Cargando…
Tissue-Specificity of Dystrophin–Actin Interactions: Isoform-Specific Thermodynamic Stability and Actin-Binding Function of Tandem Calponin-Homology Domains
[Image: see text] Genetic mutations in Duchenne muscular dystrophy (DMD) gene affecting the expression of dystrophin protein lead to a number of muscle disorders collectively called dystrophinopathies. In addition to muscle dystrophin, mutations in brain-specific dystrophin isoforms, in particular t...
Autores principales: | Upadhyay, Vaibhav, Bandi, Swati, Panja, Sudipta, Saba, Laura, Mallela, Krishna M. G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7016916/ https://www.ncbi.nlm.nih.gov/pubmed/32064376 http://dx.doi.org/10.1021/acsomega.9b02911 |
Ejemplares similares
-
Opening of tandem calponin homology domains regulates their affinity for F-actin
por: Galkin, Vitold E., et al.
Publicado: (2010) -
Steric regulation of tandem calponin homology domain actin-binding affinity
por: Harris, Andrew R., et al.
Publicado: (2019) -
Calponin-homology domain mediated bending of membrane-associated actin filaments
por: Palani, Saravanan, et al.
Publicado: (2021) -
Calponin-3 is critical for coordinated contractility of actin stress fibers
por: Ciuba, Katarzyna, et al.
Publicado: (2018) -
Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion
por: Shibukawa, Yukinao, et al.
Publicado: (2010)