Results 21 to 30 of about 897,439 (267)

Protein phosphorylation in cyanobacteria [PDF]

open access: yesMicrobiology, 1994
The post-translational modification of proteins by phosphorylation may take a variety of forms, but in essence it is always a component of a process of adaptation that enables cells to sense and respond to changes in their external or internal environments.
openaire   +2 more sources

Structural and dynamic determinants for highly selective RET kinase inhibition reveal cryptic druggability

open access: yesJournal of Advanced Research, 2023
Introduction: The structural and dynamic determinants that confer highly selective RET kinase inhibition are poorly understood. Objectives: To explore the druggability landscape of the RET active site in order to uncover structural and dynamic ...
Moustafa A. Shehata   +6 more
doaj   +1 more source

The E3 ubiquitin ligase ZNRF2 is a substrate of mTORC1 and regulates its activation by amino acids

open access: yeseLife, 2016
The mechanistic Target of Rapamycin complex 1 (mTORC1) senses intracellular amino acid levels through an intricate machinery, which includes the Rag GTPases, Ragulator and vacuolar ATPase (V-ATPase).
Gerta Hoxhaj   +9 more
doaj   +1 more source

A genetically-encoded crosslinker screen identifies SERBP1 as a PKCε substrate influencing translation and cell division

open access: yesNature Communications, 2021
PKCε is known to exert a role in genome protection by directly phosphorylating and switching the specificity of Aurora B. Here the authors identify SERBP1 as a parallel mitotic PKCε substrate controlling translation and ensuring the integrity of ...
Silvia Martini   +11 more
doaj   +1 more source

USP45 and Spindly are part of the same complex implicated in cell migration

open access: yesScientific Reports, 2018
Ubiquitylation is a protein modification implicated in several cellular processes. This process is reversible by the action of deubiquinating enzymes (DUBs).
Claudia Conte   +3 more
doaj   +1 more source

An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function

open access: yesNature Communications, 2023
Autophosphorylation controls the transition between discrete functional and conformational states in protein kinases, yet the structural and molecular determinants underlying this fundamental process remain unclear.
Hipólito Nicolás Cuesta-Hernández   +10 more
doaj   +1 more source

Tissue environment, not ontogeny, defines murine intestinal intraepithelial T lymphocytes

open access: yeseLife, 2021
Tissue-resident intestinal intraepithelial T lymphocytes (T-IEL) patrol the gut and have important roles in regulating intestinal homeostasis. T-IEL include both induced T-IEL, derived from systemic antigen-experienced lymphocytes, and natural T-IEL ...
Alejandro J Brenes   +8 more
doaj   +1 more source

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

open access: yesFEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho   +3 more
wiley   +1 more source

Determination of VPS34/PIK3C3 Activity in vitro Utilising 32P-γATP

open access: yesBio-Protocol, 2016
VPS34 is the only class III phosphatidylinositol-3-kinase (PI3K) in mammalian cells and produces the vast majority of cellular phosphatidylinositol-3-phosphate [PI(3)P].
Michael Munson, Ian Ganley
doaj   +1 more source

Functional characterization of C21ORF2 association with the NEK1 kinase mutated in human in diseases

open access: yesLife Science Alliance, 2023
This study shows that the endogenous NEK1 kinase and C21ORF2 form a tight complex in human cells and characterises the functional significance of the association of the two partner proteins. The NEK1 kinase controls ciliogenesis, mitosis, and DNA repair,
Mateusz Gregorczyk   +15 more
doaj   +1 more source

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