Introduction to Novel Phosphorylation

Novel Phosphorylation - VEGFR2 carries out the novel phosphorylation of Y135 within the DRY microswitch of CXCR4, sequentially activating Gαiβγ, AC7 and PKA, which phosphorylates S988 on the integrin. ^[1] The data demonstrate a novel phosphorylation-dependent mechanism to regulate Gld2 activity, revealing tumour suppressor miRNAs as a previously unknown target of Akt1-dependent signalling. ^[2] Disruption of this function by disease mutations suggests a novel phosphorylation-independent loss of function mechanism that may synergize with other neurotoxic effects caused by LRRK2 mutations. ^[3] Preliminary findings show that our hit compound inhibits CDK5 with simultaneous elevation of novel phosphorylation on pS65-PRKAG2 embarking catalytic activation of AMPK kinase. ^[4] In some cases, novel phosphorylation-dependent regulatory paradigms for cell division, gene transcription, and protein translation have been identified suggesting that a wide scope of prokaryotic physiology remains to be characterized. ^[5]

novel phosphorylation site

Mass spectrometric analysis of immunoprecipitated Runx2 protein from HEK293 cells overexpressing MST2 and SAV1 revealed two novel phosphorylation sites at Ser-339 and Ser-370 residues of mouse Runx2 protein. ^[1] We previously identified a novel phosphorylation site in JFH-1 NS5A: S146. ^[2] Novel phosphorylation sites were found on IAV-encoded proteins, and the functional analysis of selected phosphorylation sites showed that they either support (NA Ser178) or inhibit (PB1 Thr223) virus propagation. ^[3] We show that both MCPH1 isoforms are phosphorylated in a cyclin‐dependent kinase‐1–dependent manner in mitosis and identify several novel phosphorylation sites. ^[4] Here we reveal a novel phosphorylation site of SET isoform 1, and we have determined its biological significance in tumorigenesis. ^[5] Here, we performed CTCF mass spectrometry, identified a novel phosphorylation site at Serine 224 (Ser224-P), and demonstrate that phosphorylation is carried out by Polo-like kinase 1 (PLK1). ^[6] Phosphoproteomics and high throughput screening identified novel phosphorylation sites downstream of Cdk5. ^[7] For functional verification of novel phosphorylation sites, the authors use a binding assay, combining CENP-F containing a phosphomimetic mutation and karyopherin α, a nuclear transport receptor, thus providing cross-validation. ^[8] CONCLUSION We identified a novel phosphorylation site of DJ-1. ^[9] Phosphoproteomics revealed four novel phosphorylation sites on the third intracellular loop of the 5-HT1B receptor, and mutations of serine-256 and serine-291 to alanine led to reduced levels of ERK1/2 phosphorylation following receptor activation. ^[10] We demonstrate that HSD3B2 is phosphorylated at Ser95 or 96 and identify a novel phosphorylation site, Ser489, in CYP21A2, suggesting that steroidogenic enzymes are regulated by phosphorylation. ^[11] We determined the phosphorylation pattern of MST1 using a phosphoproteomic approach and identified two amino acid residues phosphorylated in an ERK-dependent manner after GDC-0941 treatment together with a novel phosphorylation site at S21 residue, which was extensively phosphorylated in an ERK-independent manner during PI3K signaling blockade. ^[12] Here, we identified tyrosine 78 residue (Y78) of NP as a novel phosphorylation site by mass spectrometry. ^[13]

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Mass spectrometric analysis of immunoprecipitated Runx2 protein from HEK293 cells overexpressing MST2 and SAV1 revealed two novel phosphorylation sites at Ser-339 and Ser-370 residues of mouse Runx2 protein.

We previously identified a novel phosphorylation site in JFH-1 NS5A: S146.

VEGFR2 carries out the novel phosphorylation of Y135 within the DRY microswitch of CXCR4, sequentially activating Gαiβγ, AC7 and PKA, which phosphorylates S988 on the integrin.

The data demonstrate a novel phosphorylation-dependent mechanism to regulate Gld2 activity, revealing tumour suppressor miRNAs as a previously unknown target of Akt1-dependent signalling.

Disruption of this function by disease mutations suggests a novel phosphorylation-independent loss of function mechanism that may synergize with other neurotoxic effects caused by LRRK2 mutations.

Preliminary findings show that our hit compound inhibits CDK5 with simultaneous elevation of novel phosphorylation on pS65-PRKAG2 embarking catalytic activation of AMPK kinase.

In some cases, novel phosphorylation-dependent regulatory paradigms for cell division, gene transcription, and protein translation have been identified suggesting that a wide scope of prokaryotic physiology remains to be characterized.

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novel phosphorylation site

Mass spectrometric analysis of immunoprecipitated Runx2 protein from HEK293 cells overexpressing MST2 and SAV1 revealed two novel phosphorylation sites at Ser-339 and Ser-370 residues of mouse Runx2 protein.