Results 71 to 80 of about 391,128 (337)

MYST4 (MYST histone acetyltransferase (monocytic leukemia) 4) [PDF]

open access: yes, 2006
Review on MYST4 (MYST histone acetyltransferase (monocytic leukemia) 4), with data on DNA, on the protein encoded, and where the gene is ...
Vizmanos, JL
core   +1 more source

Targeting transcription factors associated with hemoglobinopathies: Lessons from successful interventions and implications for cancer

open access: yesMolecular Oncology, EarlyView.
This review summarizes the transcription factors, repressive chromatin‐modifying complexes, and epigenetic mechanisms that control fetal hemoglobin repression. Notably, many regulators of γ‐globin silencing also function in transcriptional and epigenetic networks that drive cancer, highlighting opportunities to translate advances in hemoglobinopathy ...
Meigen Yu   +3 more
wiley   +1 more source

Proximity labelling of pro-interleukin-1α reveals evolutionary conserved nuclear interactions

open access: yesNature Communications
Interleukin-1α is a suggested dual-function cytokine that diverged from interleukin-1β in mammals potentially by acquiring additional biological roles that relate to highly conserved regions in the pro-domain of interleukin-1α, including a nuclear ...
Rose Wellens   +11 more
doaj   +1 more source

BRD4 is a Histone Acetyltransferase that Evicts Nucleosomes from Chromatin

open access: yesNature Structural &Molecular Biology, 2016
Bromodomain protein 4 (BRD4) is a chromatin-binding protein implicated in cancer and autoimmune diseases that functions as a scaffold for transcription factors at promoters and super-enhancers.
B. N. Devaiah   +8 more
semanticscholar   +1 more source

ADP‐ribosylation: An emerging regulator of the epigenome

open access: yesMolecular Oncology, EarlyView.
ADP‐ribosylation has emerged as a dynamic epigenetic signaling mechanism that modifies histones and chromatin‐associated proteins. Through coordinated PARylation and MARylation, it integrates with other histone modifications to regulate chromatin structure, transcription factor activity, and gene expression, influencing genome function and disease ...
Cristel V. Camacho   +2 more
wiley   +1 more source

Acetyltransferase p300 Is a Putative Epidrug Target for Amelioration of Cellular Aging-Related Cardiovascular Disease

open access: yesCells, 2021
Cardiovascular disease is the leading cause of accelerated as well as chronological aging-related human morbidity and mortality worldwide. Genetic, immunologic, unhealthy lifestyles including daily consumption of high-carb/high-fat fast food, lack of ...
Asish K. Ghosh
doaj   +1 more source

Paclitaxel induces NM2‐dependent cellular contraction through GEF‐H1 dissociation from microtubules and RhoA/ROCK activation in cancer cells

open access: yesMolecular Oncology, EarlyView.
Taxanes are widely used chemotherapeutics whose effects on cellular mechanics remain poorly understood. We show that paclitaxel induces rapid cellular contraction by promoting GEF‐H1 dissociation from microtubules and non‐muscle myosin II activation through RhoA/ROCK.
Gloria Asensio‐Juárez   +5 more
wiley   +1 more source

Beyond Wolbachia—Can a small molecule control insect reproduction?

open access: yesCell Reports
Kaur et al.1 demonstrate reduced histone acetylation as a key mechanism underpinning Wolbachia’s paternal-effect embryonic lethality trait in Drosophila melanogaster.
Robson Kriiger Loterio   +1 more
doaj   +1 more source

Ada2 and Ada3 Regulate Hyphal Growth, Asexual Development, and Pathogenicity in Beauveria bassiana by Maintaining Gcn5 Acetyltransferase Activity

open access: yesMicrobiology Spectrum, 2023
The histone acetyltransferase (HAT) Gcn5 ortholog is essential for a variety of fungi. Here, we characterize the roles of Ada2 and Ada3, which are functionally linked to Gcn5, in the insect-pathogenic fungus Beauveria bassiana.
Shun-Juan Hu   +10 more
doaj   +1 more source

Emerging Role of Histone Acetyltransferase in Stem Cells and Cancer

open access: yesStem Cells International, 2018
Protein acetylation is one of the most important posttranslational modifications catalyzed by acetyltransferases and deacetylases, through the addition and removal of acetyl groups to lysine residues. Lysine acetylation can affect protein-nucleic acid or
D. Trisciuoglio   +2 more
semanticscholar   +1 more source

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