Crystal Structure of the α-Actinin Rod Reveals an Extensive Torsional Twist
By J. Ylänne, K. Scheffzek, P. Young, M. Saraste. 2001
167 citations recorded by the source corpus.
Subfields: Cardiology and Cardiovascular Medicine, Cell Biology, Genetics
View Paper: https://www.semanticscholar.org/paper/63f53dc283484efa307cdc1c438b96f087c5c859
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In Cardiology and Cardiovascular Medicine
In Cell Biology
Citations in the corpus
- Structural Dynamics of α-Actinin-Vinculin Interactions (2005, methodology): “Comparisons of our Vh1- VBS structure to that of the twisted antiparallel -actinin rod (13, 29, 40) suggest that the VBS -helix found in one protomer of the R4 spectrin repeat (a three-helical bundle) of the -actinin dimer first unravels from its buried location within the triple helix to allow it t”
- The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling (2009, background): “Micrograph c from Hampton et al. (2007), with permission from Elsevier Science remarkable fact about the rod formed by the four spectrin repeats is that there is a twist of 90 from one end of the rod to the other (Ylanne et al. 2001).”