Evidence map›Paper›PMID 39223086›Full record

ArticleAngewandte Chemie (International ed. in English)2024

Enzymatic Synthesis of Disialyllacto-N-Tetraose (DSLNT) and Related Human Milk Oligosaccharides Reveals Broad Siglec Recognition of the Atypical Neu5Acα2-6GlcNAc Motif.

Shumin Bao, Tangliang Shen, Mohammad Hossein Shabahang, Guitao Bai, Lei Li

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

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

5 authors.

Shumin BaoDepartment of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Tangliang ShenDepartment of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Mohammad Hossein ShabahangDepartment of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Guitao BaiDepartment of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Lei LiDepartment of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.ORCID 0000-0002-1146-0761

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI LIVE, DAVID H · 2012 to 2019
$14.5M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY · 2013 to 2017
$7.5M
Programable Modular Synthesis of Sulfated N-Glycans and O-GlycansR01GM152688 · NIGMS · GEORGIA STATE UNIVERSITY · PI Lei Li · 2024 to 2026
$983k
Expedite Enzymatic Assembly of Glycans via DNA (de)Hybridization-Enabled Catch-and-ReleaseR21GM150050 · NIGMS · GEORGIA STATE UNIVERSITY · PI LI, LEI · 2023 to 2024
$429k
NIGMS NIH HHS P01 GM107012NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM152688NIGMS NIH HHS R01GM152688NIGMS NIH HHS R21 GM150050NIGMS NIH HHS R21GM150050
6 · The paper itself

Abstract

Sialic acids (Sias) are ubiquitously expressed on all types of glycans, typically as terminating residues. They usually link to galactose, N-acetylgalactosamine, or other Sia residues, forming ligands of many glycan-binding proteins. An atypical linkage to the C6 of N-acetylglucosamine (GlcNAc) has been identified in human milk oligosaccharides (HMOs, e.g., DSLNT) and tumor-associated glycoconjugates. Herein, describe the systematic synthesis of these HMOs in an enzymatic modular manner. The synthetic strategy relies on a novel activity of ST6GalNAc6 for efficient construction of the Neu5Acα2-6GlcNAc linkage, and another 12 specific enzyme modules for sequential HMO assembly. The structures enabled comprehensive exploration of their structure-function relationships using glycan microarrays, revealing broad yet distinct recognition by Siglecs of the atypical Neu5Acα2-6GlcNAc motif. The work provides tools and new insight for the functional study and potential applications of Siglecs and HMOs.

Indexed as

Milk, HumanOligosaccharidesHumansSialic Acid Binding Immunoglobulin-like LectinsSialic Acidslacto-N-neotetraoseOligosaccharidesSialic Acid Binding Immunoglobulin-like LectinsSialic Acidsatypical sialosidesenzyamtic synthesishuman milk oligosaccharidesSiglecST6GalNAc6

Identifiers

PMID39223086
PMCPMC11631665

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Registered trials

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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.