Results 61 to 70 of about 77,829 (292)

PARP7 as a new target for activating anti-tumor immunity in cancer

open access: yesEMBO Molecular Medicine
ADP-ribosyl transferases (ARTs) are a family of enzymes which catalyze the addition of a chain (PARylation) or a single moiety (MARylation) of ADP-ribose to their substrates.
Katerina Popova   +7 more
doaj   +1 more source

Nutrition-Based Modulation of Poly-ADP-Ribosylation and its possible role in Alzheimer’s disease [PDF]

open access: yes, 2015
Alzheimer’s Disease (AD) is the most common neurodegenerative disease and the main reason of dementia in the elderly. On the pathological point of view, it is characterized by extracellular aggregates of amyloid peptides and intracellular deposits of tau
Fuso, Andrea, Martire, Sara
core  

A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi. [PDF]

open access: yes, 2017
Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi.
Baddeley, David   +12 more
core   +2 more sources

SIRT4 positively regulates autophagy via ULK1, but independently of HDAC6 and OPA1

open access: yesFEBS Open Bio, EarlyView.
Cells expressing SIRT4 (H161Y), a catalytically inactive mutant of the sirtuin SIRT4, fail to upregulate LC3B‐II and exhibit a reduced autophagic flux under stress conditions. Interestingly, SIRT4(H161Y) promotes phosphorylation of ULK1 at S638 and S758 that are associated with inhibition of autophagy initiation.
Isabell Lehmkuhl   +13 more
wiley   +1 more source

PIK3CA Mutations Downregulate PPT1 to Promote Adipogenesis by Suppressing P300 Depalmitoylation and Phase Separation

open access: yesAdvanced Science, EarlyView.
This study demonstrates that somatic PIK3CA mutations suppress PPT1 expression via activation of the PI3K–AKT–c‐JUN axis. This reduction in PPT1 weakens its interaction with P300, thereby increasing palmitoylation at C1176 of P300 and protecting P300 from lysosomal degradation.
Hongrui Chen   +7 more
wiley   +1 more source

Activation of ADP-ribosylation Factor 1 GTPase-Activating Protein by Phosphatidylcholine-derived Diacylglycerols*

open access: yesJournal of Biological Chemistry, 1997
Disassembly of the coatomer from Golgi vesicles requires that the small GTP-binding protein ADP-ribosylation factor 1 (ARF1) hydrolyzes its bound GTP by the action of a GTPase-activating protein.
B. Antonny   +4 more
semanticscholar   +1 more source

5mC-hydroxylase activity is influenced by the PARylation of TET1 enzyme [PDF]

open access: yes, 2015
5-hydroxymethylcytosine is a new epigenetic modification deriving from the oxidation of 5-methylcytosine by the TET hydroxylase enzymes. DNA hydroxymethylation drives DNA demethylation events and is involved in the control of gene expression ...
CAIAFA, Paola   +3 more
core   +2 more sources

Plasma Proteomics Identifies TAOK3 as a Potential Biomarker of Rheumatoid Arthritis Activity and a Novel Therapeutic Target

open access: yesArthritis &Rheumatology, Accepted Article.
Objective Bone destruction associated with active rheumatoid arthritis (RA) remains a major therapeutic challenge, with a lack of reliable molecular markers reflecting bone injury. This study aims to identify novel biomarkers linked to bone destruction in active RA through proteomic analysis, providing new strategies for precise monitoring and targeted
Pengfei Xin   +15 more
wiley   +1 more source

Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1

open access: yesNature Communications
The chromatin remodeler ALC1 is activated by DNA damage-induced poly(ADP-ribose) deposited by PARP1/PARP2 and their co-factor HPF1. ALC1 has emerged as a cancer drug target, but how it is recruited to ADP-ribosylated nucleosomes to affect their ...
Luka Bacic   +8 more
doaj   +1 more source

Study of the role of transmembrane emp24 domain-containing protein 2 in oral squamous cell carcinoma [PDF]

open access: yesJournal of Applied Oral Science
Objective This study aimed to investigate the role of transmembrane emp24 domain-containing protein 2 (TMED2) in oral squamous cell carcinoma (OSCC). Methodology A bioinformatics analysis was first conducted to explore TMED2 expression in OSCC and its
RUAN Zhao-wei   +5 more
doaj   +1 more source

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