Evidence map›Paper›PMID 24586658›Full record

ArticlePloS one2014

Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa).

Babi Ramesh Reddy Nallamilli, Mariola J Edelmann, Xiaoxian Zhong, Feng Tan, Hana Mujahid, Jian Zhang, Bindu Nanduri, Zhaohua Peng

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

56 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Article
  3. Response ofJournal of bacteriology · 2024
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  4. International journal of molecular sciences · 2024
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  5. Article
  6. Article
  7. Global Analysis of Lysine Lactylation of Germinated Seeds in Wheat.International journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
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  13. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Babi Ramesh Reddy NallamilliDepartment of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
Mariola J EdelmannInstitute of Genomics, Biocomputing and Biotechnology, Mississippi Agricultural and Forestry Experimental Station, Mississippi State University, Starkville, Mississippi, United States of America.
Xiaoxian ZhongDepartment of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
Feng TanDepartment of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
Hana MujahidDepartment of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
Jian ZhangDepartment of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
Bindu NanduriInstitute of Genomics, Biocomputing and Biotechnology, Mississippi Agricultural and Forestry Experimental Station, Mississippi State University, Starkville, Mississippi, United States of America ; College of Veterinary Medicine, Mississippi State University, Starkville, Mississippi, United States of America.
Zhaohua PengDepartment of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
Mississippi State University · USExperimental Station · US

Funding

Training and Mentoring Core P20GM103476 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI MICHAEL R GARRETT · 2012 to 2026
$60.2M
NIGMS NIH HHS P20 GM103476
6 · The paper itself

Abstract

Lysine acetylation is a reversible, dynamic protein modification regulated by lysine acetyltransferases and deacetylases. Recent advances in high-throughput proteomics have greatly contributed to the success of global analysis of lysine acetylation. A large number of proteins of diverse biological functions have been shown to be acetylated in several reports in human cells, E.coli, and dicot plants. However, the extent of lysine acetylation in non-histone proteins remains largely unknown in monocots, particularly in the cereal crops. Here we report the mass spectrometric examination of lysine acetylation in rice (Oryza sativa). We identified 60 lysine acetylated sites on 44 proteins of diverse biological functions. Immunoblot studies further validated the presence of a large number of acetylated non-histone proteins. Examination of the amino acid composition revealed substantial amino acid bias around the acetylation sites and the amino acid preference is conserved among different organisms. Gene ontology analysis demonstrates that lysine acetylation occurs in diverse cytoplasmic, chloroplast and mitochondrial proteins in addition to the histone modifications. Our results suggest that lysine acetylation might constitute a regulatory mechanism for many proteins, including both histones and non-histone proteins of diverse biological functions.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceBiological PhenomenaBlotting, WesternChromatography, AffinityGene OntologyHumansLysineMolecular Sequence DataOryzaPlant ProteinsProteomeProteomicsTandem Mass SpectrometryLysinePlant ProteinsProteome

Identifiers

PMID24586658
PMCPMC3930695
OpenAlexW2056142322

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.