Results 61 to 70 of about 5,280 (145)
PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
EMBO ReportsPoly(ADP-ribose) polymerase 1 (PARP1) is one of the first responders to DNA damage and plays crucial roles in recruiting DNA repair proteins through its activity – poly(ADP-ribosyl)ation (PARylation). The enrichment of DNA repair proteins at sites of DNA
Christopher Chin Sang +10 more
doaj +1 more source
Poly(ADP-Ribosyl)ation Affects Histone Acetylation and Transcription.
PLoS ONE, 2015 Poly(ADP-ribosyl)ation (PARylation) is a posttranslational protein modification catalyzed by members of the poly(ADP-ribose) polymerase (PARP) enzyme family.
Loredana Verdone +5 more
doaj +1 more source
Advanced Science, Volume 13, Issue 35, 24 June 2026.Antibody–drug conjugates (ADCs) transform breast cancer therapy, yet resistance limits their durability. Emerging evidence reveals that ADC failure is not solely tumor‐intrinsic but shaped by dynamic tumor–microenvironment interactions that alter drug delivery, processing, and response.
Minji Seo, Jangsoon Lee, Naoto T. Ueno
wiley +1 more source
Advanced Science, Volume 13, Issue 33, 15 June 2026.Lung cancer remains the leading cause of cancer‐related death. We investigated the role of the epigenetic regulator DMAP1 in NSCLC and found that its loss induces replication stress and DNA damage. This in turn activates type I IFN signaling via the cGAS–STING pathway and transcriptional ISG de‐repression, enhancing anti‐tumor immune responses ...
Kan Huang +10 more
wiley +1 more source
Cell ReportsSummary: Poly(ADP-ribosyl)ation (PARylation), catalyzed mainly by poly(ADP-ribose) polymerase (PARP)1, is a key posttranslational modification involved in DNA replication and repair.
Julie Rageul +5 more
doaj +1 more source
The Polymers of Life: Exploring Cellular Function Through Polymer Concepts
Advanced Science, Volume 13, Issue 33, 15 June 2026.Biomolecular phase separation reveals that a hidden layer of cellular organization is governed by the principles of polymer science. This review bridges polymer physics and cell biology, offering a primer on fundamental concepts, proposing a framework for interrogating cellular function, and synthesizing biophysical methods for decoding macromolecular ...
Mark Chen, Ashutosh Chilkoti
wiley +1 more source
Inputs and outputs of poly(ADP-ribosyl)ation: Relevance to oxidative stress
Redox Biology, 2014 Oxidative stress can cause DNA breaks which induce activation of the DNA nick sensor enzyme poly(ADP-ribose) polymerase-1 (PARP-1), part of the 17 member PARP enzyme family.
Csaba Hegedűs, László Virág
doaj +1 more source
Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1
Biomolecules, 2020 Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity.
Konstantin N. Naumenko +7 more
doaj +1 more source
Cryo‐EM structure of ALC1 in an open conformation bound to a PARylated nucleosome
Acta Crystallographica Section D, Volume 82, Issue 6, Page 683-699, June 2026.Reanalysis of a publicly available cryo‐EM dataset identifies a new conformation of the oncogenic chromatin remodeler ALC1/CHD1L bound to a PARylated nucleosome. This new structure reveals the position of the macro domain in the complex, and may help to understand the large conformational change leading to the activation of ALC1.Nucleosomes are the ...
Hannah R. Bridges +3 more
wiley +1 more source
Automodification of N‐terminal serine residues facilitates PARP2 release from DNA
The FEBS Journal, Volume 293, Issue 11, Page 3274-3287, June 2026.PARP2 is involved in detecting DNA damage and its N‐terminal role is largely unknown. Based on biochemical and biophysical data, our findings suggest that in the presence of HPF1, N‐terminal serine 8 and 73 are enriched in auto‐ADP‐ribosylation. Our results provide insight into the mechanistic role of PARP2 N‐terminus in the PARylation‐dependent ...
Saurabh Singh Dhakar +6 more
wiley +1 more source