ReviewCurrent opinion in immunology2016
Distinct antibody species: structural differences creating therapeutic opportunities.
Review in Current opinion in immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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.
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.
Who cites it
36 citing papers in PubMed, 60 citations in OpenAlex.
- Characterization of immunoglobulin loci inNAR genomics and bioinformatics · 2026Article
- Review
- Species-Dependent Structural Variations in Single-Domain Antibodies.Antibodies (Basel, Switzerland) · 2025Article
- Immunoglobulin constant regions provide stabilization to the paratope and enforce epitope specificity.The Journal of biological chemistry · 2024Article
- Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons.World journal of microbiology & biotechnology · 2024Review
- The release of host-derived antibodies bound to the variant surface glycoprotein (VSG) ofOpen research Europe · 2024Article
- The smallest functional antibody fragment: Ultralong CDR H3 antibody knob regions potently neutralize SARS-CoV-2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Therapeutic Antibodies in Medicine.Molecules (Basel, Switzerland) · 2023Review
- Evolution of immunogenetic components encoding ultralong CDR H3.Immunogenetics · 2023Article
- Principles and current clinical landscape of NK cell engaging bispecific antibody against cancer.Human vaccines & immunotherapeutics · 2023Review
- Review
- Article
- Structural Classification of CDR-H3 in Single-Domain VMethods in molecular biology (Clifton, N.J.) · 2023Article
- Cattle-derived knob paratopes grafted onto peripheral loops of the IgG1 Fc region enable the generation of a novel symmetric bispecific antibody format.Frontiers in immunology · 2023Article
- Gene prediction in the immunoglobulin loci.Genome research · 2022Article
- Variations in antibody repertoires correlate with vaccine responses.Genome research · 2022Article
- Half-Life Extended Nanobody-Based CD38-Specific Bispecific Killercell Engagers Induce Killing of Multiple Myeloma Cells.Frontiers in immunology · 2022Article
- Using cross-species vaccination approaches to counter emerging infectious diseases.Nature reviews. Immunology · 2021Review
- Mechanistic principles of an ultra-long bovine CDR reveal strategies for antibody design.Nature communications · 2021Article
- Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VScientific reports · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Antibodies have been a remarkably successful class of molecules for binding a large number of antigens in therapeutic, diagnostic, and research applications. Typical antibodies derived from mouse or human sources use the surface formed by complementarity determining regions (CDRs) on the variable regions of the heavy chain/light chain heterodimer, which typically forms a relatively flat binding surface. Alternative species, particularly camelids and bovines, provide a unique paradigm for antigen recognition through novel domains which form the antigen binding paratope. For camelids, heavy chain antibodies bind antigen with only a single heavy chain variable region, in the absence of light chains. In bovines, ultralong CDR-H3 regions form an independently folding minidomain, which protrudes from the surface of the antibody and is diverse in both its sequence and disulfide patterns. The atypical paratopes of camelids and bovines potentially provide the ability to interact with different epitopes, particularly recessed or concave surfaces, compared to traditional antibodies.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.