Evidence map›Paper›PMID 33497192›Full record

ReviewACS chemical biology2021

Strategies and Tactics for the Development of Selective Glycan-Binding Proteins.

Elizabeth M Ward, Megan E Kizer, Barbara Imperiali

Open access · greenAbstract readReview
In one paragraph

Review in ACS chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Defined Glycan Ligands for Detecting Rare l-Sugar-Binding Proteins.Journal of the American Chemical Society · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. The Anxiolytic Activity ofPharmaceuticals (Basel, Switzerland) · 2022
    Article
  18. Article
  19. Extending Janus lectins architecture: Characterization and application to protocells.Computational and structural biotechnology journal · 2022
    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.

Elizabeth M WardDepartment of Biology, Massachusetts Institute of Technology, 31 Ames Street, Cambridge, Massachusetts 02142, United States.ORCID 0000-0001-6410-1116
Megan E KizerDepartment of Biology, Massachusetts Institute of Technology, 31 Ames Street, Cambridge, Massachusetts 02142, United States.ORCID 0000-0003-3549-8606
Barbara ImperialiDepartment of Biology, Massachusetts Institute of Technology, 31 Ames Street, Cambridge, Massachusetts 02142, United States.ORCID 0000-0002-5749-7869
Massachusetts Institute of Technology · US

Funding

Interdepartmental Biotechnology Training ProgramT32GM008334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WITTRUP, KARL DANE · 1989 to 2018
$15.2M
Development of multifunctional probes for profiling microbial glycansU01CA231079 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI IMPERIALI, BARBARA, KIESSLING, LAURA L · 2018 to 2020
$1.4M
Developing glycan-directed tools to investigate microbial infectionF32GM137477 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KIZER, MEGAN E · 2020 to 2022
$170k
NCI NIH HHS U01 CA231079NIGMS NIH HHS F32 GM137477NIGMS NIH HHS T32 GM008334
6 · The paper itself

Abstract

The influences of glycans impact all biological processes, disease states, and pathogenic interactions. Glycan-binding proteins (GBPs), such as lectins, are decisive tools for interrogating glycan structure and function because of their ease of use and ability to selectively bind defined carbohydrate epitopes and glycosidic linkages. GBP reagents are prominent tools for basic research, clinical diagnostics, therapeutics, and biotechnological applications. However, the study of glycans is hindered by the lack of specific and selective protein reagents to cover the massive diversity of carbohydrate structures that exist in nature. In addition, existing GBP reagents often suffer from low affinity or broad specificity, complicating data interpretation. There have been numerous efforts to expand the GBP toolkit beyond those identified from natural sources through protein engineering, to improve the properties of existing GBPs or to engineer novel specificities and potential applications. This review details the current scope of proteins that bind carbohydrates and the engineering methods that have been applied to enhance the affinity, selectivity, and specificity of binders.

Indexed as

AnimalsAntibodiesGlycoside HydrolasesHumansLectinsMutagenesis, Site-DirectedPolysaccharidesProtein BindingProtein DomainsReceptors, AntigenAntibodiesGlycoside HydrolasesLectinsPolysaccharidesReceptors, Antigen

Identifiers

PMID33497192
PMCPMC9200409
OpenAlexW3124118836

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.