Results 81 to 90 of about 1,989,427 (395)

Alterations in vasodilator-stimulated phosphoprotein (VASP) phosphorylation: associations with asthmatic phenotype, airway inflammation and β\u3csub\u3e2\u3c/sub\u3e-agonist use [PDF]

open access: yes, 2006
Background Vasodilator-stimulated phosphoprotein (VASP) mediates focal adhesion, actin filament binding and polymerization in a variety of cells, thereby inhibiting cell movement.
Batra, Vikas   +8 more
core   +1 more source

The Regulation of NF-κB Subunits by Phosphorylation

open access: yesCells, 2016
The NF-κB transcription factor is the master regulator of the inflammatory response and is essential for the homeostasis of the immune system. NF-κB regulates the transcription of genes that control inflammation, immune cell development, cell cycle ...
F. Christian, Emma L. Smith, R. Carmody
semanticscholar   +1 more source

Evolutionary interplay between viruses and R‐loops

open access: yesFEBS Letters, EarlyView.
Viruses interact with specialized nucleic acid structures called R‐loops to influence host transcription, epigenetic states, latency, and immune evasion. This Perspective examines the roles of R‐loops in viral replication, integration, and silencing, and how viruses co‐opt or avoid these structures.
Zsolt Karányi   +4 more
wiley   +1 more source

PROTAC-mediated conditional degradation of the WRN helicase as a potential strategy for selective killing of cancer cells with microsatellite instability

open access: yesScientific Reports
Multiple studies have demonstrated that cancer cells with microsatellite instability (MSI) are intolerant to loss of the Werner syndrome helicase (WRN), whereas microsatellite-stable (MSS) cancer cells are not.
Vikram Tejwani   +7 more
doaj   +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

Regulation of Op18 during Spindle Assembly in Xenopus Egg Extracts [PDF]

open access: yes, 2001
Oncoprotein 18 (Op18) is a microtubule-destabilizing protein that is negatively regulated by phosphorylation. To evaluate the role of the three Op18 phosphorylation sites in Xenopus (Ser 16, 25, and 39), we added wild-type Op18, a nonphosphorylatable ...
Andersen   +67 more
core   +4 more sources

Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)*

open access: yesJournal of Biological Chemistry, 1996
The small GTPase Rho is implicated in physiological functions associated with actin-myosin filaments such as cytokinesis, cell motility, and smooth muscle contraction.
M. Amano   +7 more
semanticscholar   +1 more source

Single‐cell insights into the role of T cells in B‐cell malignancies

open access: yesFEBS Letters, EarlyView.
Single‐cell technologies have transformed our understanding of T cell–tumor cell interactions in B‐cell malignancies, revealing new T‐cell subsets, functional states, and immune evasion mechanisms. This Review synthesizes these findings, highlighting the roles of T cells in pathogenesis, progression, and therapy response, and underscoring their ...
Laura Llaó‐Cid
wiley   +1 more source

Tau phosphorylation at Alzheimer\u27s disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated. [PDF]

open access: yes, 2016
Abnormal phosphorylation of the microtubule-associated protein tau is observed in many neurodegenerative diseases, including Alzheimer\u27s disease (AD).
Ando, Kanae   +6 more
core   +1 more source

The chloroplast import receptor Toc34 functions as preprotein-regulated GTPase [PDF]

open access: yes, 2002
Toc34 is a protein of the chloroplast outer envelope membrane that acts as receptor for preproteins containing a transit sequence. The recognition of preproteins by Toc34 is regulated by GTP binding and phosphorylation.
Hörth, P.   +5 more
core   +1 more source

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