Crystal structures of human cardiac β-myosin II S2-Δ provide insight into the functional role of the S2 subfragment
By W. Blankenfeldt, N. Thomä, J. Wray, Mathias Gautel, I. Schlichting. Proceedings of the National Academy of Sciences of the United States of America, 2006
90 citations recorded by the source corpus.
Subfields: Cardiology and Cardiovascular Medicine, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/765d4c47cb0d45ab3812715377f7a4bcf8b46be6
How researchers see this paper
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In Cardiology and Cardiovascular Medicine
In Molecular Biology
- Shizuo Akira
- O. Takeuchi
- T. Fujita
- Mitsutoshi Yoneyama
- A. Craievich
- Igor Polikarpov
- Shintaro Sato
- H. Fischer
Citations in the corpus
- Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale (2010, background): “8 the crystallographic structure of myosin (PDB code 2fxo; Blankenfeldt et al., 2006), an extremely anisotropic and elongated protein, with the anisotropy parameter of 10.”
- LGP2 is a positive regulator of RIG-I– and MDA5-mediated antiviral responses (2010, background): “The latter function is in agreement with the presence of similar dynamic or destabilizing coiled-coil features in myosin (Blankenfeldt et al., 2006; Li et al., 2003), tropomyosin (Brown et al.”