Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase [PDF]
Cell Metabolism, 2005 The AMP-activated protein kinase (AMPK) is a critical regulator of energy balance at both the cellular and whole-body levels. Two upstream kinases have been reported to activate AMPK in cell-free assays, i.e., the tumor suppressor LKB1 and calmodulin-dependent protein kinase kinase. However, evidence that this is physiologically relevant currently only
Hawley, Simon A. +7 more
openaire +4 more sources
Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP [PDF]
, 1999 Raf-1 phosphorylates and activates MEK-1, a kinase that activates the extracellular signal regulated kinases (ERK). This kinase cascade controls the proliferation and differentiation of different cell types.
A Minden +25 more
core +1 more source
Deactivatable Bisubstrate Inhibitors of Protein Kinases
Molecules, 2022 Bivalent ligands, including bisubstrate inhibitors, are conjugates of pharmacophores, which simultaneously target two binding sites of the biomolecule. Such structures offer attainable means for the development of compounds whose ability to bind to the ...
Tanel Sõrmus +4 more
doaj +1 more source
An evolutionary perspective on the kinome of malaria parasites [PDF]
, 2012 Malaria parasites belong to an ancient lineage that diverged very early from the main branch of eukaryotes. The approximately 90-member plasmodial kinome includes a majority of eukaryotic protein kinases that clearly cluster within the AGC, CMGC, TKL ...
Andrew B. Tobin +6 more
core +1 more source
Using the structural kinome to systematize kinase drug discovery [PDF]
arXiv, 2021 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
KSP: an integrated method for predicting catalyzing kinases of phosphorylation sites in proteins
BMC Genomics, 2020 Background Protein phosphorylation by kinases plays crucial roles in various biological processes including signal transduction and tumorigenesis, thus a better understanding of protein phosphorylation events in cells is fundamental for studying protein ...
Hongli Ma, Guojun Li, Zhengchang Su
doaj +1 more source
Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]
, 2018 Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika +3 more
core +1 more source
A knowledge graph representation learning approach to predict novel kinase-substrate interactions [PDF]
arXiv, 2022 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
Analysis of somatic mutations across the kinome reveals loss-of-function mutations in multiple cancer types [PDF]
, 2017 In this study we use somatic cancer mutations to identify important functional residues within sets of related genes. We focus on protein kinases, a superfamily of phosphotransferases that share homologous sequences and structural motifs and have many ...
Bose, Ron, Kumar, Runjun D
core +2 more sources
eLifeA study of two enzymes in the brain reveals new insights into how redox reactions regulate the activity of protein kinases.
Iván Plaza-Menacho
doaj +1 more source