Results 21 to 30 of about 34,146 (129)
Structural biology has the potential to illuminate the evolution of pathogen effectors and their commonalities that cannot be readily detected at the primary sequence level.
Kyungyong Seong, Ksenia V. Krasileva
doaj +1 more source
Host ADP-ribosylation and the SARS-CoV-2 macrodomain
The COVID-19 pandemic has prompted intense research efforts into elucidating mechanisms of coronavirus pathogenesis and to propose antiviral interventions.
N. Hoch
semanticscholar +1 more source
ING1 and 5-azacytidine act synergistically to block breast cancer cell growth. [PDF]
Inhibitor of Growth (ING) proteins are epigenetic "readers" that recognize trimethylated lysine 4 of histone H3 (H3K4Me3) and target histone acetyl transferase (HAT) and histone deacetylase (HDAC) complexes to chromatin.Here we asked whether ...
Satbir Thakur +7 more
doaj +1 more source
Emerging Concepts on the Role of ADP-Ribosylation
NAD+ has emerged as a crucial element in both bioenergetic and signaling pathways, since it acts as a key regulator of cellular and organism homeostasis.
Palmiro Poltronieri
doaj +1 more source
Abstract Ischemic stroke is known to cause the accumulation of misfolded proteins and loss of calcium homeostasis, leading to impairment of endoplasmic reticulum (ER) function and activating the unfolded protein response (UPR). PARP16 is an active (ADP‐ribosyl)transferase known tail‐anchored ER transmembrane protein with a cytosolic ...
Jinghuan Wang +6 more
openaire +2 more sources
The transcription factor Stat6 plays a critical role in interleukin-4-dependent gene activation. To mediate this function, Stat6 recruits canonical transcriptional co-activators including the histone acetyl transferases CREB-binding protein and NCoA-1 ...
S. Goenka, S. Cho, M. Boothby
semanticscholar +1 more source
Chemical Tools to Study Protein ADP-Ribosylation
Post-translational modification of substrate proteins plays crucial roles in the regulation of their activity, cellular localization, and ability to be recognized by other proteins.
Gerbrand J. van der Heden van Noort
semanticscholar +1 more source
Destabilization of Zn2+ coordination in ADP‐ribose transferase (polymerizing) by 6‐nitroso‐1,2‐benzopyrone coincidental with inactivation of the polymerase but not the DNA binding function [PDF]
6‐Nitroso‐ 1,2‐benzopyrone, an oxidation product of 6‐amino‐ 1,2‐benzopyrone, binds to the DNA‐recognizing domain of the ADP‐ribose transferase protein and preferentially destabilizes Zn2+ from one of the two zinc finger polypeptide complexes present in the intact enzyme, as determined by the loss of 50% of 65Zn2+ from the 65Zn2+‐isolated protein ...
Buki, Kalman G. +4 more
openaire +2 more sources
Chilling followed by incubation at 37°C causes a reduction in NAD+ levels which can be prevented by the poly(ADP‐ribose)transferase inhibitor 3‐aminobenzamide [PDF]
The exposure of cells for 60 min to a serum free medium at ice temperature followed by a return to normal culture conditions (30 min at 37°C) caused a dramatic decrease in NAD+ levels. This decrease in NAD+ was prevented by 3‐aminobenzamide. Alkaline elution analysis of DNA from cultures that were sisters to the ones utilized for measuring cellular NAD+
CANTONI, ORAZIO +3 more
openaire +4 more sources
Endothelin receptor type A (EDNRA) and the Hippo/YAP pathway form a self‐reinforcing loop that sustains triple‐negative breast cancer. EDNRA activates YAP through Gαq/11–Rho/ROCK–LATS signaling, while YAP/TEAD4 reciprocally drives EDNRA transcription.
Zehao Hong +10 more
wiley +1 more source

