Evidence map›Paper›PMID 25545206›Full record

ArticleMonoclonal antibodies in immunodiagnosis and immunotherapy2014

Proteoliposome-based selection of a recombinant antibody fragment against the human M2 muscarinic acetylcholine receptor.

Suharni, Yayoi Nomura, Takatoshi Arakawa, Tomoya Hino, Hitomi Abe, Yoshiko Nakada-Nakura, Yumi Sato, Hiroko Iwanari, Mitsunori Shiroishi, Hidetsugu Asada and 6 more

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Monoclonal antibodies in immunodiagnosis and immunotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Discovery of Therapeutic Antibodies Targeting Complex Multi-Spanning Membrane Proteins.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2024
    Review
  3. Article
  4. Article
  5. Review
  6. Improving antibody drug development using bionanotechnology.Current opinion in biotechnology · 2022
    Review
  7. Article
  8. Recombinant Antibodies in Basic Neuroscience Research.Current protocols in neuroscience · 2020
    Review
  9. Article
  10. 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

16 authors at 5 institutions in 3 countries.

Suharni1 Department of Cell Biology, Graduate School of Medicine, Kyoto University , Sakyo-ku, Kyoto, Japan .
Yayoi Nomura
Takatoshi Arakawa
Tomoya Hino
Hitomi Abe
Yoshiko Nakada-Nakura
Yumi Sato
Hiroko Iwanari
Mitsunori Shiroishi
Hidetsugu Asada
Tatsuro Shimamura
Takeshi Murata
Takuya Kobayashi
Takao Hamakubo
So Iwata
Norimichi Nomura
Kyoto University · JPJapan Science and Technology Agency · JPThe University of Tokyo · JPCentre for Structural Systems Biology · DEImperial College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of antibodies against human G-protein-coupled receptors (GPCRs) has achieved limited success, which has mainly been attributed to their low stability in a detergent-solubilized state. We herein describe a method that can generally be applied to the selection of phage display libraries with human GPCRs reconstituted in liposomes. A key feature of this approach is the production of biotinylated proteoliposomes that can be immobilized on the surface of streptavidin-coupled microplates or paramagnetic beads and used as a binding target for antibodies. As an example, we isolated a single chain Fv fragment from an immune phage library that specifically binds to the human M2 muscarinic acetylcholine receptor with nanomolar affinity. The selected antibody fragment recognized the GPCR in both detergent-solubilized and membrane-embedded forms, which suggests that it may be a potentially valuable tool for structural and functional studies of the GPCR. The use of proteoliposomes as immunogens and screening bait will facilitate the application of phage display to this difficult class of membrane proteins.

Indexed as

Enzyme-Linked Immunosorbent AssayEpitope MappingHumansImmunoglobulin FragmentsKineticsMutagenesis, Site-DirectedPeptide LibraryProtein BindingProteolipidsReceptor, Muscarinic M2Recombinant ProteinsSaccharomyces cerevisiaeImmunoglobulin FragmentsPeptide LibraryProteolipidsproteoliposomesReceptor, Muscarinic M2Recombinant Proteins

Identifiers

PMID25545206
PMCPMC4278166
OpenAlexW2116834781

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.