ArticleMicrobial cell factories2017
Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 29 citations in OpenAlex.
- Site-Specific Antigen Immobilization Improves Autoantibody Binding Efficiency on the Luminex Platform.ACS omega · 2026Article
- Review
- Construction and application of a large capacity VNAR library from the whitespotted bamboo shark (Acta pharmaceutica Sinica. B · 2025Article
- Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons.World journal of microbiology & biotechnology · 2024Review
- NbThermo: a new thermostability database for nanobodies.Database : the journal of biological databases and curation · 2023Article
- Therapeutic applications of nanobodies against SARS-CoV-2 and other viral infections: Current update.International journal of biological macromolecules · 2023Review
- Structural Insights into the Design of Synthetic Nanobody Libraries.Molecules (Basel, Switzerland) · 2022Review
- Research progress on unique paratope structure, antigen binding modes, and systematic mutagenesis strategies of single-domain antibodies.Frontiers in immunology · 2022Review
- Perspective on therapeutic and diagnostic potential of camel nanobodies for coronavirus disease-19 (COVID-19).3 Biotech · 2021Review
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- Prospects of Neutralizing Nanobodies Against SARS-CoV-2.Frontiers in immunology · 2021Review
- High affinity nanobodies block SARS-CoV-2 spike receptor binding domain interaction with human angiotensin converting enzyme.Scientific reports · 2020Article
- Selection and Characterization of Single-Domain Antibodies for Detection of Lassa Nucleoprotein.Antibodies (Basel, Switzerland) · 2020Article
- Toward Drug-Like Multispecific Antibodies by Design.International journal of molecular sciences · 2020Review
- An update on antiviral antibody-based biopharmaceuticals.International immunopharmacology · 2020Review
- Evaluation of a noncanonical Cys40-Cys55 disulfide linkage for stabilization of single-domain antibodies.Protein science : a publication of the Protein Society · 2019Article
- A field effect transistor modified with reduced graphene oxide for immunodetection of Ebola virus.Mikrochimica acta · 2019Article
- Selection and Characterization of Anti-Dengue NS1 Single Domain Antibodies.Scientific reports · 2018Article
- Selection of Single-Domain Antibodies towards Western Equine Encephalitis Virus.Antibodies (Basel, Switzerland) · 2018Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundA key advantage of recombinant antibody technology is the ability to optimize and tailor reagents. Single domain antibodies (sdAbs), the recombinantly produced variable domains derived from camelid and shark heavy chain antibodies, provide advantages of stability and solubility and can be further engineered to enhance their properties. In this study, we generated sdAbs specific for Ebola virus envelope glycoprotein (GP) and increased their stability to expand their utility for use in austere locals. Ebola virus is extremely virulent and causes fatal hemorrhagic fever in ~ 50 percent of the cases. The viral GP binds to host cell receptors to facilitate viral entry and thus plays a critical role in pathogenicity.
resultsAn immune phage display library containing more than 10
conclusionsSdAbs specific for Ebola GP were selected and their stability and functionality were improved utilizing protein engineering. Thermal stability of antibody reagents may be of particular importance when operating in austere locations that lack reliable refrigeration. Future efforts can evaluate the potential of these isolated sdAbs as candidates for diagnostic or therapeutic applications for Ebola.
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.