Evidence map›Paper›PMID 32170178›Full record

ArticleNature communications2020

An amber obligate active site-directed ligand evolution technique for phage display.

Jeffery M Tharp, J Trae Hampton, Catrina A Reed, Andreas Ehnbom, Peng-Hsun Chase Chen, Jared S Morse, Yadagirri Kurra, Lisa M Pérez, Shiqing Xu, Wenshe Ray Liu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Incorporation of Butyryl-Lysine into Phage-Displayed Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Review
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  7. De novo design of D-peptide ligands: Application to influenza virus hemagglutinin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  17. Article
  18. Article
  19. Article
  20. Encoding Noncanonical Amino Acids into Phage Displayed Proteins.Methods in molecular biology (Clifton, N.J.) · 2023
    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

10 authors at 1 institution in 1 country.

Jeffery M Tharp *The Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.ORCID http://orcid.org/0000-0002-2362-3249
J Trae Hampton *The Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.ORCID http://orcid.org/0000-0001-5562-162X
Catrina A Reed *The Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
Andreas EhnbomLaboratory for Molecular Simulation, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.ORCID http://orcid.org/0000-0002-7044-1712
Peng-Hsun Chase ChenThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
Jared S MorseThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
Yadagirri KurraThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
Lisa M PérezLaboratory for Molecular Simulation, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.ORCID http://orcid.org/0000-0003-1176-1027
Shiqing XuThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA. shiqing.xu@tamu.edu.
Wenshe Ray LiuThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA. wliu@chem.tamu.edu.ORCID http://orcid.org/0000-0002-7078-6534
Texas A&M University · US

Funding

Phage Display with Two Genetically Incorporated Noncanonical Amino AcidsR01CA161158 · NCI · TEXAS A&M UNIVERSITY · PI LIU, WENSHE RAY · 2011 to 2015
$1.6M
NCI NIH HHS R01 CA161158
6 · The paper itself

Abstract

Although noncanonical amino acids (ncAAs) were first incorporated into phage libraries through amber suppression nearly two decades ago, their application for use in drug discovery has been limited due to inherent library bias towards sense-containing phages. Here, we report a technique based on superinfection immunity of phages to enrich amber-containing clones, thus avoiding the observed bias that has hindered incorporation of ncAAs into phage libraries. We then take advantage of this technique for development of active site-directed ligand evolution of peptides, where the ncAA serves as an anchor to direct the binding of its peptides to the target's active site. To demonstrate this, phage-displayed peptide libraries are developed that contain a genetically encoded butyryl lysine and are subsequently used to select for ligands that bind SIRT2. These ligands are then modified to develop low nanomolar inhibitors of SIRT2.

Indexed as

Catalytic DomainAmberBacteriophagesDrug DiscoveryGenetic TechniquesHumansLigandsLysineMolecular Docking SimulationPeptide LibraryPeptidesSirtuin 2AmberLigandsLysinePeptide LibraryPeptidesSirtuin 2

Identifiers

PMID32170178
PMCPMC7070036
OpenAlexW3010669865

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.