denaturation,
    Continuous Multi-Wavelength T-Ramp, Global Thermodynamic Analysis.
  19. Roeters, Iyer, Pletikapiä, Kogan, Subramaniam, and Woutersen. 2017.
    “Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy.”
    Scientific Reports 7 (January): 41051.
    https://doi.org/10.1038/srep41051.
    Keywords: Amyloid Fibrils, Intrinsically Disordered Proteins.
  20. Ropiak, Lachmann, Ramsay, Green, and Mueller-Harvey. 2017.
    “Identification of Structural Features of Condensed Tannins That Affect Protein Aggregation.”
    Edited by Jamshidkhan Chamani. PLoS ONE 12: e0170768.
    https://doi.org/10.1371/journal.pone.0170768.
  21. Roth, Schoelkopf, Huwyler, and Puchkov. 2018.
    “Functionalized Calcium Carbonate Microparticles for the Delivery of Proteins.”
    European Journal of Pharmaceutics and Biopharmaceutics 122 (January): 96–103.
    https://doi.org/10.1016/j.ejpb.2017.10.012.
  22. Sani, Carne, Overall, Poulhazan, and Separovic. 2017.
    “One Pathogen Two Stones: Are Australian Tree Frog Antimicrobial Peptides Synergistic against Human Pathogens?”
    European Biophysics Journal 46: 639–46.
    https://doi.org/10.1007/s00249-017-1215-9.
    Keywords: Antimicrobial Peptides, Lipid Vesicles, Live Cells.
  23. Scalabrin, Palumbo, and Richter. 2017.
    “Highly Improved Electrospray Ionization-Mass Spectrometry Detection of GQuadruplex-Folded Oligonucleotides and Their Complexes with Small Molecules.”
    Analytical Chemistry 89: 8632–37.
    https://doi.org/10.1021/acs.analchem.7b01282.
    Keywords: G-Quadruplex, DNA Stability, Drug Development.
  24. Schiavone, Pirrone, Guetschow, Mangion, and Makarov. 2019.
    “Combination of Circular Dichroism Spectroscopy and
    Size-Exclusion Chromatography Coupled with HDX-MS for Studying Global Conformational Structures of Peptides
    in Solution.”
    Talanta 194 (March): 177–82.
    https://doi.org/10.1016/j.talanta.2018.09.077.
    Keywords: Correlation of CD and SEC-HDX-MS as two orthogonal techniques.
  25. Selegård, Aronsson, Brommesson, Dånmark, and Aili. 2017.
    “Folding Driven Self-Assembly of a Stimuli-Responsive
    Peptide-Hyaluronan Hybrid Hydrogel.”
    Scientific Reports 7: 7013.
    https://doi.org/10.1038/s41598-017-06457-9.
  26. Shen, Du, Qiao, Kong, Yuan, Zhang, Wu, Li, and Wu. 2018.
    “Biophysical and Structural Characterization of the Thermostable WD40 Domain of a Prokaryotic Protein, Thermomonospora Curvata PkwA.”
    Scientific Reports 8:12965.
    https://doi.org/10.1038/s41598-018-31140-y.
    Keywords: Far- and Near-UV CD, Stopped-Flow, Fluorescence, Thermal and Chemical Stability.
  27. Slator, Molphy, McKee, Long, Brown, and Kellett. 2018.
    “Di-Copper Metallodrugs Promote NCI-60 Chemotherapy via
    Singlet Oxygen and Superoxide Production with Tandem TA/TA and AT/AT Oligonucleotide Discrimination.”
    Nucleic Acids Research 46: 2733–50.
    https://doi.org/10.1093/nar/gky105.
  28. Varizhuk, Ischenko, Tsvetkov, Novikov, Kulemin, Kaluzhny, Vlasenok, Naumov, Smirnov, and Pozmogova. 2017.
    “The Expanding Repertoire of G4 DNA Structures.”
    Biochimie 135 (April): 54–62.
    https://doi.org/10.1016/j.biochi.2017.01.003.
  29. J. Wei, Guo, Cao, Kou, Xu, Górecki, Di Bari, Pescitelli, and Gao. 2018.
    “Polyoxygenated Cyathane Diterpenoids from the Mushroom Cyathus Africanus, and Their Neurotrophic and Anti-Neuroinflammatory Activities.”
    Scientific Reports 8: 2175.
    https://doi.org/10.1038/s41598-018-20472-4.
  30. Y. Wei, Wahome, Kumar, Whitaker, Picking, and Middaugh. 2018.
    “Effect of Phosphate Ion on the Structure of Lumazine Synthase, an Antigen Presentation System From Bacillus Anthracis.”
    Journal of Pharmaceutical Sciences 107: 814–23.
    https://doi.org/10.1016/j.xphs.2017.10.013.
    Keywords: Vaccines, Thermal Denaturation, 6-Cell Turret.
  31. Wu, Zhou, Yin, Hang, Li, Ågren, Yi, Zhang, and Zhu. 2017.
    “Helical Self-Assembly-Induced Singlet–Triplet Emissive Switching in a Mechanically Sensitive System”
    Journal of the American Chemical Society 139:785–91.
    https://doi.org/10.1021/jacs.6b10550.
  32. Yang, Zhang, Wang, Yu, and Wei. 2017.
    “A Novel Chimeric Lysin with Robust Antibacterial Activity against Planktonic and Biofilm Methicillin-Resistant Staphylococcus Aureus.”
    Scientific Reports 7 (January): 40182.
    https://doi.org/10.1038/srep40182.
  33. Zavyalova, Legatova, Alieva, Zalevsky, Tashlitsky, Arutyunyan, and Kopylov. 2019.
    “Putative Mechanisms Underlying High Inhibitory Activities of Bimodular DNA Aptamers to Thrombin.”
    Biomolecules 9: 41.
    https://doi.org/10.3390/biom9020041.
    Keywords: Aptamers, G-Quadruplexes, Stability, Thermal Melting.
  34. Zhao, Wei, Liu, Yao, Xu, Wei, Wang, Wang, and Chen. 2016.
    “Structural Insights on PHA Binding Protein PhaP from Aeromonas Hydrophila.”
    Scientific Reports 6: 39424.
    https://doi.org/10.1038/srep39424. Keywords: Single-Amino Acid Mutants, Thermal Denaturation.
  35. Zhao, Yao, Chen, Wang, and Chen. 2017.
    “Modelling of Microbial Polyhydroxyalkanoate Surface Binding Protein PhaP for Rational Mutagenesis.”
    Microbial Biotechnology 10: 1400–1411.
    https://doi.org/10.1111/1751-7915.12820.
    Keywords: Single-Amino Acid Mutants, Thermal Denaturation.
  36. Zuberek and Stelmachowska. 2017.
    “Tryptophan Residues from Cap Binding Slot in EIF4E Family Members: Their Contributions to Near-UV Circular Dichroism Spectra.”
    Journal of Physical Chemistry & Biophysics 07: 250.
    https://doi.org/10.4172/2161-0398.1000250.

Stopped-Flow Citations (6K+ and counting)

Recommeded Publications

  1. Posson, David J et al. 2018.
    “Stopped-Flow Fluorometric Ion Flux Assay for Ligand-Gated Ion Channel Studies.”
    Methods in molecular biology (Clifton, N.J.) vol. 1684: 223-235.
    https://doi.org/10.1007/978-1-4939-7362-0_17.
    Keywords: Ion channel function, Stopped-flow assay, Liposomal ion flux assay, ANTS quenching, Thallium.
  2. Xin Peng, Xiangchao Wang, Wei Qi, Rongxin Su, Zhimin He 2016.
    "Affinity of rosmarinic acid to human serum albumin and its effect on protein conformation stability."
    Food Chemistry, Vol. 192: 178-187
    https://doi.org/10.1016/j.foodchem.2015.06.109
    Keywords: Rosmarinic acid; Human serum albumin; Multi-spectroscopic; Molecular docking; Molecular dynamics simulation.
  3. Nathaniel R. Beattie, Nicholas D. Keul, Tiffany N. Hicks Sirmans, Weston E. McDonald, Trevor M. Talmadge, Rahil Taujale, Natarajan Kannan, and Zachary A. Wood
    "
    Conservation of Atypical Allostery in C. elegans UDP-Glucose Dehydrogenase."
    ACS Omega 2019 4 (15), 16318-16329
    https://doi.org/10.1021/acsomega.9b01565
    Keywords: Conformation, Cooperativity, Crystal Structure, Defects, Peptides and Proteins
  4. Bibifatima Kaupbayeva, Hironobu Murata, Amber Lee Wilson, Krzysztof Matyjaszewski, Jonathan S. Minden, and Alan J. Russell 
    "Molecular Sieving on the Surface of a Nano-Armored Protein." 
    Biomacromolecules 2019 20 (3), 1235-1245
    https://doi.org/10.1021/acs.biomac.8b01651 
    Keywords: Conjugate Acid-Base Pairs, Ligands, Organic Compounds, peptides and Proteins, Polymers

  5. Karolina Dębowska, Dawid Dębski, Bartosz Michałowski, Agnieszka Dybala-Defratyka, Tomasz Wójcik, Radosław Michalski, Małgorzata Jakubowska, Anna Selmi, Renata Smulik, Łukasz Piotrowski, Jan Adamus, Andrzej Marcinek, Stefan Chlopicki, and Adam Sikora 
    "
    Characterization of Fluorescein-Based Monoboronate Probe and Its Application to the Detection of Peroxynitrite in Endothelial Cells Treated with Doxorubicin." 
    Chemical Research in Toxicology 2016 29 (5), 735-746
    https://doi.org/10.1021/acs.chemrestox.5b00431 
    Keywords: Anions, Flourescence, Oxidation, Oxides, Probes 
  6. Micael Paulino, Ignacio Pérez-Juste, María Magdalena Cid, José P. Da Silva, M. Manuela A. Pereira, and Nuno Basílio
    "2-Hydroxychalcone−β-Cyclodextrin Conjugate with pH-Modulated Photoresponsive Binding Properties."
    The Journal of Organic Chemistry 2022 87 (21), 14422-14432
    https://pubs.acs.org/doi/10.1021/acs.joc.2c01864 
    Keywords: Cavities, Circular Dichroism, Spectroscopy, Conformations, Irradiation, Titration
  7. Li Xu, György Csekő, and Attila K. Horváth
    "Autoinhibition by Iodide Ion in the Methionine–Iodine Reaction." 
    The Journal of Physical Chemistry A 2020 124 (29), 6029-6038
    https://doi.org/10.1021/acs.jpca.0c04271 
    Keywords: Anions, Ions, Kinetics, Monomers, peptides and Proteins

  8. Rodriguez. Roberto A., Chan. Ruth, Liang. Huiyun, Chen, Liao Y.,
    "Quantitative study of unsaturated transport of glycerol through aquaglyceroporin that has high affinity for glycerol."
    RSC Advances, 2020 10 (56)
    http://dx.doi.org/10.1039/D0RA05262K 
    Keywords: Kinetics, Biotechnology, Lipids, AQP3
  9. Johann. Kerstin, Svatunek. Dennis, Seidl. Christine, Rizzelli. Silvia, Bauer. Tobias A., Braun. Lydia, Koynov. Kaloian, Mikula. Hannes, Barz. Matthias
    "Tetrazine- and trans-cyclooctene-functionalised polypept(o)ides for fast bioorthogonal tetrazine ligation."
    Polymer Chemistry, 2020 11 (27), 1759-9954
    http://dx.doi.org/10.1039/D0PY00375A 
    Keywords: Ligation, Bioorthogonal, Polymer, Peptides, Chromatography, Spectroscopy, Fluorescence, Synthesis
  10. Chatterjee. Debabrata, Chrzanowska. Marta, Katafias. Anna, Oszajca. Maria, van Eldik. Rudi
    "RuIII(edta) complexes as molecular redox catalysts in chemical and electrochemical reduction of dioxygen and hydrogen peroxide: inner-sphere versus outer-sphere mechanism."
    RSC Advances, 2021 11 (35)
    http://dx.doi.org/10.1039/D1RA03293C 
    Keywords: Spectroscopy, Kinetics, Oxidation, Electrochemical
  11. Lomora. Mihai, Itel. Fabian, Dinu. Ionel Adrian, Palivan. Cornelia G.,
    "Selective ion-permeable membranes by insertion of biopores into polymersomes."
    Physical Chemistry Chemical Physics, 2015 17 (24), 1463-9076
    http://dx.doi.org/10.1039/C4CP05879H 
    Keywrods: Polymersomes, Ion, Synthetic, Fluorescence
  12. Held. Barbara, Tang. Hao, Natarajan. Palani, da Silva. Cassio Pacheco, de Oliveira Silva. Volnir, Bohne. Cornelia, Quina. Frank H.,
    "Cucurbit[7]uril inclusion complexation as a supramolecular strategy for color stabilization of anthocyanin model compounds."
    Photochemical & Photobiological Sciences, 2016 15 (6), 1474-905X
    http://dx.doi.org/10.1039/C6PP00060F 
    Keywords: Thermodynamic, Fluorescence, Stopped-Flow, Kinetics
  13. Peng. Weicheng, Maydew. Caden C., Kam. Hiu, Lynd. Jacob K., Tutol. Jasmine N., Phelps. Shelby M., Abeyrathna. Sameera, Meloni. Gabriele, Dodani. Sheel C.,
    "Discovery of a monomeric green fluorescent protein sensor for chloride by structure-guided bioinformatics."
    Chemical Science, 2022 13 (43), 2041-6520
    http://dx.doi.org/10.1039/D2SC03903F 
    Keywords: Fluorescence, Protein, Microscopy, Ion, Kinetics
  14. Petroff. John T., Dietzen. Noah M., Santiago-McRae. Ezry, Deng. Brett, Washington. Maya S., Chen. Lawrence J., Trent Moreland. K., Deng. Zengqin, Rau. Michael, Fitzpatrick. James A. J., Yuan. Peng, Joseph. Thomas T., Hénin. Jérôme, Brannigan. Grace, Cheng. Wayland W. L.,
    "Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation."
    Nature Communications, 2022 13 (1), 2041-1723
    https://doi.org/10.1038/s41467-022-34813-5
    Keywords: Phospholipid, Kinetic, Fluorescence, Anionic, Stopped-Flow