Evidence map›Paper›PMID 25801767›Full record

ArticleScientific reports2015

Caught in action: selecting peptide aptamers against intrinsically disordered proteins in live cells.

Jacqueline D Cobbert, Christopher DeMott, Subhabrata Majumder, Eric A Smith, Sergey Reverdatto, David S Burz, Kathleen A McDonough, Alexander Shekhtman

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Conditional protein splicing of thebioRxiv : the preprint server for biology · 2024
    Article
  3. Review
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  5. Article
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  8. Article
  9. Article
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  12. Article
  13. Article
  14. Review
  15. Review
  16. Peptide aptamers: development and applications.Current topics in medicinal chemistry · 2015
    Review
  17. Synthetic biology for pharmaceutical drug discovery.Drug design, development and therapy · 2015
    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

8 authors at 1 institution in 1 country.

Jacqueline D CobbertDepartment of Chemistry, University at Albany, Albany, NY.
Christopher DeMottDepartment of Chemistry, University at Albany, Albany, NY.
Subhabrata MajumderDepartment of Chemistry, University at Albany, Albany, NY.
Eric A SmithWadsworth Center, NY State Department of Health, Albany, NY.
Sergey ReverdattoDepartment of Chemistry, University at Albany, Albany, NY.
David S BurzDepartment of Chemistry, University at Albany, Albany, NY.
Kathleen A McDonoughWadsworth Center, NY State Department of Health, Albany, NY.
Alexander ShekhtmanDepartment of Chemistry, University at Albany, Albany, NY.
University at Albany, State University of New York · US

Funding

cAMP signaling pathways within Mycobacterium tuberculosisR01AI063499 · NIAID · WADSWORTH CENTER · PI MCDONOUGH, KATHLEEN A · 2005 to 2016
$2.8M
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
NIAID NIH HHS R01 AI063499NIAID NIH HHS R01AI063499NIGMS NIH HHS GM085006NIGMS NIH HHS R01 GM085006
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) or unstructured segments within proteins play an important role in cellular physiology and pathology. Low cellular concentration, multiple binding partners, frequent post-translational modifications and the presence of multiple conformations make it difficult to characterize IDP interactions in intact cells. We used peptide aptamers selected by using the yeast-two-hybrid scheme and in-cell NMR to identify high affinity binders to transiently structured IDP and unstructured segments at atomic resolution. Since both the selection and characterization of peptide aptamers take place inside the cell, only physiologically relevant conformations of IDPs are targeted. The method is validated by using peptide aptamers selected against the prokaryotic ubiquitin-like protein, Pup, of the mycobacterium proteasome. The selected aptamers bind to distinct sites on Pup and have vastly different effects on rescuing mycobacterial proteasome substrate and on the survival of the Bacille-Calmette-Guèrin, BCG, strain of M. bovis. This technology can be applied to study the elusive action of IDPs under near physiological conditions.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAptamers, PeptideBacterial ProteinsBinding SitesIntrinsically Disordered ProteinsMicrobial ViabilityModels, MolecularMolecular Sequence DataMycobacterium bovisMycobacterium tuberculosisProteasome Endopeptidase ComplexProtein BindingProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryAptamers, PeptideBacterial ProteinsIntrinsically Disordered ProteinsProteasome Endopeptidase ComplexPup protein, Mycobacterium tuberculosisUbiquitins

Identifiers

PMID25801767
PMCPMC4371151
OpenAlexW2083715061

What OpenQuestion holds

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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 OpenQuestion graph.