Evidence map›Paper›PMID 25348396›Full record

ArticleNucleic acids research2014

Identification of target-binding peptide motifs by high-throughput sequencing of phage-selected peptides.

Inmaculada Rentero Rebollo, Michal Sabisz, Vanessa Baeriswyl, Christian Heinis

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. High-throughput protein binder discovery by rapid in vivo selection.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
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  8. Article
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  11. De novo mapping of α-helix recognition sites on protein surfaces using unbiased libraries.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Synergetic collision and space separation in microfluidic chip for efficient affinity-discriminated molecular selection.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
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  18. Quantitative profiling of protease specificity.PLoS computational biology · 2021
    Article
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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 at 1 institution in 1 country.

Inmaculada Rentero RebolloInstitute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland inmaculada.rentero@epfl.ch.
Michal SabiszInstitute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Vanessa BaeriswylInstitute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Christian HeinisInstitute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland christian.heinis@epfl.ch.
École Polytechnique Fédérale de Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-throughput sequencing was previously applied to phage-selected peptides in order to gain insight into the abundance and diversity of isolated peptides. Herein we developed a procedure to efficiently compare the sequences of large numbers of phage-selected peptides for the purpose of identifying target-binding peptide motifs. We applied the procedure to analyze bicyclic peptides isolated against five different protein targets: sortase A, urokinase-type plasminogen activator, coagulation factor XII, plasma kallikrein and streptavidin. We optimized sequence data filters to reduce biases originating from the sequencing method and developed sequence correction algorithms to prevent identification of false consensus motifs. With our strategy, we were able to identify rare target-binding peptide motifs, as well as to define more precisely consensus sequences and sub-groups of consensus sequences. This information is valuable to choose peptide leads for drug development and it facilitates identification of epitopes. We furthermore show that binding motifs can be identified after a single round of phage selection. Such a selection regimen reduces propagation-related bias and may facilitate application of phage display in non-specialized laboratories, as procedures such as bacterial infection, phage propagation and purification are not required.

Indexed as

Amino Acid MotifsAmino Acid SequenceBacteriophagesCell Surface Display TechniquesConsensus SequenceLigandsPeptides, CyclicSequence Analysis, ProteinSoftwareLigandsPeptides, Cyclic

Identifiers

PMID25348396
PMCPMC4267670
OpenAlexW2109088164

What OpenQuestion holds

Textmetadata
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.