Evidence map›Paper›PMID 38844638›Full record

ArticleNature chemistry2024

Integrated chemoenzymatic synthesis of a comprehensive sulfated ganglioside glycan library to decipher functional sulfoglycomics and sialoglycomics.

Zhuojia Xu, Yating Liu, Jialin Liu, Wenjing Ma, Zhumin Zhang, Digantkumar G Chapla, Liuqing Wen, Kelley W Moremen, Wen Yi, Tiehai Li

Abstract read
In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Defining substrate specificities ofOrganic chemistry frontiers : an international journal of organic chemistry · 2026
    Article
  4. Article
  5. Article
  6. Stereoselective Ferrier-Type O-Glycosylation Enabled by Difluoromethylated Glycal Donors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Highly efficient α-sialylation withScience advances · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Cyclopropenium functionalization.Nature chemistry · 2024
    Article
  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

10 authors.

Zhuojia XuState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-9383-2070
Yating LiuState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0009-0002-0980-389X
Jialin LiuState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-1672-8210
Wenjing MaState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0009-0001-8457-5412
Zhumin ZhangState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-9780-5571
Digantkumar G ChaplaComplex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
Liuqing WenState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0001-9187-7999
Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.ORCID 0000-0003-1768-582X
Wen YiCollege of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0002-4257-3355
Tiehai LiState Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China. tiehaili@simm.ac.cn.ORCID 0000-0002-3600-1828

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Origin of N-Glycan Site-Specific HeterogeneityR01GM130915 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, MOREMEN, KELLEY W. · 2019 to 2022
$3.4M
National Natural Science Foundation of China (National Science Foundation of China) 22077130National Natural Science Foundation of China (National Science Foundation of China) 22325704National Natural Science Foundation of China (National Science Foundation of China) 22377134National Natural Science Foundation of China (National Science Foundation of China) 92353303NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM130915Science and Technology Commission of Shanghai Municipality (Shanghai Municipal Science and Technology Commission) 20ZR1467900
6 · The paper itself

Abstract

Ganglioside glycans are ubiquitous and complex biomolecules that are involved in a wide range of biological functions and disease processes. Variations in sialylation and sulfation render the structural complexity and diversity of ganglioside glycans, and influence protein-carbohydrate interactions. Structural and functional insights into the biological roles of these glycans are impeded due to the limited accessibility of well-defined structures. Here we report an integrated chemoenzymatic strategy for expeditious and systematic synthesis of a comprehensive 65-membered ganglioside glycan library covering all possible patterns of sulfation and sialylation. This strategy relies on the streamlined modular assembly of three common sialylated precursors by highly stereoselective iterative sialylation, modular site-specific sulfation through flexible orthogonal protecting-group manipulations and enzymatic-catalysed diversification using three sialyltransferase modules and a galactosidase module. These diverse ganglioside glycans enable exploration into their structure-function relationships using high-throughput glycan microarray technology, which reveals that different patterns of sulfation and sialylation on these glycans mediate their unique binding specificities.

Indexed as

GangliosidesPolysaccharidesGlycomicsSialyltransferasesSulfatesGangliosidesPolysaccharidesSialyltransferasesSulfates

Identifiers

PMID38844638
PMCPMC12382592

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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.