Metal Sequestration and Antimicrobial Activity of Human Calprotectin Are pH-Dependent
© 2020 American Chemical Society. Human calprotectin (CP, S100A8/S100A9 oligomer) is an abundant innate immune protein that sequesters transition metal ions in the extracellular space to limit nutrient availability and the growth of invading microbial pathogens. Our current understanding of the meta...
Autores principales: | Rosen, Tomer, Nolan, Elizabeth M |
---|---|
Otros Autores: | Massachusetts Institute of Technology. Department of Chemistry |
Formato: | Artículo |
Lenguaje: | English |
Publicado: |
American Chemical Society (ACS)
2021
|
Acceso en línea: | https://hdl.handle.net/1721.1/135317 |
Ejemplares similares
-
Transition Metal Sequestration by the Host-Defense Protein Calprotectin
por: Zygiel, Emily Mikayla, et al.
Publicado: (2020) -
Coordinated adaptation of Staphylococcus aureus to calprotectin-dependent metal sequestration
por: Valeria M. Reyes Ruiz, et al.
Publicado: (2024-07-01) -
Nickel Sequestration by the Host-Defense Protein Human Calprotectin
por: Nakashige, Toshiki George, et al.
Publicado: (2018) -
Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin
por: Silvers, Robert, et al.
Publicado: (2022) -
Metal sequestration of the host-defense protein human calprotectin
por: Nakashige, Toshiki G
Publicado: (2017)