Results 101 to 110 of about 116,902 (309)

Poly(ADP-ribose)polymerase-1 modulates microglial responses to amyloid β

open access: yesJournal of Neuroinflammation, 2011
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

open access: yes, 2011
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  

Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1: a nuclear target protein of PARP-1-10

open access: yes, 2011
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

Membrane Fusion‐Mediated Cytosolic Delivery of Threose Nucleic Acids via Homotypic Nanoparticles Overcomes Drug Resistance in Triple‐Negative Breast Cancer

open access: yesAdvanced Science, EarlyView.
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

open access: yesCell Communication and Signaling, 2010
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

Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1: a nuclear target protein of PARP-1-6

open access: yes, 2011
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

open access: yesAdvanced Science, EarlyView.
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

Multi-stage structure-based virtual screening approach combining 3D pharmacophore, docking and molecular dynamic simulation towards the identification of potential selective PARP-1 inhibitors

open access: yesBMC Chemistry
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

NAD+ Metabolism Licenses Zygotic Genome Activation via PARP7‐Mediated ADP‐Ribosylation of UHRF1 in Mouse Early Embryos

open access: yesAdvanced Science, EarlyView.
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

RBM12 Maintains Glioma Stem Cells by Activating Amino Acid‐Dependent mTORC1 Signaling via SLC7A5 mRNA Stabilization

open access: yesAdvanced Science, EarlyView.
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

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