Definitions
from Wiktionary, Creative Commons Attribution/Share-Alike License.
- noun Plural form of
serine .
Etymologies
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Examples
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The phosphates attached to the serines are negatively charged.
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The key difference between dry silks from moths and butterflies and wet silks from caddisflies is that the serines in the silk from caddisflies are "phosphorylated," meaning phosphates are added to the serines as the fibroin silk protein is synthesized.
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The key difference between dry silks from moths and butterflies and wet silks from caddisflies is that the serines in the silk from caddisflies are "phosphorylated," meaning phosphates are added to the serines as the fibroin silk protein is synthesized.
THE MEDICAL NEWS Editors 2010
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The phosphates attached to the serines are negatively charged.
THE MEDICAL NEWS Editors 2010
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On the other hand, the CTD of NFAT5 has a high content of serines (145 residues) and threonines (74 residues), which together comprise more than 22% of this domain, suggesting the possibility of a complex phosphorylation-dependent regulation.
PLoS ONE Alerts: New Articles Anaïs Estrada-Gelonch et al. 2009
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Previously uncharacterized phosphorylation sites at serines 46/47, 282, 294, and 559 were identified by manual Edman degradation and phosphoamino acid analysis and confirmed by mutagenesis and phospho-specific antibodies.
BioMed Central - Latest articles Christopher Williams 2009
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Fitzpatrick PF, Daubner SC (2005) Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate: effects on enzyme stability and activity.
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The most frequently acylated residues within proteins are lysines (as in histone N-acetylation) and cysteines (as in protein S-palmitoylation); serines seem to be seldom acylated.
PLoS ONE Alerts: New Articles Akihiko Ozawa et al. 2009
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The most frequently acylated residues within proteins are lysines (as in histone N-acetylation) and cysteines (as in protein S-palmitoylation); serines seem to be seldom acylated.
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[15], which requires phosphorylation of β-catenin by Gsk3β on 3 serines and one threonine residue, all of which are encoded in exon 3 of the β-catenin gene
PLoS ONE Alerts: New Articles Myoung Sook Kim et al. 2010
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