Evidence map›Paper›PMID 34890875›Full record

ReviewCurrent opinion in biotechnology2022

Improving antibody drug development using bionanotechnology.

Emily K Makowski, John S Schardt, Peter M Tessier

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current opinion in biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Deciphering the language of mingling lipids and proteins.Current opinion in structural biology · 2025
    Review
  2. Article
  3. Review
  4. 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

3 authors at 1 institution in 1 country.

Emily K MakowskiDepartment of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 48109, USA; Biointerfaces Institute, University of Michigan, Ann Arbor, MI 48109, USA.
John S SchardtDepartment of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemical Engineering, University of Michigan, Ann Arbor, MI 48109, USA; Biointerfaces Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Peter M TessierDepartment of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemical Engineering, University of Michigan, Ann Arbor, MI 48109, USA; Departmant of Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109, USA; Biointerfaces Institute, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: ptessier@umich.edu.
University of Michigan · US

Funding

Interdepartmental Training in Pharmacological SciencesT32GM140223 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lori L. Isom · 2021 to 2026
$3.8M
Design and Evolution of Polyvalent Domain Antibodies Specific for Tau AggregatesRF1AG059723 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KANE, RAVI S., TESSIER, PETER M · 2018 to 2022
$2.4M
Mechanisms transducing insulin and insulin resistance in the hippocampusR01AG050598 · NIA · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI MCNAY, EWAN C · 2016 to 2020
$1.9M
Structure-guided antibody targeting of pre-selected epitopes in amyloidogenic aggregatesR35GM136300 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESSIER, PETER M · 2020 to 2024
$1.5M
Design of Antibody Fragments Specific For Amyloidogenic AggregatesR01GM104130 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESSIER, PETER M · 2014 to 2018
$1.3M
Administrative Supplement: Activity-based Discovery and OptimizationF32GM137513 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHARDT, JOHN SAMUEL · 2020 to 2022
$141k
NIA NIH HHS R01 AG050598NIA NIH HHS RF1 AG059723NIGMS NIH HHS F32 GM137513NIGMS NIH HHS R01 GM104130NIGMS NIH HHS R35 GM136300NIGMS NIH HHS T32 GM140223
6 · The paper itself

Abstract

Monoclonal antibodies are being used to treat a remarkable breadth of human disorders. Nevertheless, there are several key challenges at the earliest stages of antibody drug development that need to be addressed using simple and widely accessible methods, especially related to generating antibodies against membrane proteins and identifying antibody candidates with drug-like biophysical properties (high solubility and low viscosity). Here we highlight key bionanotechnologies for preparing functional and stable membrane proteins in diverse types of lipoparticles that are being used to improve antibody discovery and engineering efforts. We also highlight key bionanotechnologies for high-throughput and ultra-dilute screening of antibody biophysical properties during antibody discovery and optimization that are being used for identifying antibodies with superior combinations of in vitro (formulation) and in vivo (half-life) properties.

Indexed as

Antibodies, MonoclonalDrug DevelopmentHumansMembrane ProteinsSolubilityViscosityAntibodies, MonoclonalMembrane Proteins

Identifiers

PMID34890875
PMCPMC9356538
OpenAlexW4200009136

What OpenQuestion holds

Textmetadata
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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.