Evidence map›Paper›PMID 34500643›Full record

ReviewMolecules (Basel, Switzerland)2021

Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down.

Ravneet Kaur Grewal, Abdul Rajjak Shaikh, Suresh Gorle, Manjeet Kaur, Paula Alexendra Videira, Luigi Cavallo, Mohit Chawla

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 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, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  9. Article
  10. Putative role of TMEM165 in congenital cardiomyopathies.Frontiers in molecular neuroscience · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Sialyl LewisCancers · 2023
    Article
  17. Article
  18. The Search for Cryptic L-Rhamnosyltransferases on theJournal of fungi (Basel, Switzerland) · 2022
    Article
  19. 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

7 authors at 4 institutions in 4 countries.

Ravneet Kaur GrewalSTEMskills Research and Education Lab Private Limited, Faridabad 121002, Haryana, India.ORCID 0000-0002-7251-7979
Abdul Rajjak ShaikhSTEMskills Research and Education Lab Private Limited, Faridabad 121002, Haryana, India.ORCID 0000-0003-4444-0684
Suresh GorleSTEMskills Research and Education Lab Private Limited, Faridabad 121002, Haryana, India.
Manjeet KaurBiotechnology Engineering, University Institute of Engineering & Technology (UIET), Maharshi Dayanand University, Rohtak 124001, Haryana, India.
Paula Alexendra VideiraAssociate Laboratory i4HB-Institute for Health and Bioeconomy, NOVA School of Science and Technology, NOVA University Lisbon, 2819-516 Caparica, Portugal.ORCID 0000-0001-5987-2485
Luigi CavalloKaust Catalysis Center, Physical Sciences and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.
Mohit ChawlaKaust Catalysis Center, Physical Sciences and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.ORCID 0000-0002-3332-3055
King Abdullah University of Science and Technology · SAMaharshi Dayanand University · INThe University of Texas Medical Branch at Galveston · USUnidade em Ciências Biomoleculares Aplicadas

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian cell surfaces are modified with complex arrays of glycans that play major roles in health and disease. Abnormal glycosylation is a hallmark of cancer; terminal sialic acid and fucose in particular have high levels in tumor cells, with positive implications for malignancy. Increased sialylation and fucosylation are due to the upregulation of a set of sialyltransferases (STs) and fucosyltransferases (FUTs), which are potential drug targets in cancer. In the past, several advances in glycostructural biology have been made with the determination of crystal structures of several important STs and FUTs in mammals. Additionally, how the independent evolution of STs and FUTs occurred with a limited set of global folds and the diverse modular ability of catalytic domains toward substrates has been elucidated. This review highlights advances in the understanding of the structural architecture, substrate binding interactions, and catalysis of STs and FUTs in mammals. While this general understanding is emerging, use of this information to design inhibitors of STs and FUTs will be helpful in providing further insights into their role in the manifestation of cancer and developing targeted therapeutics in cancer.

Indexed as

AnimalsCatalysisCatalytic DomainFucosyltransferasesGlycosylationHumansMammalsSialyltransferasesFucosyltransferasesSialyltransferasesdrug designfucosyltransferaseglyocosyltransferases in cancersialyltransferase

Identifiers

PMID34500643
PMCPMC8433944
OpenAlexW3198328878

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.