Results 81 to 90 of about 6,418,118 (368)

Protein phosphorylation in stomatal movement

open access: yesPlant Signalling & Behavior, 2014
As research progresses on how guard cells perceive and transduce environmental cues to regulate stomatal movement, plant biologists are discovering key roles of protein phosphorylation.
Tong Zhang, Sixue Chen, A. Harmon
semanticscholar   +1 more source

The cytoskeletal control of B cell receptor and integrin signaling in normal B cells and chronic lymphocytic leukemia

open access: yesFEBS Letters, EarlyView.
In lymphoid organs, antigen recognition and B cell receptor signaling rely on integrins and the cytoskeleton. Integrins act as mechanoreceptors, couple B cell receptor activation to cytoskeletal remodeling, and support immune synapse formation as well as antigen extraction.
Abhishek Pethe, Tanja Nicole Hartmann
wiley   +1 more source

Mechanism of TNFα-induced downregulation of salt-inducible kinase 2 in adipocytes

open access: yesScientific Reports, 2023
Salt-inducible kinase 2 (SIK2) is highly expressed in white adipocytes, but downregulated in individuals with obesity and insulin resistance. These conditions are often associated with a low-grade inflammation in adipose tissue.
Magdaléna Vaváková   +3 more
doaj   +1 more source

Dynamics of allosteric action in multisite protein modification [PDF]

open access: yes, 2006
Protein functions in cells may be activated or modified by the attachment of several kinds of chemical groups. While protein phosphorylation, i.e. the attachment of a phosphoryl (PO$_3^-$) group, is the most studied form of protein modification, and is known to regulate the functions of many proteins, protein behavior can also be modified by ...
arxiv   +1 more source

Turnover of protein phosphorylation evolving under stabilizing selection

open access: yesFrontiers in Genetics, 2014
Most proteins are regulated by posttranslational modifications and changes in these modifications contribute to evolutionary changes as well as to human diseases.
C. Landry   +3 more
semanticscholar   +1 more source

Surfaceome: a new era in the discovery of immune evasion mechanisms of circulating tumor cells

open access: yesMolecular Oncology, EarlyView.
In the era of immunotherapies, many patients either do not respond or eventually develop resistance. We propose to pave the way for proteomic analysis of surface‐expressed proteins called surfaceome, of circulating tumor cells. This approach seeks to identify immune evasion mechanisms and discover potential therapeutic targets. Circulating tumor cells (
Doryan Masmoudi   +3 more
wiley   +1 more source

Protein Phosphorylation and Neuronal Function [PDF]

open access: yesJournal of Neurochemistry, 1985
Studies in the past several years have provided direct evidence that protein phosphorylation is involved in the regulation of neuronal function. Electrophysiological experiments have demonstrated that three distinct classes of protein kinases, i.e., cyclic AMP-dependent protein kinase, protein kinase C, and CaM kinase II, modulate physiological ...
Paul Greengard   +2 more
openaire   +3 more sources

Protein phosphorylation in neurodegeneration: friend or foe?

open access: yesFrontiers in Molecular Neuroscience, 2014
Protein misfolding and aggregation is a common hallmark in neurodegenerative disorders, including Alzheimer's disease (AD), Parkinson's disease (PD), and fronto-temporal dementia (FTD).
S. Tenreiro, K. Eckermann, T. Outeiro
semanticscholar   +1 more source

Targeting rapid TKI‐induced AXL upregulation overcomes adaptive ERK reactivation and exerts antileukemic effects in FLT3/ITD acute myeloid leukemia

open access: yesMolecular Oncology, EarlyView.
Adaptive ERK reactivation hinders FLT3 tyrosine kinase inhibitor (TKI) treatment in FLT3/ITD acute myeloid leukemia. Here, we report that FLT3 TKI treatment rapidly induces AXL expression and upregulation that is temporally associated with the adaptive ERK reactivation.
Tessa S. Seale   +9 more
wiley   +1 more source

N-site phosphorylation systems with 2N-1 steady states [PDF]

open access: yesarXiv, 2013
Multisite protein phosphorylation plays a prominent role in intracellular processes like signal transduction, cell-cycle control and nuclear signal integration. Many proteins are phosphorylated in a sequential and distributive way at more than one phosphorylation site.
arxiv  

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