Phospho.ELM:a database of experimentally verified phosphorylation sites in eukaryotic proteins [PDF]
, 2004 BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes.
Blom, Nikolaj +8 more
core +4 more sources
Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry [PDF]
, 2012 Protein phosphorylation is a common post-translational modification in eukaryotic cells and has a wide range of functional effects. Here, we used mass spectrometry to search for phosphorylated residues in all the proteins of influenza A and B viruses ...
Denham, Eleanor M. +8 more
core +3 more sources
Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase
eLife, 2022 The p97/Cdc48 ATPase and its ubiquitin receptors Ufd1-Npl4 are essential to unfold ubiquitylated proteins in many areas of eukaryotic cell biology.
Ryo Fujisawa +2 more
doaj +1 more source
Erythrocyte Protein Phosphorylation
Journal of Biological Chemistry, 1973 Abstract Human erythrocyte membrane protein components have been phosphorylated by an endogenous protein kinase. This transfer of phosphate from [γ-32P]ATP was stimulated by cyclic adenosine 3',5'-monophosphate and inhibited by calcium. The formation of phosphoserine and phosphothreonine bonds and the negligible effect of large changes in sodium and ...
A D, Roses, S H, Appel
openaire +2 more sources
On the existence of Hopf bifurcations in the sequential and distributive double phosphorylation cycle [PDF]
, 2019 Protein phosphorylation cycles are important mechanisms of the post translational modification of a protein and as such an integral part of intracellular signaling and control. We consider the sequential phosphorylation and dephosphorylation of a protein
Conradi, Carsten +2 more
core +2 more sources
PHYTOCHROME and PROTEIN PHOSPHORYLATION [PDF]
Photochemistry and Photobiology, 1990 Abstract— The molecular mode of signal transduction triggered by phytochrome is unknown. One characteristic structural/topographic feature of the physiologically active form (Pfr) of phytochrome is that its tetrapyrrole chromophore becomes preferentially exposed in the Pfr form (compared to the Pr form).
B R, Singh, P S, Song
openaire +2 more sources
Protein phosphorylation in yeast mitochondria [PDF]
, 1987 We describe the identification and submitochondrial localization of four protein kinases and of their target proteins in derepressed yeast mitochondria. The activity of one of the kinases depends on the presence of cyclic AMP (cAMP).
Ashwell +37 more
core +2 more sources
Prevention and partial reversion of the lupus phenotype in ABIN1[D485N] mice by an IRAK4 inhibitor
Lupus Science and Medicine, 2021 Objective We have reported previously that the IRAK4 inhibitor PF06426779 given to ubiquitin-binding-defective ABIN1[D485N] mice at 6 weeks of age prevents the major facets of lupus that develop 10 weeks later.
Philip Cohen +5 more
doaj +1 more source
The role of phosphorylation and dephosphorylation of shell matrix proteins in shell formation : an in vivo and in vitro study [PDF]
, 2018 Protein phosphorylation is a fundamental mechanism regulating many aspects of cellular processes. Shell matrix proteins (SMPs) control crystal nucleation, polymorphism, morphology, and organization of calcium carbonate crystallites during shell formation.
Du, J., Liu, C., Xu, G., Zhang, R.
core +2 more sources
PKCɛ switches Aurora B specificity to exit the abscission checkpoint
Nature Communications, 2016 The Aurora B abscission checkpoint is activated when DNA is retained in the cleavage furrow on completion of anaphase. Here the authors show that PKCɛ directly phosphorylates Aurora B triggering a switch in Aurora B substrate specificity to elicit ...
Tanya Pike +4 more
doaj +1 more source