Evidence map›Paper›PMID 20583754›Full record

ArticleJournal of the American Chemical Society2010

An array-based method to identify multivalent inhibitors.

Yalong Zhang, Qian Li, Luis G Rodriguez, Jeffrey C Gildersleeve

Open access · greenAbstract readValidation Study
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 87 citations in OpenAlex.

  1. GCI-Based Affinity Screening of Synthetic Oligomannosides toward Concanavalin A.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Human oral lectin ZG16B acts as a cell wall polysaccharide probe to decode host-microbe interactions with oral commensals.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Synthetic Plant Glycan Microarrays as Tools for Plant Biology.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Article
  13. Article
  14. Glycan Array Technology.Advances in biochemical engineering/biotechnology · 2021
    Article
  15. On-Chip Neo-Glycopeptide Synthesis for Multivalent Glycan Presentation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Yalong ZhangChemical Biology Laboratory, National Cancer Institute, 376 Boyles Street, Building 376, Frederick, Maryland 21702, USA.
Qian Li
Luis G Rodriguez
Jeffrey C Gildersleeve
Science Applications International Corporation (United States) · US

Funding

Carbohydrate Microarray Profiling of Glycan-Binding Antibodies and LectinsZIABC010740 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GILDERSLEEVE, JEFFREY · 2009 to 2025
$10.7M
Development of a Carbohydrate MicroarrayZIABC010675 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GILDERSLEEVE, JEFFREY · 2009 to 2025
$6.1M
Development of a Carbohydrate MicroarrayZ01BC010675 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GILDERSLEEVE, JEFF · 2005 to 2008
$438k
Intramural NIH HHS Z01 BC010675Intramural NIH HHS ZIA BC010740
6 · The paper itself

Abstract

Carbohydrate-protein interactions play a critical role in a variety of biological processes, and agonists/antagonists of these interactions are useful as biological probes and therapeutic agents. Most carbohydrate-binding proteins achieve tight binding through formation of a multivalent complex. Therefore, both ligand structure and presentation contribute to recognition. Since there are many potential combinations of structure, spacing, and orientation to consider and the optimal one cannot be predicted, high-throughput approaches for analyzing carbohydrate-protein interactions and designing inhibitors are appealing. In this report, we develop a strategy to vary neoglycoprotein density on a surface of a glycan array. This feature of presentation was combined with variations in glycan structure and glycan density to produce an array with approximately 600 combinations of glycan structure and presentation. The unique array platform allows one to distinguish between different types of multivalent complexes on the array surface. To illustrate the advantages of this format, it was used to rapidly identify multivalent probes for various lectins. The new array was first tested with several plant lectins, including concanavalin A (conA), Vicia villosa isolectin B4 (VVL-B(4)), and Ricinus communis agglutinin (RCA120). Next, it was used to rapidly identify potent multivalent inhibitors of Pseudomonas aeruginosa lectin I (PA-IL), a key protein involved in opportunistic infections of P. aeruginosa , and mouse macrophage galactose-type lectin (mMGL-2), a protein expressed on antigen presenting cells that may be useful as a vaccine targeting receptor. An advantage of the approach is that structural information about the lectin/receptor is not required to obtain a multivalent inhibitor/probe.

Indexed as

CarbohydratesEnzyme-Linked Immunosorbent AssayPlantsProtein BindingProteinsSurface PropertiesCarbohydratesProteins

Identifiers

PMID20583754
PMCPMC2923827
OpenAlexW1988027949

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.