Evidence map›Paper›PMID 18626516›Full record

ArticlePloS one2008

In-cell biochemistry using NMR spectroscopy.

David S Burz, Alexander Shekhtman

Abstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Controlling and quantifying protein concentration in Escherichia coli.Protein science : a publication of the Protein Society · 2019
    Article
  6. Review
  7. Article
  8. Review
  9. A Unique Tool for Cellular Structural Biology: In-cell NMR.The Journal of biological chemistry · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. In-cell NMR spectroscopy.Progress in nuclear magnetic resonance spectroscopy · 2011
    Review
  16. Article
  17. Protein (19)F NMR in Escherichia coli.Journal of the American Chemical Society · 2010
    Article
  18. Article
  19. 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

2 authors.

David S BurzDepartment of Chemistry, State University of New York at Albany, Albany, New York, United States of America.
Alexander Shekhtman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biochemistry and structural biology are undergoing a dramatic revolution. Until now, mostly in vitro techniques have been used to study subtle and complex biological processes under conditions usually remote from those existing in the cell. We developed a novel in-cell methodology to post-translationally modify interactor proteins and identify the amino acids that comprise the interaction surface of a target protein when bound to the post-translationally modified interactors. Modifying the interactor proteins causes structural changes that manifest themselves on the interacting surface of the target protein and these changes are monitored using in-cell NMR. We show how Ubiquitin interacts with phosphorylated and non-phosphorylated components of the receptor tyrosine kinase (RTK) endocytic sorting machinery: STAM2 (Signal-transducing adaptor molecule), Hrs (Hepatocyte growth factor regulated substrate) and the STAM2-Hrs heterodimer. Ubiquitin binding mediates the processivity of a large network of interactions required for proper functioning of the RTK sorting machinery. The results are consistent with a weakening of the network of interactions when the interactor proteins are phosphorylated. The methodology can be applied to any stable target molecule and may be extended to include other post-translational modifications such as ubiquitination or sumoylation, thus providing a long-awaited leap to high resolution in cell biochemistry.

Indexed as

Adaptor Proteins, Signal TransducingBiochemistryCytological TechniquesDimerizationEndocytosisEndosomal Sorting Complexes Required for TransportEscherichia coliHumansMagnetic Resonance SpectroscopyModels, StatisticalPhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalReceptor Protein-Tyrosine KinasesUbiquitinAdaptor Proteins, Signal TransducingEndosomal Sorting Complexes Required for Transporthepatocyte growth factor-regulated tyrosine kinase substratePhosphoproteinsReceptor Protein-Tyrosine KinasesSTAM2 protein, humanUbiquitin

Identifiers

PMID18626516
PMCPMC2453524

What OpenQuestion holds

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Registered trials

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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.