Evidence map›Paper›PMID 26117840›Full record

ArticleJournal of molecular cell biology2016

E-selectin ligand complexes adopt an extended high-affinity conformation.

Roland C Preston, Roman P Jakob, Florian P C Binder, Christoph P Sager, Beat Ernst, Timm Maier

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 69 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Article
  4. Article
  5. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Review
  10. Review
  11. E-selectin in vascular pathophysiology.Frontiers in immunology · 2024
    Review
  12. Article
  13. Review
  14. Receptor-Ligand Binding: Effect of Mechanical Factors.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Computationally guided conversion of the specificity of E-selectin to mimic that of Siglec-8.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    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

6 authors at 1 institution in 1 country.

Roland C PrestonInstitute of Molecular Pharmacy, Universität Basel, 4056 Basel, Switzerland.
Roman P JakobBiozentrum, Universität Basel, 4056 Basel, Switzerland.
Florian P C BinderInstitute of Molecular Pharmacy, Universität Basel, 4056 Basel, Switzerland.
Christoph P SagerInstitute of Molecular Pharmacy, Universität Basel, 4056 Basel, Switzerland.
Beat ErnstInstitute of Molecular Pharmacy, Universität Basel, 4056 Basel, Switzerland timm.maier@unibas.ch beat.ernst@unibas.ch.
Timm MaierBiozentrum, Universität Basel, 4056 Basel, Switzerland timm.maier@unibas.ch beat.ernst@unibas.ch.
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)). Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode. Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations. Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution. This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment. The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists. This is of special interest, since their therapeutic potential was recently demonstrated with the pan-selectin antagonists GMI-1070 (Rivipansel).

Indexed as

E-SelectinGlycolipidsHumansProtein BindingProtein ConformationProtein Structure, SecondaryE-SelectinGlycolipidsrivipanselconformational changeE-selectinglycomimetic antagonistinflammationleukocyte adhesionsialyl Lewisx

Identifiers

PMID26117840
PMCPMC4710209
OpenAlexW1955707222

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.