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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:

The determination of aggregation size on the emulsion properties of myofibrillar protein
Haozhen Zhang, Weiyi Zhang, Xue Zhao, et al.
Food Hydrocolloids (2023) Vol. 144, pp. 109015-109015
Closed Access | Times Cited: 36

Showing 26-50 of 36 citing articles:

Abelmoschus manihot gum improves the water retention capacity of low-salt myofibrillar protein gels: Perspective on aggregation behaviour and conformational changes during heating
Dongxue Yuan, Cheng Li, Jingming Zhang, et al.
International Journal of Biological Macromolecules (2024) Vol. 282, pp. 137483-137483
Closed Access | Times Cited: 1
Improving the emulsifying properties and oil–water interfacial behaviors of chickpea protein isolates through Maillard reaction with citrus pectin
Yibo Liu, Xiaobing Guo, Xuemei Fan, et al.
International Journal of Biological Macromolecules (2024), pp. 137671-137671
Closed Access | Times Cited: 1
Myofibrillar protein aggregate evolution regulates interfacial adsorption behavior to maintain long-term stability of high internal phase Pickering emulsions
Jiaqi Zhao, Ruren Li, Fan Song, et al.
Food Hydrocolloids (2024), pp. 111039-111039
Closed Access | Times Cited: 1
Insights into the Pickering Emulsions Stabilized by Yeast Dietary Fiber: Interfacial Adsorption Kinetics, Rheological Characteristics, and Stabilization Mechanisms
Yaqiu Kong, Jieling Chen, Zehan Hong, et al.
(2024)
Closed Access
l-Arginine and l-lysine improve the emulsifying and dissolution properties of pale, soft, exudative-like chicken myofibrillar proteins by modifying their conformations
Xun Gao, Axiang Li, Cunliu Zhou
Food Chemistry (2024) Vol. 463, pp. 141136-141136
Closed Access
Peanut de-oiling at room temperature by micro-aqueous hydration: Co-destabilization driven by oleosome coalescence and protein aggregation
Juncai Tu, Shenghai Liu, Weidong Bai, et al.
International Journal of Biological Macromolecules (2024) Vol. 280, pp. 136366-136366
Closed Access
Revealing protein aggregation behaviour and dispersion properties induced by molecular interactions between sucrose esters and myofibrillar protein in an aqueous phase system
Xiang Li, Wenwen Hou, Y. Yi, et al.
International Journal of Biological Macromolecules (2024) Vol. 282, pp. 136768-136768
Closed Access
Encapsulation and release of salidroside in myofibrillar protein‑sodium alginate gel: Effects of different M/G ratios of sodium alginate
Zerun Zhao, Di Zhao, Liuyu Su, et al.
International Journal of Biological Macromolecules (2024), pp. 136811-136811
Closed Access
Myosin supramolecular self-assembly: The crucial precursor that manipulates the covalent aggregation, emulsification and rheological properties of myosin
Li Hu, Sinong Liu, Ruibang Zhang, et al.
Food Research International (2024) Vol. 198, pp. 115320-115320
Closed Access
Improving the rheological and tribological properties of emulsion-filled gel by ultrasound-assisted cross-linked myofibrillar protein emulsion: Insight into the simulation of oral processing
Tao Ye, Jiaming Cai, Peng Wang, et al.
Ultrasonics Sonochemistry (2024) Vol. 112, pp. 107205-107205
Open Access
How chloride salt mixtures affect the final gel properties of low-sodium myofibrillar protein: Underlining the perspective of gelation process
Haibo Shi, Yong-Jie Li, Jiabao Zheng, et al.
Meat Science (2024), pp. 109735-109735
Closed Access
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