Evidence map›Paper›PMID 29427760›Full record

ReviewJournal of proteomics2019

Interaction proteomics by using in-cell NMR spectroscopy.

Leonard Breindel, David S Burz, Alexander Shekhtman

Abstract readReview
In one paragraph

Review in Journal of proteomics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  2. Article
  3. Article
  4. Review
  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
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.

Leonard BreindelDepartment of Chemistry, University at Albany, State University of New York, Albany, NY 12222, USA.
David S BurzDepartment of Chemistry, University at Albany, State University of New York, Albany, NY 12222, USA.
Alexander ShekhtmanDepartment of Chemistry, University at Albany, State University of New York, Albany, NY 12222, USA. Electronic address: ashekhtman@albany.edu.

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 R01 GM085006
6 · The paper itself

Abstract

A synopsis of in-cell NMR spectroscopic approaches to study interaction proteomics in prokaryotic and eukaryotic cells is presented. We describe the use of in-cell NMR spectroscopy to resolve high resolution protein structures, discuss methodologies for determining and analyzing high and low affinity protein-target structural interactions, including intrinsically disordered proteins, and detail important functional interactions that result from these interactions. SIGNIFICANCE: The ultimate goal of structural and biochemical research is to understand how macromolecular interactions give rise to and regulate biological activity in living cells. The challenge is formidable due to the complexity that arises not only from the number of proteins (genes) expressed by the organism, but also from the combinatorial interactions between them. Despite ongoing efforts to decipher the complex nature of protein interactions, new methods for structurally characterizing protein complexes are needed to fully understand molecular networks. With the onset of in-cell NMR spectroscopy, molecular structures and interactions can be studied under physiological conditions shedding light on the structural underpinning of biological activity.

Indexed as

AnimalsHumansMagnetic Resonance SpectroscopyMolecular ImagingMolecular StructureNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Interaction MapsProteomicsIn-cell NMRNMR spectroscopyProtein-protein interactionsProtein-RNA interactionsProtein structure

Identifiers

PMID29427760
PMCPMC6082733

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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.