Results 71 to 80 of about 261,891 (384)

ERBIN limits epithelial cell plasticity via suppression of TGF‐β signaling

open access: yesFEBS Letters, EarlyView.
In breast and lung cancer patients, low ERBIN expression correlates with poor clinical outcomes. Here, we show that ERBIN inhibits TGF‐β‐induced epithelial‐to‐mesenchymal transition in NMuMG breast and A549 lung adenocarcinoma cell lines. ERBIN suppresses TGF‐β/SMAD signaling and reduces TGF‐β‐induced ERK phosphorylation.
Chao Li   +3 more
wiley   +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

Binding of PTEN to Specific PDZ Domains Contributes to PTEN Protein Stability and Phosphorylation by Microtubule-associated Serine/Threonine Kinases*

open access: yesJournal of Biological Chemistry, 2005
The tumor suppressor phosphatase PTEN is a key regulator of cell growth and apoptosis that interacts with PDZ domains from regulatory proteins, including MAGI-1/2/3, hDlg, and MAST205.
M. Valiente   +7 more
semanticscholar   +1 more source

Organoids in pediatric cancer research

open access: yesFEBS Letters, EarlyView.
Organoid technology has revolutionized cancer research, yet its application in pediatric oncology remains limited. Recent advances have enabled the development of pediatric tumor organoids, offering new insights into disease biology, treatment response, and interactions with the tumor microenvironment.
Carla Ríos Arceo, Jarno Drost
wiley   +1 more source

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

Tv-RIO1 – an atypical protein kinase from the parasitic nematode Trichostrongylus vitrinus [PDF]

open access: yes, 2008
Background: Protein kinases are key enzymes that regulate a wide range of cellular processes, including cell-cycle progression, transcription, DNA replication and metabolic functions. These enzymes catalyse the transfer of phosphates to serine, threonine
Gasser, Robin B.   +3 more
core   +6 more sources

Vacuolar transport and function of Saccharomyces cerevisiae sterol ester hydrolase Tgl1

open access: yesFEBS Letters, EarlyView.
Tgl1, one of yeast sterol ester hydrolases, had been found on the lipid droplets where sterol esters are mainly stored. This study revealed that Tgl1 is transported into the vacuole depending on the ESCRT‐I–III complex, and that it exhibits intra‐vacuolar sterol ester hydrolase activity.
Takumi Nakatsuji   +5 more
wiley   +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

Modulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1 [PDF]

open access: yes, 2016
BACKGROUND: Modulation of protein activity by phosphorylation through kinases and subsequent de-phosphorylation by phosphatases is one of the most prominent cellular control mechanisms.
Dissmeyer, N.   +6 more
core   +2 more sources

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