Evidence map›Paper›PMID 31492684›Full record

ArticleMolecular & cellular proteomics : MCP2019

Comprehensive Analysis of the Lysine Succinylome and Protein Co-modifications in Developing Rice Seeds.

Xiaoxi Meng, Hana Mujahid, Yadong Zhang, Xiaojun Peng, Edilberto D Redoña, Cailin Wang, Zhaohua Peng

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Impact of Lysine Succinylation on the Biology of Fungi.Current issues in molecular biology · 2024
    Review
  8. Article
  9. Global Analysis of Lysine Lactylation of Germinated Seeds in Wheat.International journal of molecular sciences · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
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  19. Article
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

7 authors at 3 institutions in 2 countries.

Xiaoxi MengDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville MS, 39762.
Hana MujahidDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville MS, 39762.
Yadong ZhangDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville MS, 39762; Institute of Food Crops, Jiangsu Academy of Agricultural Sciences, Jiangsu High Quality Rice Research and Development Center, Nanjing Branch of China National Center for Rice Improvement, Nanjing 210014, China.
Xiaojun PengDepartment of Bioinformatics, Jingjie PTM Biolab Co. Ltd, Hangzhou 310018, China.
Edilberto D RedoñaDelta Research and Extension Center, Mississippi State University, Stoneville MS, 38776.
Cailin WangInstitute of Food Crops, Jiangsu Academy of Agricultural Sciences, Jiangsu High Quality Rice Research and Development Center, Nanjing Branch of China National Center for Rice Improvement, Nanjing 210014, China. Electronic address: clwang@jaas.ac.cn.
Zhaohua PengDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville MS, 39762. Electronic address: zp7@BCH.msstate.edu.
Mississippi State University · USJiangsu Academy of Agricultural Sciences · CNMississippi Delta Community College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine succinylation has been recognized as a post-translational modification (PTM) in recent years. It is plausible that succinylation may have a vaster functional impact than acetylation because of bulkier structural changes and more significant charge differences on the modified lysine residue. Currently, however, the quantity and identity of succinylated proteins and their corresponding functions in cereal plants remain largely unknown. In this study, we estimated the native succinylation occupancy on lysine was between 2% to 10% in developing rice seeds. Eight hundred fifty-four lysine succinylation sites on 347 proteins have been identified by a thorough investigation in developing rice seeds. Six motifs were revealed as preferred amino acid sequence arrangements for succinylation sites, and a noteworthy motif preference was identified in proteins associated with different biological processes, molecular functions, pathways, and domains. Remarkably, heavy succinylation was detected on major seed storage proteins, in conjunction with critical enzymes involved in central carbon metabolism and starch biosynthetic pathways for rice seed development. Meanwhile, our results showed that the modification pattern of

Indexed as

Protein Processing, Post-TranslationalAcetylationAcyl Coenzyme ABlotting, WesternCatalytic DomainLysineOryzaPlant ProteinsSeedsSuccinatesAcyl Coenzyme ALysinePlant ProteinsSuccinatessuccinyl-coenzyme Aacetylationlysine succinylationmass spectrometryplant biologypost-translational modificationsprotein modificationriceseedsstorage nutrientsuccinylome

Identifiers

PMID31492684
PMCPMC6885699
OpenAlexW2972211546

What OpenQuestion holds

Textmetadata
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.