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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Milk Processing Affects Structure, Bioavailability and Immunogenicity of β-lactoglobulin
Kerensa Broersen
Foods (2020) Vol. 9, Iss. 7, pp. 874-874
Open Access | Times Cited: 43

Showing 1-25 of 43 citing articles:

Heat-induced denaturation and bioactivity changes of whey proteins
Lina Zhang, Ruoya Zhou, Jinyue Zhang, et al.
International Dairy Journal (2021) Vol. 123, pp. 105175-105175
Closed Access | Times Cited: 53
A comprehensive review on recent advances in fluorescence-based bio-analytes sensing
Dibya Kanti Mal, Haridas Pal, Goutam Chakraborty
TrAC Trends in Analytical Chemistry (2023) Vol. 171, pp. 117493-117493
Closed Access | Times Cited: 20
Ameliorative effect of liprotide-encapsulated vitamin D3 on blood glucose, calcium homeostasis, and vitamin D level in a vitamin D and calcium deficient rat model
Gemala Anjani, Reza Achmad Maulana, Sylvia Rahmi Putri, et al.
Frontiers in Nutrition (2025) Vol. 12
Open Access
Structural properties of food proteins underlying stability or susceptibility to human gastrointestinal digestion
Gianluca Picariello, Francesco Siano, Luigia Di Stasio, et al.
Current Opinion in Food Science (2023) Vol. 50, pp. 100992-100992
Open Access | Times Cited: 17
New perspective into the interaction behavior explore of Nano-berberine with alpha-lactalbumin in the presence of beta-lactoglobulin: Multi-spectroscopic and molecular dynamic investigations
Parisa Jouyaeian, Melika Kamkar-Vatanparast, Fatemeh Tehranian-Torghabeh, et al.
Journal of Molecular Structure (2024) Vol. 1316, pp. 139020-139020
Closed Access | Times Cited: 5
Red emitting fluorogenic dye as an efficient turn-on probe for milk allergen
Goutam Chakraborty
International Journal of Biological Macromolecules (2022) Vol. 221, pp. 1527-1535
Closed Access | Times Cited: 19
Impact of somatic cell count combined with differential somatic cell count on milk protein fractions in Holstein cattle
Vittoria Bisutti, A. Vanzin, Alessandro Toscano, et al.
Journal of Dairy Science (2022) Vol. 105, Iss. 8, pp. 6447-6459
Open Access | Times Cited: 17
Comparison of the Effects of High Hydrostatic Pressure and Pasteurization on Quality of Milk during Storage
Tongtong Yu, Xiaojun Zhang, Ruoyi Feng, et al.
Foods (2022) Vol. 11, Iss. 18, pp. 2837-2837
Open Access | Times Cited: 16
Heat-Induced Interaction of Milk Proteins: Impact on Yoghurt Structure
Md Asaduzzaman, Md. Sultan Mahomud, Mohammod Enamul Haque
International Journal of Food Science (2021) Vol. 2021, pp. 1-10
Open Access | Times Cited: 20
Pasteurization in the food industry
Maryam Azizi‐Lalabadi, Najme Rezaee Moghaddam, Seid Mahdi Jafari
Elsevier eBooks (2023), pp. 247-273
Closed Access | Times Cited: 7
Milk Protein Hydrolysis by Actinidin—Kinetic and Thermodynamic Characterisation and Comparison to Bromelain and Papain
Surjit Kaur, Todor Vasiljevic, Thom Huppertz
Foods (2023) Vol. 12, Iss. 23, pp. 4248-4248
Open Access | Times Cited: 5
Reactivity of amino acid residues towards 4-methylbenzoquinone: Effect on the site-specificity of quinone-protein reaction
Yuting Li, Xiaotong Li, Jinshun Ye, et al.
LWT (2024) Vol. 200, pp. 116217-116217
Open Access | Times Cited: 1
Amyloidogenic and non-amyloidogenic molten globule conformation of β-lactoglobulin in self-crowded regime
Sara Venturi, Barbara Rossi, Mariagrazia Tortora, et al.
International Journal of Biological Macromolecules (2023) Vol. 242, pp. 124621-124621
Open Access | Times Cited: 5
Hierarchical biocatalytic membranes embedded with trypsin–inorganic hybrid nanoflowers for effective β-lactoglobulin hydrolysis
Hui Ye, Jing Zhang, Guodong Yang, et al.
Colloids and Surfaces A Physicochemical and Engineering Aspects (2024) Vol. 699, pp. 134706-134706
Closed Access | Times Cited: 1
Process-Induced Molecular-Level Protein–Carbohydrate–Polyphenol Interactions in Milk–Tea Blends: A Review
Dilema Wijegunawardhana, Isuru Wijesekara, Rumesh Liyanage, et al.
Foods (2024) Vol. 13, Iss. 16, pp. 2489-2489
Open Access | Times Cited: 1
A comparison of the physicochemical properties, allergenicity, and stability of recombinant β-lactoglobulin: development of standard bovine milk allergens
Fen Xie, Wei Hu, Xuanyi Meng, et al.
Food Bioscience (2024) Vol. 61, pp. 104956-104956
Closed Access | Times Cited: 1
Development of a novel polyclonal antibody against bovine α S1 -casein IgE epitopes for prediction of potential allergenicity of milk in foods
Shengfa He, Caiyun Long, Liming Li, et al.
Food and Agricultural Immunology (2023) Vol. 34, Iss. 1
Open Access | Times Cited: 4
Aptamer-based stir bar sorptive extraction combined with MALDI-TOF-MS for the analysis of milk protein allergen β-lactoglobulin in foods
Natalia Piqueras-García, María Vergara‐Barberán, Mónica Catalá-Icardo, et al.
Microchemical Journal (2023) Vol. 197, pp. 109814-109814
Open Access | Times Cited: 4
Cholic acid inhibits amyloid fibrillation: Interplay of protonation and deprotonation
Nabeela Majid, Mohammad Khursheed Siddiqi, Aftab Alam, et al.
International Journal of Biological Macromolecules (2022) Vol. 221, pp. 900-912
Closed Access | Times Cited: 8
A new fibrillization mechanism of β-lactoglobulin in glycine solutions
Matej Jaklin, Jozef Hritz, Barbara Hribar-Lee
International Journal of Biological Macromolecules (2022) Vol. 216, pp. 414-425
Open Access | Times Cited: 7
A portable electrochemiluminescence aptasensor for β-lactoglobulin detection
Rossella Svigelj, Ivan Zuliani, Nicolò Dossi, et al.
Analytical and Bioanalytical Chemistry (2022) Vol. 414, Iss. 27, pp. 7935-7941
Open Access | Times Cited: 6
Energetic and structural effects of the Tanford transition on ligand recognition of bovine β-lactoglobulin
Alfonso Labra-Núñez, Luis Fernando Cofas‐Vargas, Gabriel Gutiérrez‐Magdaleno, et al.
Archives of Biochemistry and Biophysics (2021) Vol. 699, pp. 108750-108750
Closed Access | Times Cited: 8
A simple method for enrichment of β-lactoglobulin from bovine milk whey involving selective hydrolysis by two fungal protease preparations
Minh Ha, Alaa El‐Din A. Bekhit, Michelle McConnell, et al.
Food Chemistry (2021) Vol. 368, pp. 130820-130820
Closed Access | Times Cited: 8
Synergistic effect of whey proteins and their derived microgels in the stabilization of O/W emulsions
Jéssica Thaís do Prado Silva, Annabel Janssen, Vânia Regina Nicoletti, et al.
Food Hydrocolloids (2022) Vol. 135, pp. 108229-108229
Closed Access | Times Cited: 5
A Combined Spectroscopy and Computational Molecular Docking Investigation on the Coupling Between β-lactoglobulin Dimers and Vanillin
Layla Barbosa Alves, Thomás Valente de Oliveira, Gustavo Leite Milião, et al.
Food Biophysics (2022) Vol. 18, Iss. 2, pp. 302-313
Closed Access | Times Cited: 5
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