Evidence map›Paper›PMID 31622515›Full record

ArticleProtein science : a publication of the Protein Society2020

An engineered ultra-high affinity Fab-Protein G pair enables a modular antibody platform with multifunctional capability.

Tomasz Slezak, Lucas J Bailey, Mateusz Jaskolowski, Dominik A Nahotko, Ekaterina V Filippova, Elena K Davydova, Anthony A Kossiakoff

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Construction of αJournal of separation science · 2026
    Article
  3. Article
  4. Dynamic translocation of Inside-Out proteins to the cell surface underlies cellular adaptation to cancer-induced stress.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Engineered protein G variants for multifunctional antibody-based assemblies.Protein science : a publication of the Protein Society · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. 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

7 authors at 2 institutions in 1 country.

Tomasz SlezakDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Lucas J BaileyDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Mateusz JaskolowskiDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Dominik A NahotkoDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Ekaterina V FilippovaDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Elena K DavydovaDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Anthony A KossiakoffDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.ORCID 0000-0003-3174-9359
University of Illinois Chicago · USChicago Institute for Psychoanalysis · US

Funding

Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
CSR NIH HHS GM117372NIGMS NIH HHS R01 GM117372
6 · The paper itself

Abstract

Engineered recombinant antibody-based reagents are rapidly supplanting traditionally derived antibodies in many cell biological applications. A particularly powerful aspect of these engineered reagents is that other modules having myriad functions can be attached to them either chemically or through molecular fusions. However, these processes can be cumbersome and do not lend themselves to high throughput applications. Consequently, we have endeavored to develop a platform that can introduce multiple functionalities into a class of Fab-based affinity reagents in a "plug and play" fashion. This platform exploits the ultra-tight binding interaction between affinity matured variants of a Fab scaffold (Fab

Indexed as

Cell LineHumansImmunoglobulin Fab FragmentsModels, MolecularNerve Tissue ProteinsProtein ConformationProtein DomainsProtein EngineeringRecombinant ProteinsG-substrateImmunoglobulin Fab FragmentsNerve Tissue ProteinsRecombinant Proteinsaffinity maturationbi-specific T-cell engagersengineered FabPhage displayProtein Gproximity assaysplit enzyme

Identifiers

PMID31622515
PMCPMC6933859
OpenAlexW2980548343

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.