Tőke, O.; Koprivanacz, K.; Radnai, L.; Merő, B.; Juhász, T.; Liliom, K.; Buday, L.
Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding. Cells 2021, 10, 173.
https://doi.org/10.3390/cells10010173
AMA Style
Tőke O, Koprivanacz K, Radnai L, Merő B, Juhász T, Liliom K, Buday L.
Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding. Cells. 2021; 10(1):173.
https://doi.org/10.3390/cells10010173
Chicago/Turabian Style
Tőke, Orsolya, Kitti Koprivanacz, László Radnai, Balázs Merő, Tünde Juhász, Károly Liliom, and László Buday.
2021. "Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding" Cells 10, no. 1: 173.
https://doi.org/10.3390/cells10010173
APA Style
Tőke, O., Koprivanacz, K., Radnai, L., Merő, B., Juhász, T., Liliom, K., & Buday, L.
(2021). Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding. Cells, 10(1), 173.
https://doi.org/10.3390/cells10010173