Evidence map›Paper›PMID 38191978›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024

Native Capillary Electrophoresis-Mass Spectrometry of Near 1 MDa Non-Covalent GroEL/GroES/Substrate Protein Complexes.

Anne-Lise Marie, Florian Georgescauld, Kendall R Johnson, Somak Ray, John R Engen, Alexander R Ivanov

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–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. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  11. Article
  12. Native Proteomics by Capillary Zone Electrophoresis-Mass Spectrometry.Angewandte Chemie (International ed. in English) · 2024
    Article
  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

6 authors.

Anne-Lise MarieBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, USA.ORCID 0000-0002-7461-1838
Florian GeorgescauldBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, USA.
Kendall R JohnsonBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, USA.
Somak RayBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, USA.
John R EngenBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, USA.
Alexander R IvanovBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, USA.ORCID 0000-0002-4691-8488

Funding

Effect of methodological and biological variability on molecular profiling of extracellular vesicles in cancer detectionR01CA218500 · NCI · NORTHEASTERN UNIVERSITY · PI GHIRAN, IONITA CALIN, IVANOV, ALEXANDER R. · 2018 to 2022
$4.0M
Robust ultra-high sensitivity proteomic technologies for limited samplesR35GM136421 · NIGMS · NORTHEASTERN UNIVERSITY · PI Alexander R. Ivanov · 2020 to 2026
$3.4M
NCI NIH HHS R01 CA218500NIGMS NIH HHS R35 GM136421NIH HHS R01CA218500NIH HHS R35GM136421
6 · The paper itself

Abstract

Protein complexes are essential for proteins' folding and biological function. Currently, native analysis of large multimeric protein complexes remains challenging. Structural biology techniques are time-consuming and often cannot monitor the proteins' dynamics in solution. Here, a capillary electrophoresis-mass spectrometry (CE-MS) method is reported to characterize, under near-physiological conditions, the conformational rearrangements of ∽1 MDa GroEL upon complexation with binding partners involved in a protein folding cycle. The developed CE-MS method is fast (30 min per run), highly sensitive (low-amol level), and requires ∽10 000-fold fewer samples compared to biochemical/biophysical techniques. The method successfully separates GroEL

Indexed as

Protein FoldingProteinsElectrophoresis, CapillaryMass SpectrometryProtein ConformationProteinsATP-induced conformational rearrangementchaperonesGroELGroESnative capillary electrophoresis-mass spectrometry

Identifiers

PMID38191978
PMCPMC10953559

What Socratic 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 Socratic graph.