Evidence map›Paper›PMID 25894651›Full record

ArticleBiochemistry2015

Probing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy.

Subhabrata Majumder, Jing Xue, Christopher M DeMott, Sergey Reverdatto, David S Burz, Alexander Shekhtman

Abstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. RNA Structure: Past, Future, and Gene Therapy Applications.International journal of molecular sciences · 2024
    Review
  7. Review
  8. Diffusion and Viscosity in Mixed Protein Solutions.The journal of physical chemistry. B · 2024
    Article
  9. Article
  10. Ligand-Based Competition Binding by Real-TimeJournal of medicinal chemistry · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells.Journal of the American Chemical Society · 2021
    Article
  19. Article
  20. 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.

Subhabrata MajumderDepartment of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
Jing XueDepartment of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
Christopher M DeMottDepartment of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
Sergey ReverdattoDepartment of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
David S BurzDepartment of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
Alexander ShekhtmanDepartment of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.

Funding

Real Time (RT) In-cell NMR technology to study protein interactions in live cellsR01GM085006 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHEKHTMAN, ALEXANDER · 2010 to 2021
$2.4M
NIGMS NIH HHS 5R01GM085006NIGMS NIH HHS R01 GM085006
6 · The paper itself

Abstract

Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, weak protein (quinary) interactions are an emergent property of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro. Cross-correlated relaxation-induced polarization transfer-based in-cell nuclear magnetic resonance allows the characterization of protein quinary interactions with atomic resolution inside live prokaryotic and eukaryotic cells. We show that RNAs are an important component of protein quinary interactions. Protein quinary interactions are unique to the target protein and may affect physicochemical properties, protein activity, and interactions with drugs.

Indexed as

Base SequenceDNA ProbesElectroporationHumansMagnetic Resonance SpectroscopyModels, MolecularProteinsRNATransfectionDNA ProbesProteinsRNA

Identifiers

PMID25894651
PMCPMC4447238

What OpenQuestion holds

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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.