<script type="text/javascript">
<!--
document.write('<div id="oa_widget"></div>');
document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=undefined&type=result"></script>');
-->
</script>
pmid: 4280307
Abstract Phosphorylation of rod membrane proteins is a light-dependent reaction. Most rhodopsin molecules, however, are not phosphorylated. The protein that is highly phosphorylated (>3 moles phosphate per mole phosphorylated protein) appears to be a rhodopsin species that is different from the rest or is located in different parts of the rod membrane system.
Adenosine Triphosphatases, Rhodopsin, Light, Phosphotransferases, Sodium, Darkness, Hydrogen-Ion Concentration, Hydroxylamines, Phosphoproteins, Leucine, Spectrophotometry, Chromatography, Gel, Potassium, Animals, Cattle, Photoreceptor Cells, Spectrophotometry, Ultraviolet, Ouabain, Phosphorus Radioisotopes, Retinal Pigments
Adenosine Triphosphatases, Rhodopsin, Light, Phosphotransferases, Sodium, Darkness, Hydrogen-Ion Concentration, Hydroxylamines, Phosphoproteins, Leucine, Spectrophotometry, Chromatography, Gel, Potassium, Animals, Cattle, Photoreceptor Cells, Spectrophotometry, Ultraviolet, Ouabain, Phosphorus Radioisotopes, Retinal Pigments
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 26 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |