Evidence map›Paper›PMID 27515702›Full record

ArticleProtein engineering, design & selection : PEDS2016

A platform for constructing, evaluating, and screening bioconjugates on the yeast surface.

James A Van Deventer, Doris N Le, Jessie Zhao, Haixing P Kehoe, Ryan L Kelly

Abstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Pharmacophore-driven antibody discovery on the yeast surface.bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Incorporating, Quantifying, and Leveraging Noncanonical Amino Acids in Yeast.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  15. Article
  16. Engineering Proteins Containing Noncanonical Amino Acids on the Yeast Surface.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors.

James A Van DeventerChemical and Biological Engineering Department, Tufts University, 4 Colby Street Room 148, Medford, MA 02155, United States of America.
Doris N LeKoch Institute for Integrative Cancer Research.
Jessie ZhaoKoch Institute for Integrative Cancer Research.
Haixing P KehoeChemical and Biological Engineering Department, Tufts University, 4 Colby Street Room 148, Medford, MA 02155, United States of America.
Ryan L KellyKoch Institute for Integrative Cancer Research.

Funding

Interdepartmental Biotechnology Training ProgramT32GM008334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WITTRUP, KARL DANE · 1989 to 2018
$15.2M
New Approaches to the Selective Targeting of Cancer-associated FibroblastsF32CA168057 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI VAN DEVENTER, JAMES ALLEN · 2012 to 2014
$150k
NCI NIH HHS F32 CA168057NIGMS NIH HHS T32 GM008334
6 · The paper itself

Abstract

The combination of protein display technologies and noncanonical amino acids (ncAAs) offers unprecedented opportunities for the high throughput discovery and characterization of molecules suitable for addressing fundamental and applied problems in biological systems. Here we demonstrate that ncAA-compatible yeast display facilitates evaluations of conjugation chemistry and stability that would be challenging or impossible to perform with existing mRNA, phage, or E. coli platforms. Our approach enables site-specific introduction of ncAAs into displayed proteins, robust modification at azide-containing residues, and quantitative evaluation of conjugates directly on the yeast surface. Moreover, screening allows for the selective enrichment of chemically modified constructs while maintaining a genotype-phenotype linkage with encoded azide functionalities. Thus, this platform is suitable for the high throughput characterization and screening of libraries of chemically modified polypeptides for therapeutic lead discovery and other biological applications.

Indexed as

antibodiesclick chemistryhigh throughput screeningnoncanonical amino acidsyeast display

Identifiers

PMID27515702
PMCPMC5081042

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.