Evidence map›Paper›PMID 38616080›Full record

ReviewCarbohydrate polymers2024

Glycosaminoglycan microarrays for studying glycosaminoglycan-protein systems.

John E Chittum, Ally Thompson, Umesh R Desai

Abstract readReview
In one paragraph

Review in Carbohydrate polymers, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. 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.

John E ChittumDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, United States of America; Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA 23219, United States of America.
Ally ThompsonDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, United States of America; Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA 23219, United States of America.
Umesh R DesaiDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, United States of America; Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA 23219, United States of America. Electronic address: urdesai@vcu.edu.

Funding

Project 3: Role of Glycosaminoglycans in HematopoiesisP01HL151333 · NHLBI · VERSITI WISCONSIN, INC. · PI WEILER, HARTMUT KARL-HEINZ · 2021 to 2025
$12.3M
Glycans in Blood Homeostasis and DiseaseK12HL141954 · NHLBI · VERSITI WISCONSIN, INC. · PI DAHMS, NANCY M., DESAI, UMESH RAMANLAL · 2018 to 2022
$4.9M
Lead identification and pre-clinical studies on allosteric inhibitors of coagulation factor XIaR61HL161813 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI DESAI, UMESH RAMANLAL · 2022 to 2023
$1.1M
NHLBI NIH HHS K12 HL141954NHLBI NIH HHS P01 HL151333NHLBI NIH HHS R61 HL161813
6 · The paper itself

Abstract

More than 3000 proteins are now known to bind to glycosaminoglycans (GAGs). Yet, GAG-protein systems are rather poorly understood in terms of selectivity of recognition, molecular mechanism of action, and translational promise. High-throughput screening (HTS) technologies are critically needed for studying GAG biology and developing GAG-based therapeutics. Microarrays, developed within the past two decades, have now improved to the point of being the preferred tool in the HTS of biomolecules. GAG microarrays, in which GAG sequences are immobilized on slides, while similar to other microarrays, have their own sets of challenges and considerations. GAG microarrays are rapidly becoming the first choice in studying GAG-protein systems. Here, we review different modalities and applications of GAG microarrays presented to date. We discuss advantages and disadvantages of this technology, explain covalent and non-covalent immobilization strategies using different chemically reactive groups, and present various assay formats for qualitative and quantitative interpretations, including selectivity screening, binding affinity studies, competitive binding studies etc. We also highlight recent advances in implementing this technology, cataloging of data, and project its future promise. Overall, the technology of GAG microarray exhibits enormous potential of evolving into more than a mere screening tool for studying GAG - protein systems.

Indexed as

Biological AssayGlycosaminoglycansBinding, CompetitiveMicroarray AnalysisResearchGlycosaminoglycansGAG-binding proteinGlycosaminoglycanHigh-throughput screeningImmobilization chemistryMicroarrayProteoglycansSlide chemistry

Identifiers

PMID38616080
PMCPMC11032185

What Socratic 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 Socratic graph.