Evidence map›Paper›PMID 36479130›Full record

ReviewFrontiers in immunology2022

Research progress on unique paratope structure, antigen binding modes, and systematic mutagenesis strategies of single-domain antibodies.

Chang Liu, Hong Lin, Limin Cao, Kaiqiang Wang, Jianxin Sui

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Construction and validation of a synthetic phage-displayed nanobody library.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024
    Article
  11. Review
  12. Aging imaging: the future demand of health management.European journal of nuclear medicine and molecular imaging · 2023
    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

5 authors at 1 institution in 1 country.

Chang LiuCollege of Food Science and Engineering, Ocean University of China, Qingdao, Shandong, China.
Hong LinCollege of Food Science and Engineering, Ocean University of China, Qingdao, Shandong, China.
Limin CaoCollege of Food Science and Engineering, Ocean University of China, Qingdao, Shandong, China.
Kaiqiang WangCollege of Food Science and Engineering, Ocean University of China, Qingdao, Shandong, China.
Jianxin SuiCollege of Food Science and Engineering, Ocean University of China, Qingdao, Shandong, China.
Ocean University of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-domain antibodies (sdAbs) showed the incredible advantages of small molecular weight, excellent affinity, specificity, and stability compared with traditional IgG antibodies, so their potential in binding hidden antigen epitopes and hazard detection in food, agricultural and veterinary fields were gradually explored. Moreover, its low immunogenicity, easy-to-carry target drugs, and penetration of the blood-brain barrier have made sdAbs remarkable achievements in medical treatment, toxin neutralization, and medical imaging. With the continuous development and maturity of modern molecular biology, protein analysis software and database with different algorithms, and next-generation sequencing technology, the unique paratope structure and different antigen binding modes of sdAbs compared with traditional IgG antibodies have aroused the broad interests of researchers with the increased related studies. However, the corresponding related summaries are lacking and needed. Different antigens, especially hapten antigens, show distinct binding modes with sdAbs. So, in this paper, the unique paratope structure of sdAbs, different antigen binding cases, and the current maturation strategy of sdAbs were classified and summarized. We hope this review lays a theoretical foundation to elucidate the antigen-binding mechanism of sdAbs and broaden the further application of sdAbs.

Indexed as

Single-Domain AntibodiesImmunoglobulin GMolecular BiologyImmunoglobulin GSingle-Domain Antibodiesbinding modesepitopemutagenesisparatopesingle-domain antibodystructure

Identifiers

PMID36479130
PMCPMC9720397
OpenAlexW4309739700

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.