Reversible protein phosphorylation, regulated by protein kinases and phosphatases, mediates a switch between protein activity and cellular pathways that contribute to a large number of cellular processes.
Suereta eFortuin+8 more
doaj +1 more source
Advance in Reversible Covalent Kinase Inhibitors [PDF]
Reversible covalent kinase inhibitors (RCKIs) are a class of novel kinase inhibitors attracting increasing attention because they simultaneously show the selectivity of covalent kinase inhibitors, yet avoid permanent protein-modification-induced adverse effects.
arxiv
Positional information readout in $Ca^{2+}$ signaling [PDF]
Living cells respond to spatial signals. Signal transmission to the cell interior often involves the release of second messengers like $Ca^{2+}$ . They will eventually trigger a physiological response by activating kinases that in turn activate target proteins through phosphorylation. Here, we investigate theoretically how positional information can be
arxiv +1 more source
KA1-targeted regulatory domain mutations activate Chk1 in the absence of DNA damage [PDF]
The Chk1 protein kinase is activated in response to DNA damage through ATR-mediated phosphorylation at multiple serine-glutamine (SQ) residues within the C-terminal regulatory domain, however the molecular mechanism is not understood. Modelling indicates
Freire, Raimundo+6 more
core +1 more source
Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase. [PDF]
Protein phosphatases are integral components of the cellular signaling machinery in eukaryotes, regulating diverse aspects of growth and development. The genome of the filamentous fungus and model organism Neurospora crassa encodes catalytic subunits for
Borkovich, Katherine A+3 more
core +2 more sources
Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization
Bone morphogenetic protein (BMP) receptors are single pass transmembrane serine/threonine kinases that form tetrameric complexes comprised of two type I and two type II BMP receptors.
Christopher Agnew+10 more
doaj +1 more source
Case report: A novel frameshift mutation in BRSK2 causes autism in a 16-year old Chinese boy
Serine/threonine protein kinases are involved in axon formation and neuronal polarization and have recently been implicated in autism spectrum disorder (ASD) and neurodevelopmental disorders (NDD).
Yu Hu+18 more
doaj +1 more source
Inferring the Sign of Kinase-Substrate Interactions by Combining Quantitative Phosphoproteomics with a Literature-Based Mammalian Kinome Network [PDF]
Protein phosphorylation is a reversible post-translational modification commonly used by cell signaling networks to transmit information about the extracellular environment into intracellular organelles for the regulation of the activity and sorting of proteins within the cell.
arxiv +1 more source
Using the structural kinome to systematize kinase drug discovery [PDF]
Kinase-targeted drug design is challenging. It requires designing inhibitors that can bind to specific kinases when all kinase catalytic domains share a common folding scaffold that binds ATP. Thus, obtaining the desired selectivity, given the whole human kinome, is a fundamental task during early-stage drug discovery.
arxiv
A knowledge graph representation learning approach to predict novel kinase-substrate interactions [PDF]
The human proteome contains a vast network of interacting kinases and substrates. Even though some kinases have proven to be immensely useful as therapeutic targets, a majority are still understudied. In this work, we present a novel knowledge graph representation learning approach to predict novel interaction partners for understudied kinases.
arxiv