ArticleBiochemistry research international2017
Biochemical Analysis of Histone Succinylation.
Article in Biochemistry research international, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases.Signal transduction and targeted therapy · 2024Review
- Protein succinylation: regulating metabolism and beyond.Frontiers in nutrition · 2024Review
- Post-translational modulation of cell signalling through protein succinylation.Exploration of targeted anti-tumor therapy · 2023Review
- One genome, many cell states: epigenetic control of innate immunity.Current opinion in immunology · 2022Review
- Histone succinylation and its function on the nucleosome.Journal of cellular and molecular medicine · 2021Review
- Compartmentalised acyl-CoA metabolism and roles in chromatin regulation.Molecular metabolism · 2020Review
- Succinylation Site Prediction Based on Protein Sequences Using the IFS-LightGBM (BO) Model.Computational and mathematical methods in medicine · 2020Article
- Urine dicarboxylic acids change in pre-symptomatic Alzheimer's disease and reflect loss of energy capacity and hippocampal volume.PloS one · 2020Article
- Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational modification (PTM) of proteins is used to regulate protein activity and stability. Histone PTMs are regarded as some of the most important, as they can directly regulate gene expression through chromatin reorganization. Recently, histone proteins were found to undergo succinylation, adding to other well-known PTMs such as acetylation, methylation, and phosphorylation. However, there is little information regarding the enzyme which catalyzes histone lysine succinylation. In fact, it is unclear whether this reaction is enzymatic. In this study, we tested histone succinylation activity
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.