Evidence map›Paper›PMID 28449072›Full record

ReviewPathogens and disease2017

Functions of galectins as 'self/non-self'-recognition and effector factors.

Gerardo R Vasta, Chiguang Feng, Nuria González-Montalbán, Justin Mancini, Lishi Yang, Kelsey Abernathy, Graeme Frost, Cheyenne Palm

Open access · bronzeAbstract readReview
In one paragraph

Review in Pathogens and disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Sweetening ferroptosis spread.Nature chemical biology · 2025
    Article
  4. Galectin-9-An Emerging Glyco-Immune Checkpoint Target for Cancer Therapy.International journal of molecular sciences · 2025
    Review
  5. Article
  6. Article
  7. A "proto" type galectin expressed in striped bass (Frontiers in cellular and infection microbiology · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation.International journal of environmental research and public health · 2022
    Review
  17. Review
  18. Review
  19. Review
  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

8 authors at 2 institutions in 1 country.

Gerardo R VastaDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Chiguang FengDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Nuria González-MontalbánDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Justin ManciniDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Lishi YangDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Kelsey AbernathyDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Graeme FrostDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
Cheyenne PalmDepartment of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
University of Maryland, Baltimore · USColumbus Center · US

Funding

Signaling Pathways in Innate ImmunityT32AI095190 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI Stefanie N. Vogel · 2012 to 2026
$4.7M
Biological Roles of GalectinsR01GM070589 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI VASTA, GERARDO RAUL · 2004 to 2013
$2.0M
NIAID NIH HHS T32 AI095190NIGMS NIH HHS R01 GM070589
6 · The paper itself

Abstract

Carbohydrate structures on the cell surface encode complex information that through specific recognition by carbohydrate-binding proteins (lectins) modulates interactions between cells, cells and the extracellular matrix, or mediates recognition of potential microbial pathogens. Galectins are a family of ß-galactoside-binding lectins, which are evolutionary conserved and have been identified in most organisms, from fungi to invertebrates and vertebrates, including mammals. Since their discovery in the 1970s, their biological roles, initially understood as limited to recognition of endogenous carbohydrate ligands in embryogenesis and development, have expanded in recent years by the discovery of their roles in tissue repair and regulation of immune homeostasis. More recently, evidence has accumulated to support the notion that galectins can also bind glycans on the surface of potentially pathogenic microbes, and function as recognition and effector factors in innate immunity, thus establishing a new paradigm. Furthermore, some parasites 'subvert' the recognition roles of the vector/host galectins for successful attachment or invasion. These recent findings have revealed a striking functional diversification in this structurally conserved lectin family.

Indexed as

Host-Pathogen InteractionsImmune EvasionImmunity, InnateAnimalsGalectinsHumansReceptors, ImmunologicGalectinsReceptors, Immunologiccarbohydrate recognition domain: glycanschimerafunctiongalectins, ß-galactosidepattern recognition receptorsproto-typestructuretandem repeat

Identifiers

PMID28449072
PMCPMC5808656
OpenAlexW2609238184

What OpenQuestion holds

Textmetadata
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.