Cargando…
(1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment
Fibrillins are large extracellular glycoproteins that form the principal component of microfibrils. These perform a vital structural function in the extracellular matrix of many tissues. Fibrillins have also been implicated in mediating a number of protein–protein interactions, some of which may be...
Autores principales: | Robertson, Ian B., Osuch, Isabelle, Yadin, David A., Handford, Penny A., Jensen, Sacha A., Redfield, Christina |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3955488/ https://www.ncbi.nlm.nih.gov/pubmed/23649688 http://dx.doi.org/10.1007/s12104-013-9481-7 |
Ejemplares similares
-
The Clinical Spectrum of Missense Mutations of the First Aspartic Acid of cbEGF-like Domains in Fibrillin-1 Including a Recessive Family
por: Hilhorst-Hofstee, Yvonne, et al.
Publicado: (2010) -
Steered molecular dynamic simulations reveal Marfan syndrome mutations disrupt fibrillin-1 cbEGF domain mechanosensitive calcium binding
por: Haller, Stephen J., et al.
Publicado: (2020) -
(1)H, (13)C and (15)N assignments of the four N-terminal domains of human fibrillin-1
por: Yadin, David A., et al.
Publicado: (2012) -
Cysteine Substitution and Calcium-Binding Mutations in FBN1 cbEGF-Like Domains Are Associated With Severe Ocular Involvement in Patients With Congenital Ectopia Lentis
por: Zhang, Min, et al.
Publicado: (2022) -
The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1
por: Robertson, Ian B., et al.
Publicado: (2017)