Evidence map›Paper›PMID 31285332›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

A cell-cell interaction format for selection of high-affinity antibodies to membrane proteins.

Zhuo Yang, Yue Wan, Pingdong Tao, Min Qiang, Xue Dong, Chih-Wei Lin, Guang Yang, Tianqing Zheng, Richard A Lerner

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.8field-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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Development of a [89Zr]Zr-labeled Human Antibody using a Novel Phage-displayed Human scFv Library.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Article
  4. Article
  5. Methods for Engineering Binders to Multi-Pass Membrane Proteins.Bioengineering (Basel, Switzerland) · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Yeast biopanning against site-specific phosphorylations in tau.Protein engineering, design & selection : PEDS · 2023
    Article
  11. A robust antibody discovery platform for difficult-to-express G protein-coupled receptors.Protein science : a publication of the Protein Society · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

9 authors at 5 institutions in 2 countries.

Zhuo YangDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037.
Yue WanShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, People's Republic of China.
Pingdong TaoShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, People's Republic of China.
Min QiangShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, People's Republic of China.
Xue DongShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, People's Republic of China.
Chih-Wei LinDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037.
Guang YangShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, People's Republic of China.
Tianqing ZhengDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037; tzheng@scripps.edu rlerner@scripps.edu.
Richard A LernerDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037; tzheng@scripps.edu rlerner@scripps.edu.
Scripps Research Institute · USShanghaiTech University · CNUniversity of Chinese Academy of Sciences · CNChinese Academy of Sciences · CNShanghai Institutes for Biological Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Generating and improving antibodies and peptides that bind specifically to membrane protein targets such as ion channels and G protein-coupled receptors (GPCRs) can be challenging using established selection methods. Current strategies are often limited by difficulties in the presentation of the antigen or the efficiency of the selection process. Here, we report a method for obtaining antibodies specific for whole cell membrane-associated antigens which combines a cell-cell interaction format based on yeast display technology with fluorescence-activated cell sorting of dual fluorescent complexes. Using this method, we were able to direct the affinity maturation of an antagonist antibody specific for the proton-gated ion channel ASIC1a and showed that both the affinity and potency were improved. We were also able to use this method to do kinetic selections to generate clones with better dissociation profiles. In addition, this method was employed successfully to handle the difficult problem of selecting antibodies specific to a GPCR target, the mu-opioid receptor.

Indexed as

AnimalsAntibodiesAntibody AffinityCHO CellsCricetinaeCricetulusDrug DiscoveryFlow CytometryIon ChannelsReceptors, G-Protein-CoupledSaccharomyces cerevisiaeAntibodiesIon ChannelsReceptors, G-Protein-Coupledantibody drug discoveryGPCRsion channelsmembrane proteinsyeast display

Identifiers

PMID31285332
PMCPMC6660777
OpenAlexW2958909029

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.