Evidence map›Paper›PMID 28935113›Full record

ArticleMethods in enzymology2017

Directed Evolution of Glycopeptides Using mRNA Display.

Satoru Horiya, Jennifer K Bailey, Isaac J Krauss

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. ACS central science · 2025
    Article
  4. Review
  5. Large-Scale Synthesis of ManACS infectious diseases · 2022
    Article
  6. Article
  7. Article
  8. Decentralizing Cell-Free RNA Sensing With the Use of Low-Cost Cell Extracts.Frontiers in bioengineering and biotechnology · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Evolving a Peptide: Library Platforms and Diversification Strategies.International journal of molecular sciences · 2019
    Review
  15. Article
  16. 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

3 authors at 1 institution in 1 country.

Satoru HoriyaBrandeis University, Waltham, MA, United States.
Jennifer K BaileyBrandeis University, Waltham, MA, United States.
Isaac J KraussBrandeis University, Waltham, MA, United States. Electronic address: kraussi@brandeis.edu.
Brandeis University · US

Funding

Rational and Combinatorial Design of Immunogens to Elicit 2G12-like AntibodiesR01AI090745 · NIAID · BRANDEIS UNIVERSITY · PI KRAUSS, ISAAC JONATHAN · 2010 to 2022
$3.9M
Design of Immunogens to Elicit PGT122 like AntibodiesR01AI113737 · NIAID · BRANDEIS UNIVERSITY · PI KRAUSS, ISAAC JONATHAN · 2014 to 2018
$2.2M
Glycopeptide evolution targeting antibodies of the PGT128 lineage.R56AI090745 · NIAID · BRANDEIS UNIVERSITY · PI KRAUSS, ISAAC JONATHAN · 2017 to 2017
$523k
NIAID NIH HHS R01 AI090745NIAID NIH HHS R01 AI113737NIAID NIH HHS R56 AI090745
6 · The paper itself

Abstract

Directed evolution is a useful method for the discovery of nucleic acids, peptides, or proteins that have desired binding abilities or functions. Because of the abundance and importance of glycosylation in nature, directed evolution of glycopeptides and glycoproteins is also highly desirable. However, common directed evolution platforms such as phage-, yeast-, or mammalian-cell display are limited for these applications by several factors. Glycan structure at each glycosylation site is not genetically encoded, and yeast and mammalian cells produce a heterogeneous mixture of glycoforms at each site on the protein. Although yeast, mammalian and Escherichia coli cells can be engineered to produce a homogenous glycoform at all glycosylation sites, there are just a few specific glycan structures that can readily be accessed in this manner. Recently, we reported a novel system for the directed evolution of glycopeptide libraries, which could in principle be decorated with any desired glycan. Our method combines in vitro peptide selection by mRNA display with unnatural amino acid incorporation and chemical attachment of synthetic oligosaccharides. Here, we provide an updated and optimized protocol for this method, which is designed to create glycopeptide mRNA display libraries containing ~10

Indexed as

Amino Acid SequenceDirected Molecular EvolutionEpitopesEscherichia coliGlycopeptidesGlycoproteinsGlycosylationHIV-1HIV Envelope Protein gp120HumansPolysaccharidesRNA, MessengerYeastsEpitopesGlycopeptidesGlycoproteinsHIV Envelope Protein gp120PolysaccharidesRNA, Messenger2G12Broadly neutralizing antibodiesClick chemistryCuAACDirected evolutionGlycopeptide/glycoproteinHIVmRNA displayMultivalencySelection

Identifiers

PMID28935113
PMCPMC5993046
OpenAlexW2749879468

What OpenQuestion holds

Textmetadata
LicenceTDM
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.