Results 101 to 110 of about 116,902 (309)
Poly(ADP-ribose)polymerase-1 modulates microglial responses to amyloid β
Background Amyloid β (Aβ) accumulates in Alzheimer's disease (AD) brain. Microglial activation also occurs in AD, and this inflammatory response may contribute to disease progression.
Kauppinen Tiina M +9 more
doaj +1 more source
Poli(ADP-ribóz) mintázat vizsgálata HEK293T sejtvonalban PARP-1 és PARP-2 siRNS alkalmazásával
PARP-1 és PARP-2 poli(ADP-ribóz) mintázatát vizsgálatuk transzfekciót követően siRNS és scrRNS alkalmazásával.A PARP-1 gátlása a auto-poli(ADP-ribozil)ációs szintjének a csökkenéséhez vezetett.
Kassay, Norbert
core
Copyright information:Taken from "Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1: a nuclear target protein of PARP-1"http://www.biomedcentral.com/1471-2199/8/96BMC Molecular Biology
Sylvain L Guérin (83633) +3 more
core +1 more source
This study introduces a biomimetic “nanofusion” platform that integrates the biostability of threose nucleic acids (TNA) with homotypic cell‐membrane cloaking to combat drug‐resistant TNBC. By leveraging a non‐canonical membrane‐fusion pathway for direct cytosolic delivery, the platform bypasses endosomal sequestration. To achieve potent AKT2 silencing
Wei Zheng +7 more
wiley +1 more source
PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration
The normal function of poly (ADP-ribose) polymerase-1 (PARP-1) is the routine repair of DNA damage by adding poly (ADP ribose) polymers in response to a variety of cellular stresses.
Alexander Jonathan S +2 more
doaj +1 more source
Copyright information:Taken from "Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1: a nuclear target protein of PARP-1"http://www.biomedcentral.com/1471-2199/8/96BMC Molecular Biology
Sylvain L Guérin (83633) +3 more
core +1 more source
TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando +2 more
wiley +1 more source
Presently, humanity is confronted with a range of diseases that have high death rates, especially those linked to cancerous growths. Several enzymes and proteins have been discovered as highly attractive targets for cancer treatment.
Mahmoud A. El Hassab +3 more
doaj +1 more source
This study uncovers a metabolic‐epigenetic axis licensing zygotic genome activation (ZGA) in mouse embryos. A developmental decline in NAD+ levels activates PARP7, which mono‐ADP‐ribosylates and stabilizes UHRF1. This modification promotes the establishment of permissive histone acetylation marks, thereby facilitating timely ZGA.
Guangyi Cao +13 more
wiley +1 more source
This study shows that in glioma stem cells (GSCs), RBM12 recruits ALKBH5 to remove m6A from SLC7A5 transcripts, thereby enhancing mRNA stability, which elevates large neutral amino acid (LNAA) levels and activates mTORC1, promoting GSC proliferation, self‐renewal, and tumor growth.
Hong Lei +18 more
wiley +1 more source

