Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives
Ruiying Jia, Xiao Wan, Xu Geng, et al.
Microorganisms (2021) Vol. 9, Iss. 8, pp. 1659-1659
Open Access | Times Cited: 86

Showing 26-50 of 86 citing articles:

Potential of Low Cost Agro-Industrial Wastes as a Natural Antioxidant on Carcinogenic Acrylamide Formation in Potato Fried Chips
Adel Abdelrazek Abdelazim Mohdaly, Mohamed H. H. Roby, Seham Ahmed Rabea Sultan, et al.
Molecules (2022) Vol. 27, Iss. 21, pp. 7516-7516
Open Access | Times Cited: 13
Characterization of L-asparaginase from Streptomyces koyangensis SK4 with acrylamide-minimizing potential in potato chips
S. Shahana Kabeer, Bini Francis, S. Vishnupriya, et al.
Brazilian Journal of Microbiology (2023) Vol. 54, Iss. 3, pp. 1645-1654
Open Access | Times Cited: 7
Characterization of a novel and glutaminase-free type II L-asparaginase from Corynebacterium glutamicum and its acrylamide alleviation efficiency in potato chips
Huibing Chi, Bingjie Xia, Juan Shen, et al.
International Journal of Biological Macromolecules (2022) Vol. 221, pp. 1384-1393
Closed Access | Times Cited: 12
Acrylamide mitigation in foods using recombinant L-asparaginase: An extremozyme from Himalayan Pseudomonas sp. PCH182
Vijeta Patial, Virender Kumar, Robin Joshi, et al.
Food Research International (2022) Vol. 162, pp. 111936-111936
Closed Access | Times Cited: 11
Evaluation of the efficiency of thermostable l-asparaginase from B. licheniformis UDS-5 for acrylamide mitigation during preparation of French fries
Disha Joshi, Harsh Patel, Sadikhusain Suthar, et al.
World Journal of Microbiology and Biotechnology (2024) Vol. 40, Iss. 3
Closed Access | Times Cited: 1
Acrylamide drives amidase-mediated gut dysbiosis to aggravate colitis
Daotong Li, Yinghua Luo, Huimin Fan, et al.
Science Bulletin (2024)
Closed Access | Times Cited: 1
Comparative studies on modeling and optimization of fermentation process conditions for fungal asparaginase production using artificial intelligence and machine learning techniques
G. Baskar, Rajendran Sivakumar, Seifedine Kadry, et al.
Preparative Biochemistry & Biotechnology (2024) Vol. 55, Iss. 1, pp. 93-99
Closed Access | Times Cited: 1
Reducing the acrylamide concentration in homemade bread processed with L-asparaginase
Martina Calabrese, Lucia De Luca, G. Basile, et al.
LWT (2024), pp. 116770-116770
Open Access | Times Cited: 1
Microbial enzymes and major applications in the food industry: a concise review
Anupama Kumar, Sunny Dhiman, Bhanu Krishan, et al.
Food Production Processing and Nutrition (2024) Vol. 6, Iss. 1
Open Access | Times Cited: 1
Recent advances in L-Asparaginase enzyme production and formulation development for acrylamide reduction during food processing
Arindam Jana, Satyajit Biswas, Ritu Ghosh, et al.
Food Chemistry X (2024) Vol. 25, pp. 102055-102055
Open Access | Times Cited: 1
A Comprehensive Review of the Diversity of Fungal Secondary Metabolites and Their Emerging Applications in Healthcare and Environment
Khushbu Wadhwa, Neha Kapoor, Hardeep Kaur, et al.
Mycobiology (2024) Vol. 52, Iss. 6, pp. 335-387
Open Access | Times Cited: 1
Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
Rita A. M. Barros, Raquel O. Cristóvão, Sónia A. C. Carabineiro, et al.
BioTech (2022) Vol. 11, Iss. 2, pp. 10-10
Open Access | Times Cited: 9
Two decades of research in dietary acrylamide: What do we know today
Thierry Delatour, Richard H. Stadler
Critical Reviews in Food Science and Nutrition (2022) Vol. 63, Iss. 33, pp. 12169-12177
Closed Access | Times Cited: 9
Biochemical characterization and detection of antitumor activity of l-asparaginase from thermophilic Geobacillus kaustophilus DSM 7263T
İnci Özdemir, Müge Didem Orhan, Zeynep Tansu Atasavum, et al.
Protein Expression and Purification (2022) Vol. 199, pp. 106146-106146
Closed Access | Times Cited: 9
Improvement of recombinant L-Asparaginase production in Pichia pastoris
Fidan Erden‐Karaoğlan, Mert Karaoğlan
3 Biotech (2023) Vol. 13, Iss. 5
Open Access | Times Cited: 4
Molecular Characterization of a Stable and Robust L-Asparaginase from Pseudomonas sp. PCH199: Evaluation of Cytotoxicity and Acrylamide Mitigation Potential
Subhash Kumar, Sanyukta Darnal, Vijeta Patial, et al.
Fermentation (2022) Vol. 8, Iss. 10, pp. 568-568
Open Access | Times Cited: 8
Low Acrylamide Flatbreads from Colored Corn and Other Flours
Xueqi Li, Talwinder S. Kahlon, Selina C. Wang, et al.
Foods (2021) Vol. 10, Iss. 10, pp. 2495-2495
Open Access | Times Cited: 10
Acrylamide in foods: from regulation and registered levels to chromatographic analysis, nutritional relevance, exposure, mitigation approaches, and health effects
Mónica Quesada-Valverde, Graciela Artavia, Fabio Granados-Chinchilla, et al.
Toxin Reviews (2022) Vol. 41, Iss. 4, pp. 1343-1373
Closed Access | Times Cited: 7
Production, characterization and techno-economic evaluation of Aspergillus fusant l-asparaginase
Atim Asitok, Maurice Ekpenyong, Andrew Nosakhare Amenaghawon, et al.
AMB Express (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 3
Thermal Inactivation Mechanism and Structural Features Providing Enhanced Thermal Stability of Hyperthermophilic Thermococcus sibiricus L-Asparaginase in Comparison with Mesophilic and Thermophilic L-Asparaginases
Natalia V. Dobryakova, Dmitry D. Zhdanov, М. В. Думина, et al.
Catalysts (2023) Vol. 13, Iss. 5, pp. 832-832
Open Access | Times Cited: 3
Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems
Nicolás Lefin, Javiera Miranda, Jorge F. Beltrán, et al.
Frontiers in Pharmacology (2023) Vol. 14
Open Access | Times Cited: 3
Acrylamide in coffee and coffee substitutes
Monica Anese
Elsevier eBooks (2023), pp. 185-200
Closed Access | Times Cited: 3
Covalent immobilization of recombinant L-asparaginase from Geobacillus kaustophilus on ReliZyme supports for mitigation of acrylamide
İnci Özdemir, Burcu Karaaslan, Ahmet Tülek, et al.
Biocatalysis and Biotransformation (2023) Vol. 42, Iss. 3, pp. 426-439
Closed Access | Times Cited: 3
The Acrylamide Degradation by Probiotic Strain Lactobacillus acidophilus LA-5
Katarzyna Petka, Paweł Sroka, Tomasz Tarko, et al.
Foods (2022) Vol. 11, Iss. 3, pp. 365-365
Open Access | Times Cited: 6
Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
Rita A. M. Barros, Raquel O. Cristóvão, Sónia A. C. Carabineiro, et al.
(2022)
Open Access | Times Cited: 5

Scroll to top