Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

The integrins.

Yoshikazu Takada1, Xiaojing Ye, Scott Simon

  • 1Department of Dermatology, University of California Davis School of Medicine, Second Avenue, Sacramento, CA 95817, USA. ytakada@ucdavis.edu

Genome Biology
|June 5, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

EXPRESS: Mechanical Compaction Alters Microstructural and Magnetic Resonance Imaging Properties of Acute Ischemic Stroke Clots.

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism·2026
Same author

IGF1 Binding to Integrin αvβ3 Induces Direct Gα13 Binding to IGF1R Kinase.

International journal of molecular sciences·2026
Same author

Galectin-3 Binds to the Allosteric Site and Activates Integrins αvβ3, αIIbβ3, and α5β1, and Lactose Inhibits This Activation.

Biomolecules·2026
Same author

Amyloid-β-driven glymphatic dysfunction in Alzheimer's disease model mice is driven by Ca<sup>2+</sup>-mediated increases in astrocytic cholesterol.

Nature neuroscience·2026
Same author

Computational fluid dynamics assessment of altered hemodynamics in the Circle of Willis during acute ischemic stroke and the impact of cerebral collateral development.

Biomechanics and modeling in mechanobiology·2026
Same author

Galectin-3 binds to the RGD-binding site in a glycan-independent manner and to the allosteric site and activates integrins αvβ3, αIIbβ3, and α5β1.

bioRxiv : the preprint server for biology·2026
Same journal

Integrated lipidomic and transcriptomic profiling of the host response in human malaria.

Genome biology·2026
Same journal

Centromeric satellite expansion drives genome evolution in the snowy owl.

Genome biology·2026
Same journal

Mapping the landscape of allele-specific expression in porcine genomes.

Genome biology·2026
Same journal

Genomic sequence evolution underlying human neocortical interareal diversification.

Genome biology·2026
Same journal

Regulatory mechanisms driven by functional 3'-UTR variants in alcohol use disorder and related traits.

Genome biology·2026
Same journal

A longitudinal single-nucleus transcriptomic atlas of bovine placentation reveals dynamic cellular hierarchies and regulatory programs.

Genome biology·2026
See all related articles

Integrins are cell adhesion receptors crucial for cell communication. This overview focuses on mammalian integrins, detailing their structure, function, and diverse roles in biological processes.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrins are a large family of cell adhesion receptors.
  • They function as transmembrane alpha-beta heterodimers, with numerous subunits forming diverse combinations.
  • Integrins mediate cell interactions with extracellular matrix, other cells, and soluble molecules.

Purpose of the Study:

  • To provide an overview of mammalian integrins.
  • To focus on the organization, structure, and function of these receptors.
  • To highlight their role in cell adhesion and signaling.

Main Methods:

  • Literature review and synthesis of existing research on integrins.
  • Focus on mammalian integrin structure, ligand binding, and signaling pathways.

Related Experiment Videos

  • Comparative analysis with integrins in other organisms.

    • Main Results:

    • Mammalian integrins comprise at least 18 alpha and 8 beta subunits, forming 24 distinct heterodimers.
    • Ligand binding involves specific motifs like arginine-glycine-aspartic acid (RGD) and interactions with molecules such as intercellular adhesion molecules (ICAMs).
    • Integrins play a dual role in signal transduction, transmitting signals into and out of the cell.

    Conclusions:

    • Integrins are essential for cell adhesion, migration, and signaling.
    • Their diverse structures allow for specific interactions with various ligands.
    • Further research into mammalian integrins is crucial due to their extensive study and importance.