The DOI matches its Crossref record.
Milk β-lactoglobulin complexes with tea polyphenols
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 39
- Aguie-Beghin, 2008, Polyphenol–β-casein complexes at air/water interface and in solution: Effects of polyphenol structure, J. Agric. Food Chem., 56, 9600, 10.1021/jf801672x · doi:10.1021/jf801672x
- Ahmed Ouameur, 2006, An overview of drug binding to human serum albumin: Protein folding and unfolding, Cell Biochem. Biophys., 45, 203, 10.1385/CBB:45:2:203 · DOI
- Alexandropoulou, 2006, Effects of iron, ascorbate, meat and casein on the antioxidant capacity of green tea under conditions of in vitro digestion, Food Chem., 94, 359, 10.1016/j.foodchem.2004.11.023 · DOI
- Beauchemin, 2007, Polyamine analogues bind human serum albumin, Biomacromolecules, 8, 3177, 10.1021/bm700697a · doi:10.1021/bm700697a
- Bi, 2004, Investigation of the interaction between flavonoids and human serum albumin, J. Mol. Struct., 703, 37, 10.1016/j.molstruc.2004.05.026 · doi:10.1016/j.molstruc.2004.05.026
- Bourassa, 2010, Resveratrol. Genistein and curcumin bind bovine serum albumin, J. Phys. Chem. B, 114, 3348, 10.1021/jp9115996 · DOI · Paper page
- Byler, 1986, Examination of the secondary structure of proteins by deconvoluted FTIR spectra, Biopolymers, 25, 469, 10.1002/bip.360250307 · DOI · Paper page
- Charbonneau, 2010, Study on the interaction of cationic lipids with bovine serum albumin, J. Phys. Chem. B, 114, 1148, 10.1021/jp910077h · DOI · Paper page
- Collini, 2000, New insights on β-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay, Protein Sci., 9, 1968, 10.1110/ps.9.10.1968 · doi:10.1110/ps.9.10.1968
- De Fretias, 2001, Structural features of procyanidin interactions with salivary proteins, J. Agric. Food Chem., 49, 940, 10.1021/jf000981z · DOI · Paper page
- Dousseau, 1989, On the spectral subtraction of water from the FT-IR spectra of aqueous solutions of proteins, Appl. Spectrosc., 43, 538, 10.1366/0003702894202814 · DOI · Paper page
- Dubeau, 2010, Duel effect of milk on the antioxidant capacity of green, Darjeeling, and English breakfast teas, Food Chem., 122, 539, 10.1016/j.foodchem.2010.03.005 · DOI · Paper page
- Dufour, 2005, Flavanoid–serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy, Biochim. Biophys. Acta, 1721, 164, 10.1016/j.bbagen.2004.10.013 · DOI · Paper page
- Froehlich, 2009, Dendrimers bind human serum albumin, J. Phys. Chem. B, 113, 6986, 10.1021/jp9011119 · DOI · Paper page
- Hasni, 2011, Interaction of milk α- and β-caseins with tea polyphenol, Food. Chem., 126, 630, 10.1016/j.foodchem.2010.11.087 · DOI · Paper page
- He, 2005, Effect of Chinese medicine alpinetin on the structure of human serum albumin, Bioorg. Med. Chem., 13, 1837, 10.1016/j.bmc.2004.11.038 · DOI · Paper page
- Jiang, 2002, Study of the interaction between terazosin and serum albumin synchronous fluorescence determination of terazosin, Anal. Chim. Acta, 452, 185, 10.1016/S0003-2670(01)01453-2 · doi:10.1016/s0003-2670(01)01453-2
- Jiang, 2004, Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin, J. Mol. Struct., 692, 71, 10.1016/j.molstruc.2004.01.003 · DOI · Paper page
- Jobstl, 2006, Nocovalent cross-linking of casein by epigallocatechingallate characterized by single molecule force microscopy, J. Agric. Food Chem., 54, 4077, 10.1021/jf053259f · DOI
- Johnson, 1999, Analyzing protein circular dichroism spectra for accurate secondary structure, Proteins Struct. Funct. Genet., 35, 307, 10.1002/(SICI)1097-0134(19990515)35:3<307::AID-PROT4>3.0.CO;2-3 · DOI · Paper page
- Kartsova, 2008, Effect of milk caseins on the concentration of polyphenolic compounds in tea, J. Anal. Chem., 63, 1107, 10.1134/S1061934808110154 · DOI
- Kragh-Hansen, 1990, Structure and ligand binding properties of human serum albumin, Dan. Med. Bull., 37, 57
- Kratochwil, 2002, Predicting plasma protein binding of drugs: A new approach, Biochem. Pharmacol., 64, 1355, 10.1016/S0006-2952(02)01074-2 · DOI · Paper page
- Krimm, 1986, Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins, Adv. Protein Chem., 38, 181, 10.1016/S0065-3233(08)60528-8 · DOI · Paper page
- Liang, 2010, β-Lactoglobulin/folic acid complexes: Formation, characterization, and biological implication, J. Phys. Chem. B, 114, 6707, 10.1021/jp101096r · DOI · Paper page
- Liang, 2008, Interaction of β-lactoglobulin with resveratrol and its biological implications, Biomacromolecules, 9, 50, 10.1021/bm700728k · DOI · Paper page
- Liang, 2003, Effect of extraction temperature on cream and extractibility of black tea [Camellia sinensis (L.) O. Kuntze], Int. J. Food Sci. Technol., 38, 37, 10.1046/j.1365-2621.2003.00631.x · doi:10.1046/j.1365-2621.2003.00631.x
- Mandeville, 2010, Complexes of dendrimers with bovine serum albumin, Biomacromolecules, 11, 465, 10.1021/bm9011979 · DOI · Paper page
- McKenzie, 1967, Effect of pH on β-lactoglobulins, Nature, 214, 1101, 10.1038/2141101a0 · doi:10.1038/2141101a0
- N’soukpoé-Kossi, 2007, Retinol and retinoic acid bind human serum albumin: Stability and structural features, Int. J. Biol. Macromol., 40, 484, 10.1016/j.ijbiomac.2006.11.005 · DOI
- Qin, 1998, Structural basis of the tanford transition of bovine β-lactoglobulin, Biochemistry, 37, 14014, 10.1021/bi981016t · DOI · Paper page
- Ql, 1997, Effect of temperature on the secondary structure of β-lactoglolobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis, Biochem. J., 324, 341, 10.1042/bj3240341 · DOI · Paper page
- Shukla, 2009, Structure of casein micelles and their complexation with tannins, Soft. Matter, 5, 2884, 10.1039/b903103k · DOI
- Sreerama, 2000, Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set, Anal. Biochem., 287, 252, 10.1006/abio.2000.4880 · DOI · Paper page
- Stanner, 2007, Does adding milk remove the benefit of your daily cuppa?, Br. Nutr. Foundation Nutr. Bull., 32, 101, 10.1111/j.1467-3010.2007.00636.x · DOI
- Sulkowska, 2002, Interaction of drugs with bovine and human serum albumin, J. Mol. Struct., 614, 227, 10.1016/S0022-2860(02)00256-9 · DOI · Paper page
- Tang, 2005, Spectroscopic studies of the interaction of anti-coagulant rodenticide diphacinone with human serum albumin, J. Mol. Struct., 779, 87, 10.1016/j.molstruc.2005.07.023 · DOI
- Tayeh, 2009, Fluorescence spectral resolution of tryptophan residues in bovine and human serum albumins, J. Pharm. Biomed. Anal., 50, 107, 10.1016/j.jpba.2009.03.015 · doi:10.1016/j.jpba.2009.03.015
- Yan, 2009, Effects of casein, ovalbumin, and dextran on the astringency of tea polyphenols determined by quartz crystal microbalance with dissipation, Langmuir, 25, 397, 10.1021/la8030123 · DOI
Cited by
Protein–polyphenol conjugates: Antioxidant property, functionalities and their applications
Quan, T. H., Benjakul, S., Sae-leaw, T., Balange, A. K., & Maqsood, S. (2019) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2019.07.049 · Cited by 732
Dai, S., Lian, Z., Qi, W., Chen, Y., Tong, X., Tian, T., Lyu, B., Wang, M., Wang, H., & Jiang, L. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.132507 · Cited by 365
Zhang, Q., Cheng, Z., Wang, Y., & Fu, L. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1803199 · Cited by 339
Tang, Q., Roos, Y. H., & Miao, S. (2024) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2024.104464 · Cited by 137
Zhu, H., Guan, K., Liu, X., Xiao, R., Ma, Y., Lu, W., Han, X., Wang, R., & Niu, T. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148163 · Cited by 3
Metadata
- Authors
- Kanakis, C. D., Hasni, I., Bourassa, P., Tarantilis, P. A., Polissiou, M. G., & Tajmir-Riahi, H.-A.
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-08
- Volume
- 127
- Issue
- 3
- Pages
- 1046-1055
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W2057687949
- Cited by
- 489
- References
- 0
- FWCI
- 27.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- Funders
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Agricultural University of Athens, Greece
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Milk β-lactoglobulin complexes with tea polyphenols. https://app.cochat.ai/papers/10.1016/j.foodchem.2011.01.079
- The paper
- Kanakis, C. D., Hasni, I., Bourassa, P., Tarantilis, P. A., Polissiou, M. G., & Tajmir-Riahi, H.-A. (2011). Milk β-lactoglobulin complexes with tea polyphenols. Food Chemistry. https://doi.org/10.1016/j.foodchem.2011.01.079
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.