The sensitivity and comprehensive phosphorylation site mapping of this approach was demonstrated by using two standard phosphoprotein samples of α-casein and β-casein, and this approach was further ...

SOKENDAI and Kyushu University have uncovered the molecular mechanism that drives the "ticking" of the circadian clock in ...

Erythritol may impair cellular functions essential to maintaining brain blood vessel health, according to researchers at the ...

Abstract: Protein phosphorylation is one of the most widespread regulatory mechanisms in eukaryotes. Over the past decade, phosphorylation site prediction has emerged as an important problem in the ...

Traditionally, the study of single protein phosphorylation has relied on Western blot profiling with site-specific antibodies directed against known phosphorylation sites. Such an approach loses ...

Phosphorylation sites reduce the likelihood of amyloidogenic contacts locally. Amyloidogenicity profiles for (A) unmodified human FUS PLD, and (B) fully phosphorylated FUS PLD sequences. The ZipperDB ...

This gene encodes a kinase that is physiologically multiphosphorylated, including clusters of both heterologous phosphorylation and autophosphorylation sites. Several pieces of evidence indicate that ...

The accurate identification of phosphorylation sites can provide new insights for revealing the specific function of protein. However, it is time-consuming and inefficient to apply the ...

We describe the kinase specificity of the multiple phosphorylation sites on cMyBP-C and show that they are interdependent and have distinct effects on the structure of the thin and thick filaments.

Notably, 9% of the identified SUMOylome occurred proximal to phosphorylation, and numerous SUMOylation sites were found to be fully dependent on prior phosphorylation events. SUMO-proximal ...

Light-activated opsins undergo carboxy-terminal phosphorylation, which contributes to the deactivation of their photoresponse. The photopigment melanopsin possesses an unusually long carboxy tail ...