Evidence map›Paper›PMID 36070201›Full record

ArticleProteomics2023

Large-scale top-down proteomics of the Arabidopsis thaliana leaf and chloroplast proteomes.

Qianjie Wang, Liangliang Sun, Peter Knut Lundquist

Abstract read
In one paragraph

Article in Proteomics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. ResNeXt-Based Rescoring Model for Proteoform Characterization in Top-Down Mass Spectra.Interdisciplinary sciences, computational life sciences · 2025
    Article
  8. Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. 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

3 authors.

Qianjie WangDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.ORCID 0000-0002-1824-7111
Liangliang SunDepartment of Chemistry, Michigan State University, East Lansing, Michigan, USA.ORCID 0000-0001-8939-5042
Peter Knut LundquistDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.ORCID 0000-0001-8390-8089

Funding

Computational tools for top down mass spectrometry based proteoform identification and proteogenomicsR01GM118470 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI Xiaowen Liu · 2016 to 2026
$2.7M
Quantitative top-down proteomics of human colorectal cancer cells and tumorsR01CA247863 · NCI · MICHIGAN STATE UNIVERSITY · PI HUMMON, AMANDA B., LIU, XIAOWEN · 2021 to 2025
$1.9M
Quantitative proteomics of Zebrafish embryos and blastomeresR01GM125991 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SUN, LIANGLIANG · 2018 to 2022
$1.7M
NCI NIH HHS R01 CA247863NIGMS NIH HHS R01 GM118470NIGMS NIH HHS R01 GM125991
6 · The paper itself

Abstract

We present a large-scale top-down proteomics (TDP) study of plant leaf and chloroplast proteins, achieving the identification of over 4700 unique proteoforms. Using capillary zone electrophoresis coupled with tandem mass spectrometry analysis of offline size-exclusion chromatography fractions, we identify 3198 proteoforms for total leaf and 1836 proteoforms for chloroplast, with 1024 and 363 proteoforms having post-translational modifications, respectively. The electrophoretic mobility prediction of capillary zone electrophoresis allowed us to validate post-translational modifications that impact the charge state such as acetylation and phosphorylation. Identified modifications included Trp (di)oxidation events on six chloroplast proteins that may represent novel targets of singlet oxygen sensing. Furthermore, our TDP data provides direct experimental evidence of the N- and C-terminal residues of numerous mature proteoforms from chloroplast, mitochondria, endoplasmic reticulum, and other sub-cellular localizations. With this information, we suggest true transit peptide cleavage sites and correct sub-cellular localization signal predictions. This large-scale analysis illustrates the power of top-down proteoform identification of post-translational modifications and intact sequences that can benefit our understanding of both the structure and function of hundreds of plant proteins.

Indexed as

ArabidopsisProteomeDNA-Binding ProteinsProtein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryDNA-Binding ProteinsProteomeArabidopsis thalianachloroplastmass spectrometrypost-translational modificationsproteoformsinglet oxygentop-down proteomicstransit peptide

Identifiers

PMID36070201
PMCPMC9957804

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.