Evidence map›Paper›PMID 27655414›Full record

ReviewCurrent pharmaceutical design2016

Engineered Autonomous Human Variable Domains.

Johan Nilvebrant, Peter M Tessier, Sachdev S Sidhu

Abstract readReview
In one paragraph

Review in Current pharmaceutical design, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Construction of Synthetic Antibody Phage Display Libraries.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Recombinant antibodies and their use for food immunoanalysis.Analytical and bioanalytical chemistry · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Considerations for the Design of Antibody-Based Therapeutics.Journal of pharmaceutical sciences · 2020
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Review
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

3 authors at 1 institution in 1 country.

Johan NilvebrantProtein Technology, School of Biotechnology, Royal Institute of Technology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
Peter M Tessier
Sachdev S Sidhu
AlbaNova · SE

Funding

Design of Antibody Fragments Specific For Amyloidogenic AggregatesR01GM104130 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESSIER, PETER M · 2014 to 2018
$1.3M
CIHR MOP-93725NIGMS NIH HHS R01 GM104130
6 · The paper itself

Abstract

backgroundThe complex multi-chain architecture of antibodies has spurred interest in smaller derivatives that retain specificity but can be more easily produced in bacteria. Domain antibodies consisting of single variable domains are the smallest antibody fragments and have been shown to possess enhanced ability to target epitopes that are difficult to access using multidomain antibodies. However, in contrast to natural camelid antibody domains, human variable domains typically suffer from low stability and high propensity to aggregate.

methodsThis review summarizes strategies to improve the biophysical properties of heavy chain variable domains from human antibodies with an emphasis on aggregation resistance. Several protein engineering approaches have targeted antibody frameworks and complementarity determining regions to stabilize the native state and prevent aggregation of the denatured state.

conclusionRecent findings enable the construction of highly diverse libraries enriched in aggregation-resistant variants that are expected to provide binders to diverse antigens. Engineered domain antibodies possess unique advantages in expression, epitope preference and flexibility of formatting over conventional immunoreagents and are a promising class of antibody fragments for biomedical development.

Indexed as

Protein EngineeringAntibodiesBacteriophagesHumansPeptide LibraryAntibodiesPeptide Libraryaggregation.antibody engineeringHuman domain antibodyphage displaysynthetic antibodiesvariable heavy domain

Identifiers

PMID27655414
PMCPMC5326600
OpenAlexW2521380866

What OpenQuestion holds

Textmetadata
LicenceTDM
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.