ArticleBiomolecular NMR assignments2014
¹H, ¹³C and ¹⁵N resonance assignments for the full-length mammalian cytochrome b₅ in a membrane environment.
Article in Biomolecular NMR assignments, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Kinetic and Structural Characterization of the Effects of Membrane on the Complex of Cytochrome bScientific reports · 2017Article
- Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization.Biochimica et biophysica acta · 2015Article
- Role of protein-protein interactions in cytochrome P450-mediated drug metabolism and toxicity.Chemical research in toxicology · 2014Review
- Proton-detected 2D radio frequency driven recoupling solid-state NMR studies on micelle-associated cytochrome-b(5).Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Cytochrome-P450-cytochrome-b5 interaction in a membrane environment changes 15N chemical shift anisotropy tensors.The journal of physical chemistry. B · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Microsomal cytochrome b5 plays a key role in the oxidation of a variety of exogenous and endogenous compounds, including drugs, fatty acids, cholesterol and steroid hormones. To better understand its functional properties in a membrane mimic environment, we carried out high-resolution solution NMR studies. Here we report resonance assignments for full-length rabbit cytochrome b5 embedded in dodecylphosphocholine micelles.
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