Results 51 to 60 of about 312,553 (300)

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

Post-translational Modification Control of HBV Biological Processes

open access: yesFrontiers in Microbiology, 2018
Hepatitis B virus infection remains a global healthy issue that needs to be urgently solved. Novel strategies for anti-viral therapy are based on exploring the effective diagnostic markers and therapeutic targets of diseases caused by hepatitis B virus ...
Fan Yang
doaj   +1 more source

Insights into Regulators of p53 Acetylation

open access: yesCells, 2022
The tumor suppressor p53 is a transcription factor that regulates the expression of dozens of target genes and diverse physiological processes. To precisely regulate the p53 network, p53 undergoes various post-translational modifications and alters the ...
Mai Nagasaka   +6 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Necroptosis in cancer: insight from epigenetic, post-transcriptional and post-translational modifications

open access: yesJournal of Hematology & Oncology
Necroptosis represents a distinct form of programmed cell death that exhibits characteristics of both necrosis and apoptosis. Due to its potential to activate anti-cancer immune responses, utilizing necroptosis to enhance immune activity within the tumor
Jinxin Tang   +7 more
doaj   +1 more source

Organ‐specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides

open access: yesFEBS Letters, EarlyView.
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley   +1 more source

Current Understanding of SIRT7 Function and Its Emerging Roles in the Central Nervous System

open access: yesCells
SIRT7is an NAD+-dependent deacetylase predominantly localized in the nucleolus, where it plays important roles in chromatin regulation, transcriptional control, and cellular stress response.
Yuchen Jiao   +2 more
doaj   +1 more source

Tyrosine Sulfation as a Protein Post-Translational Modification

open access: yesMolecules, 2015
Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases.
Yuh-Shyong Yang   +5 more
doaj   +1 more source

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

open access: yesFEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes   +4 more
wiley   +1 more source

Putative post-translational modification sites in wheat AOX proteins.

open access: yes, 2018
Putative post-translational modification sites in wheat AOX proteins.
Zara B. York (5593592)   +4 more
core   +1 more source

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