ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2008
Spin-diffusion couples proton relaxation rates for proteins in exchange with a membrane interface.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- PtdInsPeLife · 2016Article
- Stabilization of a supersaturated solution of mefenamic acid from a solid dispersion with EUDRAGIT(®) EPO.Pharmaceutical research · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Changes in nuclear spin-lattice relaxation rates that are induced by a freely diffusing paramagnetic relaxation agent are examined for a protein in solution and compared to the case where the protein binds to a membrane. In the solution case, the intramolecular cross-relaxation rates are modest and large differences are observed in the oxygen induced protein-proton relaxation rates. In the case where a dynamic equilibrium between solution and membrane-bound environments is established, the intramolecular (1)H cross-relaxation rates for the protein protons increase dramatically because of the slow reorientational motion in the membrane-bound environment. As a consequence, all protein protons relax with nearly the same spin-lattice relaxation rate constants when bound to the membrane, and site specific relaxation effects of the diffusing paramagnet are suppressed. Slowly reorienting sites or rotationally immobilized sites sampled by observable molecules in vivo will demonstrate similar relaxation leveling effects.
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