The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regions.

MLA

Strauch, Annika, et al. “The Permanently Chaperone-Active Small Heat Shock Protein Hsp17 from Caenorhabditis Elegans Exhibits Topological Separation of Its N-Terminal Regions.” The Journal of Biological Chemistry, vol. 299, no. 1, Jan. 2023, p. 102753. EBSCOhost, https://doi.org/10.1016/j.jbc.2022.102753.

APA

Strauch, A., Rossa, B., Köhler, F., Haeussler, S., Mühlhofer, M., Rührnößl, F., Körösy, C., Bushman, Y., Conradt, B., Haslbeck, M., Weinkauf, S., & Buchner, J. (2023). The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regions. The Journal of Biological Chemistry, 299(1), 102753. https://doi.org/10.1016/j.jbc.2022.102753

Chicago

Strauch, Annika, Benjamin Rossa, Fabian Köhler, Simon Haeussler, Moritz Mühlhofer, Florian Rührnößl, Caroline Körösy, et al. 2023. “The Permanently Chaperone-Active Small Heat Shock Protein Hsp17 from Caenorhabditis Elegans Exhibits Topological Separation of Its N-Terminal Regions.” The Journal of Biological Chemistry 299 (1): 102753. doi:10.1016/j.jbc.2022.102753.