Evidence map›Paper›PMID 10688899›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Isolation of peptide aptamers that inhibit intracellular processes.

J H Blum, S L Dove, A Hochschild, J J Mekalanos

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

12 citing papers in PubMed, 72 citations in OpenAlex.

  1. Peptide Aptamer PA3 Attenuates the Viability ofFrontiers in microbiology · 2022
    Article
  2. Article
  3. Programmable biomaterials for dynamic and responsive drug delivery.Experimental biology and medicine (Maywood, N.J.) · 2016
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Peptide-mediated broad-spectrum plant resistance to tospoviruses.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  9. Article
  10. TEM-1 beta-lactamase as a scaffold for protein recognition and assay.Protein science : a publication of the Protein Society · 2002
    Article
  11. Targeted modification and transportation of cellular proteins.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  12. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

J H BlumDepartment of Microbiology, Shipley Institute of Medicine, Harvard Medical School, Boston, MA 02115, USA.
S L Dove
A Hochschild
J J Mekalanos
National Academy of Medicine · US

Funding

COORDINATE REGULATION OF BACTERIAL VIRULENCE FACTORSR01AI026289 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI MEKALANOS, JOHN JOSEPH · 1988 to 2018
$8.3M
NIAID NIH HHS AI26289NIAID NIH HHS R01 AI026289
6 · The paper itself

Abstract

We have developed a method for isolation of random peptides that inhibit intracellular processes in bacteria. A library of random peptides expressed as fusions to Escherichia coli thioredoxin (aptamers) were expressed under the tight control of the arabinose-inducible P(BAD) promoter. A selection was applied to the library to isolate aptamers that interfered with the activity of thymidylate synthase (ThyA) in vivo. Expression of an aptamer isolated by this method resulted in a ThyA(-) phenotype that was suppressed by simultaneous overexpression of ThyA. Two-hybrid analysis showed that this aptamer is likely to interact with ThyA in vivo. The library also was screened for aptamers that inhibited growth of bacteria expressing them, and five such aptamers were characterized. Four aptamers were bacteriostatic when expressed, whereas one showed a bactericidal effect. Introduction of translational stop codons into various aptamers blocked their activity, suggesting that their biological effects were likely to be due to protein aptamer rather than RNA. Combinatorial aptamers provide a new genetic and biochemical tool for identifying targets for antibacterial drug development.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsCloning, MolecularDrug DesignEscherichia coliGene ExpressionMolecular Sequence DataPeptide BiosynthesisPeptide Chain Termination, TranslationalPeptidesThioredoxinsThymidylate SynthaseAnti-Bacterial AgentsPeptidesThioredoxinsThymidylate Synthase

Identifiers

PMID10688899
PMCPMC15785
OpenAlexW2019649416

What OpenQuestion holds

Textmetadata
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.