Articles with "acidic domain" as a keyword



Photo from wikipedia

Erratum to: Acidic domains differentially read histone H3 lysine 4 methylation status and are widely present in chromatin-associated proteins

Sign Up to like & get
recommendations!
Published in 2017 at "Science China Life Sciences"

DOI: 10.1007/s11427-017-9025-9

Abstract: Histone methylation is believed to provide binding sites for specific reader proteins, which translate histone code into biological function. Here we show that a family of acidic domain-containing proteins including nucleophosmin (NPM1), pp32, SET/TAF1β, nucleolin… read more here.

Keywords: differentially read; methylation; present chromatin; acidic domains ... See more keywords
Photo from wikipedia

The acidic domain of Hmga2 and the domain’s linker region are critical for driving self-renewal of hematopoietic stem cell

Sign Up to like & get
recommendations!
Published in 2022 at "International Journal of Hematology"

DOI: 10.1007/s12185-021-03274-9

Abstract: High mobility group AT-hook 2 (Hmga2) is a chromatin modifier protein that plays a critical role in fetal development and leukemia propagation by binding to chromatin and DNA via its AT-hook domains. However, the molecular… read more here.

Keywords: self renewal; domain; linker region; acidic domain ... See more keywords
Photo from wikipedia

KSHV LANA acetylation-selective acidic domain reader sequence mediates virus persistence

Sign Up to like & get
recommendations!
Published in 2020 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.2004809117

Abstract: Significance Understanding how viruses modulate host cell function is central to prospects for potential therapies. A recently described mechanism mediates selective protein interactions between acidic domain readers and unacetylated, lysine-rich regions, opposite of bromodomain function.… read more here.

Keywords: latency; acetylation; acidic domain; domain reader ... See more keywords
Photo from wikipedia

The Acidic Domain of the chloroplast RNA binding protein CP31A is supporting cold-tolerance of Arabidopsis thaliana.

Sign Up to like & get
recommendations!
Published in 2021 at "Journal of experimental botany"

DOI: 10.1093/jxb/erab165

Abstract: Chloroplast RNA processing requires a large number of nuclear-encoded RNA binding proteins (RBPs) that are imported post-translationally into the organelle. The chloroplast ribonucleoprotein 31A (CP31A) supports RNA editing at 13 sites and also supports the… read more here.

Keywords: rna; chloroplast; acidic domain; cp31a ... See more keywords