Fonte: Acta Crystallographica D. Unidade: IFSC
Assuntos: BIOFILMES, ENZIMAS HIDROLÍTICAS, CRISTALOGRAFIA
ABNT
WILKENS, Casper et al. A GH115 a-glucuronidase structure reveals dimerization-mediated substrate binding and a proton wire potentially important for catalysis. Acta Crystallographica D, v. 78, p. 658-668, 2022Tradução . . Disponível em: https://doi.org/10.1107/S2059798322003527. Acesso em: 08 set. 2024.APA
Wilkens, C., Vuillemin, M., Pilgaard, B., Polikarpov, I., & Morth, J. P. (2022). A GH115 a-glucuronidase structure reveals dimerization-mediated substrate binding and a proton wire potentially important for catalysis. Acta Crystallographica D, 78, 658-668. doi:10.1107/S2059798322003527NLM
Wilkens C, Vuillemin M, Pilgaard B, Polikarpov I, Morth JP. A GH115 a-glucuronidase structure reveals dimerization-mediated substrate binding and a proton wire potentially important for catalysis [Internet]. Acta Crystallographica D. 2022 ; 78 658-668.[citado 2024 set. 08 ] Available from: https://doi.org/10.1107/S2059798322003527Vancouver
Wilkens C, Vuillemin M, Pilgaard B, Polikarpov I, Morth JP. A GH115 a-glucuronidase structure reveals dimerization-mediated substrate binding and a proton wire potentially important for catalysis [Internet]. Acta Crystallographica D. 2022 ; 78 658-668.[citado 2024 set. 08 ] Available from: https://doi.org/10.1107/S2059798322003527