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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.

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Showing 20 citing articles:

Challenges and processing strategies to produce high quality frozen meat
Renyu Zhang, C.E. Realini, Yuan H. Brad Kim, et al.
Meat Science (2023) Vol. 205, pp. 109311-109311
Closed Access | Times Cited: 25
Inhibitive effect of trehalose and sodium pyrophosphate on oxidation and structural changes of myofibrillar proteins in silver carp surimi during frozen storage
Dan Wu, Yuan Cao, Tao Yin, et al.
Food Research International (2024) Vol. 187, pp. 114361-114361
Closed Access | Times Cited: 12
Mono-frequency ultrasonic-assisted thawing of frozen goose meat: Influence on thawing efficiency, product quality and microstructure
Zhaoli Zhang, Wangbin Shi, Yang Wang, et al.
Ultrasonics Sonochemistry (2023) Vol. 98, pp. 106489-106489
Open Access | Times Cited: 17
Insights into physical property changes of fish proteins during low-frequency electric field freezing
Sun Guang-quan, Haiqiang Chen, Y. X. Feng, et al.
Food Chemistry (2025) Vol. 475, pp. 143211-143211
Closed Access
Evaluating the effects of low-frequency alternating magnetic field thawing on oxidation, denaturation, and gelling properties of porcine myofibrillar proteins
Mingming Zhu, He Wang, Jiaxing Zong, et al.
Food Chemistry (2023) Vol. 433, pp. 137337-137337
Closed Access | Times Cited: 14
Low-frequency alternating magnetic field thawing of frozen pork meat: Effects of intensity on quality properties and microstructure of meat and structure of myofibrillar proteins
Mingming Zhu, Yi Xing, Juan Zhang, et al.
Meat Science (2023) Vol. 204, pp. 109241-109241
Closed Access | Times Cited: 13
Understanding the influence of fluctuated low-temperature combined with high-humidity thawing on gelling properties of pork myofibrillar proteins
Mingming Zhu, Huijie Li, Yi Xing, et al.
Food Chemistry (2022) Vol. 404, pp. 134238-134238
Closed Access | Times Cited: 21
Physicochemical and structural changes of myofibrillar proteins in muscle foods during thawing: Occurrence, consequences, evidence, and implications
Yuanlv Zhang, Guishan Liu, Qiwen Xie, et al.
Comprehensive Reviews in Food Science and Food Safety (2023) Vol. 22, Iss. 4, pp. 3444-3477
Closed Access | Times Cited: 10
Effect of temperature and sodium bicarbonate combined on aggregation, rheology and conformation of low-salt chicken myofibrillar protein
Zhuangli Kang, Peng‐Lei Yao, Shengming Zhao, et al.
LWT (2024) Vol. 204, pp. 116417-116417
Open Access | Times Cited: 3
Effects of freezing methods and frozen storage on physicochemical, oxidative properties and protein denaturation of porcine longissimus dorsi
Mingming Zhu, Juan Zhang, Lingxia Jiao, et al.
LWT (2021) Vol. 153, pp. 112529-112529
Open Access | Times Cited: 26
Effects of temperature fluctuations on non-volatile taste compounds in tilapia fillets (Oreochromis niloticus)
Mingyu Yin, Yinci Xi, Yuyao Shi, et al.
Food Chemistry (2022) Vol. 408, pp. 135227-135227
Closed Access | Times Cited: 17
Effect of Flammulina velutipes polysaccharides on the physicochemical properties of catfish surimi and myofibrillar protein oxidation during frozen storage
Ling Liang, Ying Liu, Xin Zhang, et al.
Frontiers in Nutrition (2023) Vol. 10
Open Access | Times Cited: 6
Effects of high-pressure thawing on the quality and myofibrillar protein denaturation of Atlantic salmon
Li LI
European Food Research and Technology (2024) Vol. 250, Iss. 6, pp. 1789-1802
Closed Access | Times Cited: 1
Effects of high pressure versus conventional thawing on the quality changes and myofibrillar protein denaturation of slow/fast freezing beef rump muscle
Li LI
Food Science and Technology (2021) Vol. 42
Open Access | Times Cited: 9
Experimental study on the effect of heating plate (Heat source) temperature on a new vacuum sublimation - rehydration thawing
Shanshan Chen, Weidong Wu, Fangran Liu, et al.
International Journal of Refrigeration (2022) Vol. 136, pp. 27-35
Closed Access | Times Cited: 5
Optimization of a novel vacuum sublimation–rehydration thawing process
Shanshan Chen, Weidong Wu, Shijie Mao, et al.
Journal of Food Science (2022) Vol. 88, Iss. 1, pp. 259-272
Closed Access | Times Cited: 5
Understanding the effect of different rehydration water temperatures on a novel vacuum sublimation-rehydration thawing method
Shanshan Chen, Weidong Wu, Hao Wang, et al.
LWT (2023) Vol. 174, pp. 114436-114436
Open Access | Times Cited: 2
Electrostatically-enhanced two-stage low-temperature tempering: Effects on the quality of frozen tan mutton
Yuanlv Zhang, Guishan Liu
Food Chemistry X (2024) Vol. 24, pp. 101926-101926
Open Access
Improvement of gelation properties of myofibrillar proteins from porcine longissimus dorsi muscle through microwave combined with air convection thawing treatment
Fenxia Han, Mingming Zhu, Yi Xing, et al.
International journal of agricultural and biological engineering (2023) Vol. 16, Iss. 3, pp. 254-261
Open Access | Times Cited: 1
Comparison of five thermal treatments on the formation of Nε-carboxymethyl-lysine in duck breast
Qiannan Wang, Zongshuai Zhu, Anthony Pius Bassey, et al.
LWT (2023) Vol. 185, pp. 115127-115127
Open Access
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