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Cited by in F6Publishing
For: Han M, Yu X. Enhanced expression of heterologous proteins in yeast cells via the modification of N-glycosylation sites. Bioengineered 2015;6:115-8. [PMID: 25671496 DOI: 10.1080/21655979.2015.1011031] [Cited by in Crossref: 16] [Cited by in F6Publishing: 14] [Article Influence: 2.7] [Reference Citation Analysis]
Number Citing Articles
1 Juturu V, Wu JC. Heterologous Protein Expression in Pichia pastoris : Latest Research Progress and Applications. ChemBioChem 2018;19:7-21. [DOI: 10.1002/cbic.201700460] [Cited by in Crossref: 65] [Cited by in F6Publishing: 51] [Article Influence: 13.0] [Reference Citation Analysis]
2 Zubieta MP, Contesini FJ, Rubio MV, Gonçalves AESS, Gerhardt JA, Prade RA, Damasio ARL. Protein profile in Aspergillus nidulans recombinant strains overproducing heterologous enzymes. Microb Biotechnol 2018;11:346-58. [PMID: 29316319 DOI: 10.1111/1751-7915.13027] [Cited by in Crossref: 8] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
3 Rosales-mendoza S, Angulo C, Meza B. Food-Grade Organisms as Vaccine Biofactories and Oral Delivery Vehicles. Trends in Biotechnology 2016;34:124-36. [DOI: 10.1016/j.tibtech.2015.11.007] [Cited by in Crossref: 58] [Cited by in F6Publishing: 47] [Article Influence: 9.7] [Reference Citation Analysis]
4 Chun J, Bai J, Ryu S. Yeast Surface Display System for Facilitated Production and Application of Phage Endolysin. ACS Synth Biol 2020;9:508-16. [PMID: 32119773 DOI: 10.1021/acssynbio.9b00360] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
5 Baghban R, Farajnia S, Rajabibazl M, Ghasemi Y, Mafi A, Hoseinpoor R, Rahbarnia L, Aria M. Yeast Expression Systems: Overview and Recent Advances. Mol Biotechnol 2019;61:365-84. [PMID: 30805909 DOI: 10.1007/s12033-019-00164-8] [Cited by in F6Publishing: 25] [Reference Citation Analysis]
6 Cid R, Bolívar J. Platforms for Production of Protein-Based Vaccines: From Classical to Next-Generation Strategies. Biomolecules 2021;11:1072. [PMID: 34439738 DOI: 10.3390/biom11081072] [Reference Citation Analysis]
7 Wang N, Wang KY, Xu F, Li G, Liu D. The effect of N-glycosylation on the expression of the tetanus toxin fragment C in Pichia pastoris. Protein Expr Purif 2020;166:105503. [PMID: 31550499 DOI: 10.1016/j.pep.2019.105503] [Cited by in Crossref: 1] [Article Influence: 0.3] [Reference Citation Analysis]
8 Tian M, Yang L, Wang Z, Lv P, Fu J, Miao C, Li M, Liu T, Luo W. Improved methanol tolerance of Rhizomucor miehei lipase based on N‑glycosylation within the α-helix region and its application in biodiesel production. Biotechnol Biofuels 2021;14:237. [PMID: 34911574 DOI: 10.1186/s13068-021-02087-6] [Reference Citation Analysis]
9 Kashyap A, Gupta R. Disrupting putative N-glycosylation site N17 in lipase Lip11 of Yarrowia lipolytica yielded a catalytically efficient and thermostable variant accompanying conformational changes. Enzyme Microb Technol 2021;151:109922. [PMID: 34649689 DOI: 10.1016/j.enzmictec.2021.109922] [Reference Citation Analysis]
10 Villa-ruano N, Rivera A, Rubio-rosas E, Landeta-cortés G, Varela-caselis JL, Romero-arenas O. Comparative Activity of Six Recombinant Stilbene Synthases in Yeast for Resveratrol Production. Applied Sciences 2020;10:4847. [DOI: 10.3390/app10144847] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
11 Han M, Wang W, Zhou J, Gong X, Xu C, Li Y, Li Q. Activation of the Unfolded Protein Response via Co-expression of the HAC1i Gene Enhances Expression of Recombinant Elastase in Pichia pastoris. Biotechnol Bioproc E 2020;25:302-7. [DOI: 10.1007/s12257-019-0381-2] [Cited by in Crossref: 4] [Article Influence: 2.0] [Reference Citation Analysis]
12 Palm D, Uzoni A, Simon F, Fischer M, Coogan A, Tucha O, Thome J, Faltraco F. Evolutionary conservations, changes of circadian rhythms and their effect on circadian disturbances and therapeutic approaches. Neurosci Biobehav Rev 2021;128:21-34. [PMID: 34102148 DOI: 10.1016/j.neubiorev.2021.06.007] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
13 Criscuolo E, Caputo V, Diotti RA, Sautto GA, Kirchenbaum GA, Clementi N. Alternative Methods of Vaccine Delivery: An Overview of Edible and Intradermal Vaccines. J Immunol Res 2019;2019:8303648. [PMID: 30949518 DOI: 10.1155/2019/8303648] [Cited by in Crossref: 29] [Cited by in F6Publishing: 27] [Article Influence: 9.7] [Reference Citation Analysis]
14 Uhoraningoga A, Kinsella GK, Henehan GT, Ryan BJ. The Goldilocks Approach: A Review of Employing Design of Experiments in Prokaryotic Recombinant Protein Production. Bioengineering (Basel) 2018;5:E89. [PMID: 30347746 DOI: 10.3390/bioengineering5040089] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 2.3] [Reference Citation Analysis]
15 Kang H, Park Y, Lee Y, Yoo YJ, Hwang I. Fusion of a highly N-glycosylated polypeptide increases the expression of ER-localized proteins in plants. Sci Rep 2018;8:4612. [PMID: 29545574 DOI: 10.1038/s41598-018-22860-2] [Cited by in Crossref: 9] [Cited by in F6Publishing: 8] [Article Influence: 2.3] [Reference Citation Analysis]
16 Aza P, de Salas F, Molpeceres G, Rodríguez-Escribano D, de la Fuente I, Camarero S. Protein Engineering Approaches to Enhance Fungal Laccase Production in S. cerevisiae. Int J Mol Sci 2021;22:1157. [PMID: 33503813 DOI: 10.3390/ijms22031157] [Cited by in Crossref: 3] [Article Influence: 3.0] [Reference Citation Analysis]
17 Kalinina AN, Borshchevskaya LN, Gordeeva TL, Sineoky SP. Comparison of Xylanases of Various Origin Obtained in the Expression System of Pichia pastoris: Gene Expression, Biochemical Characteristics, and Biotechnological Potential. Appl Biochem Microbiol 2019;55:733-40. [DOI: 10.1134/s0003683819070044] [Reference Citation Analysis]
18 Govindan P, Manjusha P, Saravanan KM, Natesan V, Salmen SH, Alfarraj S, Wainwright M, Shakila H. Expression and preliminary characterization of the potential vaccine candidate LipL32 of leptospirosis. Appl Nanosci 2021;:1-15. [PMID: 34608427 DOI: 10.1007/s13204-021-02097-8] [Reference Citation Analysis]
19 Kurup VM, Thomas J. Edible Vaccines: Promises and Challenges. Mol Biotechnol 2020;62:79-90. [PMID: 31758488 DOI: 10.1007/s12033-019-00222-1] [Cited by in Crossref: 11] [Cited by in F6Publishing: 11] [Article Influence: 5.5] [Reference Citation Analysis]