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For: Permyakov EA. α-Lactalbumin, Amazing Calcium-Binding Protein. Biomolecules 2020;10:E1210. [PMID: 32825311 DOI: 10.3390/biom10091210] [Cited by in Crossref: 20] [Cited by in F6Publishing: 21] [Article Influence: 6.7] [Reference Citation Analysis]
Number Citing Articles
1 Yu Y, Li X, Zheng M, Zhou L, Zhang J, Wang J, Sun B. The potential benefits and mechanisms of protein nutritional intervention on bone health improvement. Crit Rev Food Sci Nutr 2023;:1-15. [PMID: 36655469 DOI: 10.1080/10408398.2023.2168250] [Reference Citation Analysis]
2 Li QZ, Zhou ZR, Hu CY, Li XB, Chang YZ, Liu Y, Wang YL, Zhou XW. Recent advances of bioactive proteins/polypeptides in the treatment of breast cancer. Food Sci Biotechnol 2023;:1-18. [PMID: 36619215 DOI: 10.1007/s10068-022-01233-6] [Reference Citation Analysis]
3 Picariello G, Siano F, Di Stasio L, Mamone G, Addeo F, Ferranti P. Structural properties of food proteins underlying stability or susceptibility to human gastrointestinal digestion. Current Opinion in Food Science 2023. [DOI: 10.1016/j.cofs.2023.100992] [Reference Citation Analysis]
4 Gołębiowski A, Pomastowski P, Rafińska K, Žuvela P, Wong M, Madajski P, Buszewski B. Binding of silver ions to alpha-lactalbumin. Journal of Molecular Structure 2022;1270:133940. [DOI: 10.1016/j.molstruc.2022.133940] [Reference Citation Analysis]
5 Gołębiowski A, Pomastowski P, Rafińska K, Zuvela P, Wong MW, Pryshchepa O, Madajski P, Buszewski B. Functionalization of Alpha-Lactalbumin by Zinc Ions. ACS Omega. [DOI: 10.1021/acsomega.2c03674] [Reference Citation Analysis]
6 Cuevas-gómez AP, González-magallanes B, Arroyo-maya IJ, Gutiérrez-lópez GF, Cornejo-mazón M, Hernández-sánchez H. Squalene-Rich Amaranth Oil Pickering Emulsions Stabilized by Native α-Lactalbumin Nanoparticles. Foods 2022;11:1998. [DOI: 10.3390/foods11141998] [Reference Citation Analysis]
7 Prikhodchenko NG, Shumatova TA, Katenkova EY, Kovalenko DV. Clinical phenotypes of cow’s milk food allergy in children depending on the molecular profile of sensitization. Allergol immunol pediatr 2022. [DOI: 10.53529/2500-1175-2022-2-13-18] [Reference Citation Analysis]
8 Jiménez‐cruz E, Cuevas‐gómez AP, Unsworth L, Cornejo‐mazón M, Arroyo‐maya IJ, Hernandez‐sanchez H. Poly‐L ‐lysine‐coated α‐lactalbumin nanoparticles: preparation, effect of pH, and stability under in vitro simulated gastrointestinal conditions. J of Chemical Tech & Biotech 2022;97:1597-603. [DOI: 10.1002/jctb.6952] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
9 Olvera-Rosales LB, Cruz-Guerrero AE, García-Garibay JM, Gómez-Ruíz LC, Contreras-López E, Guzmán-Rodríguez F, González-Olivares LG. Bioactive peptides of whey: obtaining, activity, mechanism of action, and further applications. Crit Rev Food Sci Nutr 2022;:1-31. [PMID: 35612490 DOI: 10.1080/10408398.2022.2079113] [Reference Citation Analysis]
10 Zhang J, Wang Q, Liu B, Li D, Zhang H, Wang P, Liu J, Hou G, Li X, Yuan Y, Li Z, Chen S, Yan H, Li Y. The kinetic mechanism of cations induced protein nanotubes self-assembly and their application as delivery system. Biomaterials 2022. [DOI: 10.1016/j.biomaterials.2022.121600] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
11 Pei W, Cai L, Gong X, Zhang L, Zhang J, Zhu P, Jiang H, Wang C, Wang S, Chen J. Drug-loaded oleic-acid grafted mesoporous silica nanoparticles conjugated with α-lactalbumin resembling BAMLET-like anticancer agent with improved biocompatibility and therapeutic efficacy. Materials Today Bio 2022. [DOI: 10.1016/j.mtbio.2022.100272] [Reference Citation Analysis]
12 Ali R, Alireza N, Reza FM, Rahim M. Accelerative Effect of Cinnamon Nanoparticles as well as HAMLET on Healing of Wounds Infected with MRSA in Diabetic Rats. Biomed Res Int 2021;2021:9984540. [PMID: 34993250 DOI: 10.1155/2021/9984540] [Reference Citation Analysis]
13 Ho TM, Bansal N. α-Lactalbumin. Encyclopedia of Dairy Sciences 2022. [DOI: 10.1016/b978-0-12-818766-1.00371-8] [Reference Citation Analysis]
14 Nouri H, Ghahghaei A, Lagzian M. Impact of Synthesized AuNPs from Crocin Against Aggregation and Conformational Change in α-Lactalbumin. Int J Pept Res Ther 2021;27:2275-2289. [DOI: 10.1007/s10989-021-10252-6] [Reference Citation Analysis]
15 Raina N, Hassan MI, Ahmad F, Islam A, Singh AK. PEG mediated destabilization of holo α-lactalbumin probed by in silico and in vitro studies: deviation from excluded volume effect. J Biomol Struct Dyn 2022;40:13265-77. [PMID: 34726117 DOI: 10.1080/07391102.2021.1987990] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
16 Aprile FA, Temussi PA, Pastore A. Man does not live by intrinsically unstructured proteins alone: The role of structured regions in aggregation. Bioessays 2021;43:e2100178. [PMID: 34674273 DOI: 10.1002/bies.202100178] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
17 Spöttel J, Brockelt J, Falke S, Rohn S. Characterization of Conjugates between α-Lactalbumin and Benzyl Isothiocyanate-Effects on Molecular Structure and Proteolytic Stability. Molecules 2021;26:6247. [PMID: 34684828 DOI: 10.3390/molecules26206247] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
18 Haller N, Maier I, Kulozik U. Molecular Analytical Assessment of Thermally Precipitated α-Lactalbumin after Resolubilization. Foods 2021;10:2231. [PMID: 34574341 DOI: 10.3390/foods10092231] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
19 Akabane T, Suzuki N, Tsuchiya W, Yoshizawa T, Matsumura H, Hirotsu N, Katoh E. Expression, purification and crystallization of TGW6, which limits grain weight in rice. Protein Expr Purif 2021;188:105975. [PMID: 34536500 DOI: 10.1016/j.pep.2021.105975] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
20 De Oliveira TV, Polêto MD, Barbosa SV, Coimbra JSDR, De Oliveira EB. Impacts of Ca2+ cation and temperature on bovine α-lactalbumin secondary structures and foamability - Insights from computational molecular dynamics. Food Chem 2021;367:130733. [PMID: 34375890 DOI: 10.1016/j.foodchem.2021.130733] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
21 Chiou JT, Shi YJ, Lee YC, Wang LJ, Chen YJ, Chang LS. Carboxyl group-modified α-lactalbumin induces TNF-α-mediated apoptosis in leukemia and breast cancer cells through the NOX4/p38 MAPK/PP2A axis. Int J Biol Macromol 2021;187:513-27. [PMID: 34310992 DOI: 10.1016/j.ijbiomac.2021.07.133] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 2.5] [Reference Citation Analysis]
22 Meng F, Uniacke-lowe T, Ryan AC, Kelly AL. The composition and physico-chemical properties of human milk: A review. Trends in Food Science & Technology 2021;112:608-21. [DOI: 10.1016/j.tifs.2021.03.040] [Cited by in Crossref: 6] [Cited by in F6Publishing: 7] [Article Influence: 3.0] [Reference Citation Analysis]