Quantitative single-protein imaging reveals molecular complex formation of integrin, talin, and kindlin during cell adhesion
Single-molecule localisation microscopy is limited by low labeling and detection efficiencies of the molecular probes. Here the authors report a framework to obtain absolute molecular quantities on a true molecular scale; the data reveal a ternary adhesion complex underlying cell-matrix adhesion.
Guardado en:
Autores principales: | Lisa S. Fischer, Christoph Klingner, Thomas Schlichthaerle, Maximilian T. Strauss, Ralph Böttcher, Reinhard Fässler, Ralf Jungmann, Carsten Grashoff |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/af7ee6c4a1ba419ab1ee68cefdf933b9 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Molecular motion and tridimensional nanoscale localization of kindlin control integrin activation in focal adhesions
por: Thomas Orré, et al.
Publicado: (2021) -
miRNA-200c-3p targets talin-1 to regulate integrin-mediated cell adhesion
por: Gideon Obeng, et al.
Publicado: (2021) -
Super-resolved visualization of single DNA-based tension sensors in cell adhesion
por: Thomas Schlichthaerle, et al.
Publicado: (2021) -
A computational analysis of the dynamic roles of talin, Dok1, and PIPKI for integrin activation.
por: Florian Geier, et al.
Publicado: (2011) -
Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation
por: Liang Zhu, et al.
Publicado: (2017)