Evidence map›Paper›PMID 24692227›Full record

ArticleChembiochem : a European journal of chemical biology2014

Using singular value decomposition to characterize protein-protein interactions by in-cell NMR spectroscopy.

Subhabrata Majumder, Christopher M DeMott, David S Burz, Alexander Shekhtman

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. First hyperpolarized [2-Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Article
  4. Controlling and quantifying protein concentration in Escherichia coli.Protein science : a publication of the Protein Society · 2019
    Article
  5. Review
  6. Review
  7. Review
  8. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

4 authors.

Subhabrata MajumderDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Ave., Albany, NY 12222 (USA).
Christopher M DeMott
David S Burz
Alexander Shekhtman

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 GM085006NIGMS NIH HHS R01 GM085006
6 · The paper itself

Abstract

Distinct differences between how model proteins interact in-cell and in vitro suggest that the cytosol might have a profound effect in modulating protein-protein and/or protein-ligand interactions that are not observed in vitro. Analyses of in-cell NMR spectra of target proteins interacting with physiological partners are further complicated by low signal-to-noise ratios, and the long overexpression times used in protein-protein interaction studies may lead to changes in the in-cell spectra over the course of the experiment. To unambiguously resolve the principal binding mode between two interacting species against the dynamic cellular background, we analyzed in-cell spectral data of a target protein over the time course of overexpression of its interacting partner by using single-value decomposition (SVD). SVD differentiates between concentration-dependent and concentration-independent events and identifies the principal binding mode between the two species. The analysis implicates a set of amino acids involved in the specific interaction that differs from previous NMR analyses but is in good agreement with crystallographic data.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsMolecular Sequence DataMycobacterium tuberculosisProtein Interaction Domains and MotifsProteinsProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentUbiquitinsAdenosine TriphosphatasesBacterial ProteinsMpa protein, Mycobacterium tuberculosisProteinsPup protein, Mycobacterium tuberculosisUbiquitinsNMR spectroscopyprotein-protein interactionssingle-cell measurementssingle-value decompositionstatistical analysis

Identifiers

PMID24692227
PMCPMC4041589

What OpenQuestion holds

Textmetadata
LicenceTDM
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.