Results 11 to 20 of about 7,148,227 (413)

A secretory kinase complex regulates extracellular protein phosphorylation. [PDF]

open access: yeseLife, 2015
Although numerous extracellular phosphoproteins have been identified, the protein kinases within the secretory pathway have only recently been discovered, and their regulation is virtually unexplored.
Cui, Jixin   +5 more
core   +3 more sources

Dissecting the role of protein phosphorylation: a chemical biology toolbox.

open access: yesChemical Society Reviews, 2022
Protein phosphorylation is a crucial regulator of protein and cellular function, yet, despite identifying an enormous number of phosphorylation sites, the role of most is still unclear. Each phosphoform, the particular combination of phosphorylations, of
Timothy S. Bilbrough   +2 more
semanticscholar   +1 more source

Role of protein phosphorylation in cell signaling, disease, and the intervention therapy

open access: yesMedComm, 2022
Protein phosphorylation is an important post‐transcriptional modification involving an extremely wide range of intracellular signaling transduction pathways, making it an important therapeutic target for disease intervention.
K. Pang   +10 more
semanticscholar   +1 more source

Systematic discovery of biomolecular condensate-specific protein phosphorylation

open access: yesNature Chemical Biology, 2022
Reversible protein phosphorylation is an important mechanism for regulating (dis)assembly of biomolecular condensates. However, condensate-specific phosphosites remain largely unknown, thereby limiting our understanding of the underlying mechanisms. Here,
Sindhuja Sridharan   +9 more
semanticscholar   +1 more source

Protein Phosphorylation in Cancer: Role of Nitric Oxide Signaling Pathway

open access: yesBiomolecules, 2021
Nitric oxide (NO), a free radical, plays a critical role in a wide range of physiological and pathological processes. Due to its pleiotropic function, it has been widely investigated in various types of cancers and is strongly associated with cancer ...
Xinran Liu   +5 more
semanticscholar   +1 more source

Mapping of a N-terminal α-helix domain required for human PINK1 stabilization, Serine228 autophosphorylation and activation in cells

open access: yesOpen Biology, 2022
Autosomal recessive mutations in the PINK1 gene are causal for Parkinson's disease (PD). PINK1 encodes a mitochondrial localized protein kinase that is a master-regulator of mitochondrial quality control pathways.
Poonam Kakade   +14 more
doaj   +1 more source

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry [PDF]

open access: yes, 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

On the existence of Hopf bifurcations in the sequential and distributive double phosphorylation cycle [PDF]

open access: yes, 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

Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase

open access: yeseLife, 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

Protein phosphorylation in yeast mitochondria [PDF]

open access: yes, 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

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