Evidence map›Paper›PMID 29444440›Full record

ArticleCell reports2018

Measuring Integrin Conformational Change on the Cell Surface with Super-Resolution Microscopy.

Travis I Moore, Jesse Aaron, Teng-Leong Chew, Timothy A Springer

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Biomechanical anticoagulation by spherical platelets in extracorporeal systems.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. MUC15 Ectodomain Architecture Regulates Integrin Clustering to Control Cancer Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  11. Review
  12. pH-regulated single cell migration.Pflugers Archiv : European journal of physiology · 2024
    Review
  13. Article
  14. What's the Catch? The Significance of Catch Bonds in T Cell Activation.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. 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

4 authors at 3 institutions in 1 country.

Travis I MooreDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Jesse AaronAdvanced Imaging Center, Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA.
Teng-Leong ChewAdvanced Imaging Center, Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA.
Timothy A SpringerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA. Electronic address: springer_lab@crystal.harvard.edu.
Harvard University · USImaging Center · USJanelia Research Campus · US

Funding

LYMPHOCYTE FUNCTION ASSOCIATED ANTIGENSR37CA031798 · NCI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 2004 to 2013
$8.3M
LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGENSR01CA031798 · NCI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1985 to 2018
$5.1M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA031798NCI NIH HHS R37 CA031798
6 · The paper itself

Abstract

We use super-resolution interferometric photoactivation and localization microscopy (iPALM) and a constrained photoactivatable fluorescent protein integrin fusion to measure the displacement of the head of integrin lymphocyte function-associated 1 (LFA-1) resulting from integrin conformational change on the cell surface. We demonstrate that the distance of the LFA-1 head increases substantially between basal and ligand-engaged conformations, which can only be explained at the molecular level by integrin extension. We further demonstrate that one class of integrin antagonist maintains the bent conformation, while another antagonist class induces extension. Our molecular scale measurements on cell-surface LFA-1 are in excellent agreement with distances derived from crystallographic and electron microscopy structures of bent and extended integrins. Our distance measurements are also in excellent agreement with a previous model of LFA-1 bound to ICAM-1 derived from the orientation of LFA-1 on the cell surface measured using fluorescence polarization microscopy.

Indexed as

Allosteric RegulationCell AdhesionCell MembraneCell MovementFibronectinsFluorescent DyesHEK293 CellsHumansIntegrinsIntercellular Adhesion Molecule-1Jurkat CellsLymphocyte Function-Associated Antigen-1MicroscopyModels, BiologicalProtein ConformationRecombinant Fusion ProteinsFibronectinsFluorescent DyesIntegrinsIntercellular Adhesion Molecule-1Lymphocyte Function-Associated Antigen-1Recombinant Fusion Proteinsadhesion receptorscell adhesioncell migrationcell-surface receptorsimmunologyintegrinsiPALMlymphocyteprotein conformationsuper-resolution microscopy

Identifiers

PMID29444440
PMCPMC5851489
OpenAlexW2785355701

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

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.