Results 31 to 40 of about 138,869 (211)

Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization

open access: yesNature Communications, 2021
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

open access: yesFrontiers in Psychiatry, 2023
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

Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases

open access: yesBMC Genomics, 2010
A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A
Nyporko Alexey   +6 more
doaj   +1 more source

Detection of HBV C Protein Phosphorylation in the Cell

open access: yesBio-Protocol, 2015
Among the seven serines and one threonine in the carboxyl-terminus of HBV C protein, all but one (serine 183) appear in the context of RxxS/T consensus phosphoacceptor motifs and also overlap with other consensus motifs, such as S/TP, RS, SPRRR, RRRS/T ...
Jaesung Jung, Kyongmin Kim
doaj   +1 more source

Genome-wide survey of putative Serine/Threonine protein kinases in cyanobacteria

open access: yesBMC Genomics, 2007
Background Serine/threonine kinases (STKs) have been found in an increasing number of prokaryotes, showing important roles in signal transduction that supplement the well known role of two-component system.
Guan Xiangyu   +5 more
doaj   +1 more source

Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases

open access: yesLife, 2021
Protein phosphorylation is one of the most widely observed and important post-translational modification (PTM) processes. Protein phosphorylation is regulated by protein kinases, each of which covalently attaches a phosphate group to an amino acid side ...
Seung-Hyeon Seok
doaj   +1 more source

Structure of substrate-bound SMG1-8-9 kinase complex reveals molecular basis for phosphorylation specificity

open access: yeseLife, 2020
PI3K-related kinases (PIKKs) are large Serine/Threonine (Ser/Thr)-protein kinases central to the regulation of many fundamental cellular processes.
Lukas M Langer   +3 more
doaj   +1 more source

Phosphorylation and regulation of group II metabotropic glutamate receptors (mGlu2/3) in neurons

open access: yesFrontiers in Cell and Developmental Biology, 2022
Group II metabotropic glutamate (mGlu) receptors (mGlu2/3) are Gαi/o-coupled receptors and are primarily located on presynaptic axonal terminals in the central nervous system.
Li-Min Mao   +6 more
doaj   +1 more source

The juxtamembrane domain of StkP is phosphorylated and influences cell division in Streptococcus pneumoniae

open access: yesmBio
Eukaryotic-like membrane Ser/Thr protein kinases play a pivotal role in different aspects of bacterial physiology. In contrast to the diversity of their extracellular domains, their cytoplasmic catalytic domains are highly conserved.
Mélisse Hamidi   +9 more
doaj   +1 more source

Structure-based virtual screening for novel p38 MAPK inhibitors and a biological evaluation

open access: yesActa Materia Medica, 2023
Mitogen-activated protein kinases (MAPKs) are a group of serine-threonine protein kinases that can be activated by extracellular stimuli. MAPK14 (p38α) affects major disease processes, while inhibition of p38α has been shown to have potential therapeutic
Qinwen Zheng   +7 more
doaj   +1 more source

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