Evidence map›Paper›PMID 35482204›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Engineering Proteins Containing Noncanonical Amino Acids on the Yeast Surface.

Rebecca L Hershman, Arlinda Rezhdo, Jessica T Stieglitz, James A Van Deventer

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Pharmacophore-driven antibody discovery on the yeast surface.bioRxiv : the preprint server for biology · 2025
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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.

Rebecca L HershmanChemical and Biological Engineering Department, Tufts University, Medford, MA, USA.
Arlinda RezhdoChemical and Biological Engineering Department, Tufts University, Medford, MA, USA.
Jessica T StieglitzChemical and Biological Engineering Department, Tufts University, Medford, MA, USA.
James A Van DeventerChemical and Biological Engineering Department, Tufts University, Medford, MA, USA. James.van_deventer@tufts.edu.
Tufts University · US

Funding

Discovering hybrid inhibitors for tumor microenvironment disruptionR21CA214239 · NCI · TUFTS UNIVERSITY MEDFORD · PI VAN DEVENTER, JAMES ALLEN · 2018 to 2020
$599k
NCI NIH HHS R21 CA214239
6 · The paper itself

Abstract

Yeast display has been used to advance many critical research areas, including the discovery of unique protein binders and biological therapeutics. In parallel, noncanonical amino acids (ncAAs) have been used to tailor antibody-drug conjugates and enable discovery of therapeutic leads. Together, these two technologies have allowed for generation of synthetic antibody libraries, where the introduction of ncAAs in yeast-displayed proteins allows for library screening for therapeutically relevant targets. The combination of yeast display with genetically encoded ncAAs increases the available chemistry in proteins and advances applications that require high-throughput strategies. In this chapter, we discuss methods for displaying proteins containing ncAAs on the yeast surface, generating and screening libraries of proteins containing ncAAs, preparing bioconjugates on the yeast surface in large scale, generating and screening libraries of aminoacyl-tRNA synthetases (aaRSs) for encoding ncAAs by using reporter constructs, and characterizing ncAA-containing proteins secreted from yeast. The experimental designs laid out in this chapter are generalizable for discovery of protein binders to a variety of targets and aaRS evolution to continue expanding the genetic code beyond what is currently available in yeast.

Indexed as

Amino AcidsAmino Acyl-tRNA SynthetasesGenetic CodeProtein EngineeringProteinsSaccharomyces cerevisiaeAmino AcidsAmino Acyl-tRNA SynthetasesProteinsAminoacyl-tRNA synthetase engineeringAntibody library screeningClick chemistryHigh-throughput screeningNoncanonical amino acidsYeast display

Identifiers

PMID35482204
OpenAlexW4225963375

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.