β-Hexosaminidases Along the Secretory Pathway of Nicotiana benthamiana Have Distinct Specificities Toward Engineered Helminth N-Glycans on Recombinant Glycoproteins.

MLA

Alvisi, Nicolò, et al. “β-Hexosaminidases Along the Secretory Pathway of Nicotiana Benthamiana Have Distinct Specificities Toward Engineered Helminth N-Glycans on Recombinant Glycoproteins.” Frontiers in Plant Science, vol. 11, Mar. 2021, p. N.PAG. EBSCOhost, https://doi.org/10.3389/fpls.2021.638454.

APA

Alvisi, N., van Noort, K., Dwiani, S., Geschiere, N., Sukarta, O., Varossieau, K., Nguyen, D.-L., Strasser, R., Hokke, C. H., Schots, A., & Wilbers, R. H. P. (2021). β-Hexosaminidases Along the Secretory Pathway of Nicotiana benthamiana Have Distinct Specificities Toward Engineered Helminth N-Glycans on Recombinant Glycoproteins. Frontiers in Plant Science, 11, N.PAG. https://doi.org/10.3389/fpls.2021.638454

Chicago

Alvisi, Nicolò, Kim van Noort, Sarlita Dwiani, Nathan Geschiere, Octavina Sukarta, Koen Varossieau, Dieu-Linh Nguyen, et al. 2021. “β-Hexosaminidases Along the Secretory Pathway of Nicotiana Benthamiana Have Distinct Specificities Toward Engineered Helminth N-Glycans on Recombinant Glycoproteins.” Frontiers in Plant Science 11 (March): N.PAG. doi:10.3389/fpls.2021.638454.