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:

Multi-spectroscopic, conformational, and computational atomic-level insights into the interaction of β-lactoglobulin with apigenin at different pH levels
Junxiang Zhu, Kangjing Li, Hao Wu, et al.
Food Hydrocolloids (2020) Vol. 105, pp. 105810-105810
Closed Access | Times Cited: 62

Showing 1-25 of 62 citing articles:

Exploring the binding mechanism of pumpkin seed protein and apigenin: Spectroscopic analysis, molecular docking and molecular dynamics simulation
Fuqiang Liang, Yumeng Shi, Jiayi Shi, et al.
Food Hydrocolloids (2022) Vol. 137, pp. 108318-108318
Closed Access | Times Cited: 75

Molecular interactions between apigenin and starch with different amylose/amylopectin ratios revealed by X-ray diffraction, FT-IR and solid-state NMR
Yunxiang Ma, Zidi Chen, Zhipeng Wang, et al.
Carbohydrate Polymers (2023) Vol. 310, pp. 120737-120737
Open Access | Times Cited: 53

Protein-polyphenol functional ingredients: The foaming properties of lactoferrin are enhanced by forming complexes with procyanidin
Changhong Li, Taotao Dai, Jun Chen, et al.
Food Chemistry (2020) Vol. 339, pp. 128145-128145
Closed Access | Times Cited: 131

Study on simultaneous binding of resveratrol and curcumin to β-lactoglobulin: Multi-spectroscopic, molecular docking and molecular dynamics simulation approaches
Xiaoge Zhang, Yingcong Lu, Ru Zhao, et al.
Food Hydrocolloids (2021) Vol. 124, pp. 107331-107331
Closed Access | Times Cited: 96

pH-dependent interaction mechanisms between β-lactoglobulin and EGCG: Insights from multi-spectroscopy and molecular dynamics simulation methods
Chengzhi Liu, Nan Lv, Yongquan Xu, et al.
Food Hydrocolloids (2022) Vol. 133, pp. 108022-108022
Closed Access | Times Cited: 54

Influence of environmental pH on the interaction properties of WP‐EGCG non‐covalent nanocomplexes
Shuangling Zhang, Zixuan Dongye, Li Wang, et al.
Journal of the Science of Food and Agriculture (2023) Vol. 103, Iss. 11, pp. 5364-5375
Open Access | Times Cited: 30

Comparative interaction study of soy protein isolate and three flavonoids (Chrysin, Apigenin and Luteolin) and their potential as natural preservatives
Mingyuan Li, Jing Kong, Yanrong Chen, et al.
Food Chemistry (2023) Vol. 414, pp. 135738-135738
Closed Access | Times Cited: 29

Non-covalent interaction of complex plant protein and betanin: Mechanism of improving thermal stability of betanin
Ting Hu, Taotao Dai, Xuemei He, et al.
Food Hydrocolloids (2023) Vol. 138, pp. 108456-108456
Closed Access | Times Cited: 23

Inhibition of cinnamic acid and its derivatives on polyphenol oxidase: Effect of inhibitor carboxyl group and system pH
Hongwei� Jiang, Lei Zhou, Yue Wang, et al.
International Journal of Biological Macromolecules (2024) Vol. 259, pp. 129285-129285
Closed Access | Times Cited: 9

The effect of whey protein-puerarin interactions on the formation and performance of protein hydrogels
Yejun Zhong, Jincheng Zhao, Taotao Dai, et al.
Food Hydrocolloids (2020) Vol. 113, pp. 106444-106444
Closed Access | Times Cited: 68

Hydrophobic interaction driving the binding of soybean protein isolate and chlorophyll: Improvements to the thermal stability of chlorophyll
Jiarui Cao, Fangwei Li, Yuanyuan Li, et al.
Food Hydrocolloids (2020) Vol. 113, pp. 106465-106465
Closed Access | Times Cited: 55

pH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study
Ce Wang, Lu Chen, Yingcong Lu, et al.
Food Chemistry (2021) Vol. 362, pp. 130230-130230
Closed Access | Times Cited: 45

Multi-spectroscopies and molecular docking insights into the interaction mechanism and antioxidant activity of astaxanthin and β-lactoglobulin nanodispersions
Zhiwei Liu, Yingxue Zhou, Lang‐Hong Wang, et al.
Food Hydrocolloids (2021) Vol. 117, pp. 106739-106739
Closed Access | Times Cited: 42

Beyond particle stabilization of emulsions and foams: Proteins in liquid-liquid and liquid-gas interfaces
Fuchao Zhan, Mahmoud Youssef, Jing Li, et al.
Advances in Colloid and Interface Science (2022) Vol. 308, pp. 102743-102743
Closed Access | Times Cited: 36

Insight into the binding behavior, structure, and thermal stability properties of β-lactoglobulin/Amoxicillin complex in a neutral environment
H Saïed, Sadegh Farhadian, Mohammad Ghasemi, et al.
Food Hydrocolloids (2022) Vol. 133, pp. 107830-107830
Closed Access | Times Cited: 34

Multispectroscopic and computational simulation insights into the inhibition mechanism of epigallocatechin-3-gallate on polyphenol oxidase
Xuezhi Tian, Lei Rao, Liang Zhao, et al.
Food Chemistry (2022) Vol. 393, pp. 133415-133415
Closed Access | Times Cited: 29

Understanding molecular interaction between thermally modified β-lactoglobulin and curcumin by multi-spectroscopic techniques and molecular dynamics simulation
Ru Zhao, Yingcong Lu, Ce Wang, et al.
Colloids and Surfaces B Biointerfaces (2023) Vol. 227, pp. 113334-113334
Closed Access | Times Cited: 21

Enhanced solubility, thermal stability and antioxidant activity of resveratrol by complexation with ovalbumin amyloid-like fibrils: Effect of pH
Yaru Wang, Yang Qin, Yixuan Jiang, et al.
Food Hydrocolloids (2023) Vol. 148, pp. 109463-109463
Closed Access | Times Cited: 17

Construction of protein hydrogels with antibacterial activity by interaction of β-lactoglobulin amyloid fibrils with epigallocatechin-3-gallate
Jiaqi Ma, Xinyu Zhang, Zixuan Du, et al.
Food Bioscience (2024) Vol. 58, pp. 103632-103632
Closed Access | Times Cited: 8

Inhibition of α-amylase activity by quercetin via multi-spectroscopic and molecular docking approaches
Meigui Huang, Qiao Xiao, Yonghong Li, et al.
Food Bioscience (2024) Vol. 61, pp. 104951-104951
Closed Access | Times Cited: 8

Dielectric-barrier discharge (DBD) plasma treatment reduces IgG binding capacity of β-lactoglobulin by inducing structural changes
Zhiwei Liu, Liu Lianjie, Yingxue Zhou, et al.
Food Chemistry (2021) Vol. 358, pp. 129821-129821
Closed Access | Times Cited: 36

Limited hydrolysis as a strategy to improve the non-covalent interaction of epigallocatechin-3-gallate (EGCG) with whey protein isolate near the isoelectric point
Jiale Zhao, Weimin Lin, Jingxin Gao, et al.
Food Research International (2022) Vol. 161, pp. 111847-111847
Closed Access | Times Cited: 28

Formation mechanism of quinoa protein hydrolysate-EGCG complexes at different pH conditions and its effect on the protein hydrolysate-lipid co-oxidation in emulsions
Jingwen Xu, Hezhen Zhang, Mengyu Deng, et al.
Food Research International (2024) Vol. 186, pp. 114365-114365
Closed Access | Times Cited: 6

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