Evidence map›Paper›PMID 29039649›Full record

ArticleBiochemistry2018

Comparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein.

Peijia Yuan, Nadia G D'Lima, Sarah A Slavoff

Open access · bronzeAbstract readComparative StudyValidation Study
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Cellular function of the GndA microprotein during heat shock.bioRxiv : the preprint server for biology · 2025
    Article
  2. Eukaryotic Microproteins.Annual review of biochemistry · 2025
    Review
  3. Article
  4. Biophysical characterization of high-confidence, small human proteins.bioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Rescue ofeLife · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Identification of Translation Start Sites in Bacterial Genomes.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  13. Article
  14. Review
  15. EcoSal Plus · 2020
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Genes within Genes in Bacterial Genomes.Microbiology spectrum · 2018
    Review
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 at 1 institution in 1 country.

Peijia YuanDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.
Nadia G D'LimaDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.
Sarah A SlavoffDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.ORCID 0000-0002-4443-2070
Yale University · US

Funding

Structural and functional roles of the microprotein NoBody in mRNA decapping and decayR01GM122984 · NIGMS · YALE UNIVERSITY · PI SLAVOFF, SARAH ANN · 2017 to 2021
$1.6M
NIGMS NIH HHS R01 GM122984
6 · The paper itself

Abstract

Recent advances in proteomics and genomics have enabled discovery of thousands of previously nonannotated small open reading frames (smORFs) in genomes across evolutionary space. Furthermore, quantitative mass spectrometry has recently been applied to analysis of regulated smORF expression. However, bottom-up proteomics has remained relatively insensitive to membrane proteins, suggesting they may have been underdetected in previous studies. In this report, we add biochemical membrane protein enrichment to our previously developed label-free quantitative proteomics protocol, revealing a never-before-identified heat shock protein in Escherichia coli K12. This putative smORF-encoded heat shock protein, GndA, is likely to be ∼36-55 amino acids in length and contains a predicted transmembrane helix. We validate heat shock-regulated expression of the gndA smORF and demonstrate that a GndA-GFP fusion protein cofractionates with the cell membrane. Quantitative membrane proteomics therefore has the ability to reveal nonannotated small proteins that may play roles in bacterial stress responses.

Indexed as

Heat-Shock ResponseModels, MolecularOpen Reading FramesChromatography, High Pressure LiquidEscherichia coliEscherichia coli K12Escherichia coli ProteinsGene Expression Regulation, BacterialGreen Fluorescent ProteinsHeat-Shock ProteinsHeat-Shock Proteins, SmallMembrane ProteinsMolecular Sequence AnnotationPhosphogluconate DehydrogenaseProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsEscherichia coli ProteinsGndA protein, E ColiGreen Fluorescent ProteinsHeat-Shock ProteinsHeat-Shock Proteins, SmallMembrane ProteinsPhosphogluconate Dehydrogenasephosphogluconate dehydrogenase (decarboxylating)Recombinant Fusion Proteins

Identifiers

PMID29039649
PMCPMC5761644
OpenAlexW2766669428

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.