phosphorylate

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phosphorylate

(fŏs′fər-ə-lāt′)
tr.v. phosphoryl·ated, phosphoryl·ating, phosphoryl·ates
To add a phosphate group to (an organic molecule).

phos′pho·ryl·a′tion n.
phos′pho·ryl·a′tive adj.
References in periodicals archive ?
2]AR as GFP fusion protein and specific antibodies against PKA (Ser345/346) and GRK2 (Ser355/356) phosphorylation sites.
Results: There was no effect found on the PKA mediated phosphorylation (n = 14) but we could show that [alpha]-hederin (1 [micro]M, 12 h) significantly inhibits GRK2 mediated phosphorylation at Ser355/356 by 11 [+ or -] 5% (n [greater than or equal to] 29, p [less than or equal to] 0.
Blocking the phosphorylation at S262, by using a mutant form of tau that can't be phosphorylated at that site, prevented amyloid beta's toxic effect on spine density," Mairet-Coello said.
10] (PM [less than or equal to] 10 [micro]m in aerodynamic diameter) is mediated through an NF-[kappa]B dependent signaling mechanism that occurs through a pathway involving direct phosphorylation of the transcription factor p65 in the absence of I[kappa]B[alpha] degradation.
10]) collected from Mexicali ambient air induced NF-[kappa]B--dependent transcriptional expression of IL-8 through an alternate signaling pathway involving direct phosphorylation of p65.
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GJG elevated serum IGF-1 and maintained glycogen storage via phosphorylation of Akt and GSK-3[beta] in the soleus of SAMP8 mice
Akt is activated by phosphorylation of threonine 308 (Thr308) and of serine 473 (Ser473) (Sarbassov et al.
For example, says Tomer, phosphorylation is a frequent post-translational modification involved in cell signaling, but even during active signaling, phosphorylation may occur at only one spot on a protein and upon less than 5% of that particular protein population for less than one minute.
They speculate that phosphorylation at that site may have particular biological significance for p53, and that studying these processes could improve understanding of the health consequences resulting from phosphorylation of proteins through exposure to environmental contaminants.
ETD fragmentation breaks the peptide backbone non-ergodically and preserves functionally important post-translational modifications (PTMs), such as phosphorylation and glycosylation.