Evidence map›Paper›PMID 38503445›Full record

ReviewImmunology2024

Sialic acid in the regulation of blood cell production, differentiation and turnover.

Eric Edward Irons, Sajina Gc, Joseph T Y Lau

Open access · hybridAbstract readReview
In one paragraph

Review in Immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Sialylation in the nervous system: Functions and mechanisms.The Journal of biological chemistry · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. 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

3 authors at 1 institution in 1 country.

Eric Edward IronsDepartment of Molecular and Cellular Biology, Roswell Park Comprehensive Cancer Center, Buffalo, New York, USA.ORCID 0000-0002-2282-5244
Sajina GcDepartment of Molecular and Cellular Biology, Roswell Park Comprehensive Cancer Center, Buffalo, New York, USA.ORCID 0000-0003-2676-2794
Joseph T Y LauDepartment of Molecular and Cellular Biology, Roswell Park Comprehensive Cancer Center, Buffalo, New York, USA.ORCID 0000-0002-5128-2664
Roswell Park Comprehensive Cancer Center · US

Funding

REGULATION OF LACTOSAMINYL GLYCAN BIOSYNTHESIS IN HEMATOPOIETIC CELLSP01HL107146 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI SACKSTEIN, ROBERT · 2011 to 2017
$17.7M
Project 3: Role of Glycosaminoglycans in HematopoiesisP01HL151333 · NHLBI · VERSITI WISCONSIN, INC. · PI HOFFMEISTER, KARIN MARIA · 2021 to 2025
$12.3M
ST6Gal-1 Sialyltransferase in InflammationR01AI140736 · NIAID · ROSWELL PARK CANCER INSTITUTE CORP · PI LAU, JOSEPH TY · 2018 to 2021
$3.9M
National Institute of Allergy and Infectious Diseases R01AI140736NHLBI NIH HHS P01 HL107146NHLBI NIH HHS P01 HL151333NHLBI NIH HHS P01HL151333NIAID NIH HHS R01 AI140736
6 · The paper itself

Abstract

Sialic acid is a unique sugar moiety that resides in the distal and most accessible position of the glycans on mammalian cell surface and extracellular glycoproteins and glycolipids. The potential for sialic acid to obscure underlying structures has long been postulated, but the means by which such structural changes directly affect biological processes continues to be elucidated. Here, we appraise the growing body of literature detailing the importance of sialic acid for the generation, differentiation, function and death of haematopoietic cells. We conclude that sialylation is a critical post-translational modification utilized in haematopoiesis to meet the dynamic needs of the organism by enforcing rapid changes in availability of lineage-specific cell types. Though long thought to be generated only cell-autonomously within the intracellular ER-Golgi secretory apparatus, emerging data also demonstrate previously unexpected diversity in the mechanisms of sialylation. Emphasis is afforded to the mechanism of extrinsic sialylation, whereby extracellular enzymes remodel cell surface and extracellular glycans, supported by charged sugar donor molecules from activated platelets.

Indexed as

Cell DifferentiationN-Acetylneuraminic AcidAnimalsHematopoiesisHumansPolysaccharidesProtein Processing, Post-TranslationalN-Acetylneuraminic AcidPolysaccharidesbone marrowcell deathextrinsic sialylationgalactosegalectinhaematopoiesislectinssialic acidsialyltransferasesiglec

Identifiers

PMID38503445
PMCPMC11223974
OpenAlexW4394765460

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.