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 Concept Videos

Affinity and Avidity01:41

Affinity and Avidity

37.4K
Overview
37.4K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

3.8K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.8K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.2K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
3.2K
Activation of Integrins01:15

Activation of Integrins

4.5K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
4.5K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.2K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.2K
Types of Signaling Molecules01:32

Types of Signaling Molecules

12.0K
In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...
12.0K

You might also read

Related Articles

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

Sort by
Same author

Blocking protein quality control degradation leads to structural stabilization of DHFR indel variants.

The FEBS journal·2026
Same author

Ultrastructure of dopaminergic varicosities revealed by cryo-correlative light and electron microscopy.

The Journal of cell biology·2026
Same author

Conkazal-M1 from the MKAVA family of conotoxins: A dual-function protease inhibitor and neuroactive peptide.

Protein science : a publication of the Protein Society·2026
Same author

Transient Helicity in the Intrinsically Disordered Protein ACTR Measured by Hydrogen Exchange.

Biochemistry·2026
Same author

Residue-Specific Signatures of Structural Water Identified by Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.

Angewandte Chemie (International ed. in English)·2026
Same author

Structural heterogeneity in mRNA-LNP subpopulations revealed by AF4-SAXS: implications for cargo loading and cell transfection.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Nov 19, 2025

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

21.9K

Binding Revisited-Avidity in Cellular Function and Signaling.

Simon Erlendsson1,2, Kaare Teilum3

  • 1Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.

Frontiers in Molecular Biosciences
|February 1, 2021
PubMed
Summary

Avidity, the combined strength of multiple biomolecular interactions, explains stronger cellular binding than predicted by affinity alone. This review explores avidity principles, prediction methods, and its role in intracellular signaling.

Keywords:
aviditycellular avidityfunctional affinitymodeling avidityretention time

More Related Videos

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

16.5K
Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

3.8K

Related Experiment Videos

Last Updated: Nov 19, 2025

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

21.9K
Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

16.5K
Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

3.8K

Area of Science:

  • Biochemistry
  • Biophysics
  • Systems Biology

Background:

  • Avidity describes the accumulated strength of multiple interactions, distinct from affinity.
  • It accounts for factors like reduced dimensionality and hindered diffusion near surfaces.
  • Avidity explains discrepancies between in vitro affinity measurements and in vivo binding strength.

Purpose of the Study:

  • To review the principles and theoretical frameworks of avidity in biological systems.
  • To discuss methods for predicting and simulating avidity.
  • To explore the influence of avidity on intracellular signaling processes.

Main Methods:

  • Literature review of avidity principles and theoretical frameworks.
  • Analysis of existing methods for avidity prediction and simulation.
  • Case study examination of avidity in intracellular signaling.

Main Results:

  • Avidity is a macroscopic parameter influenced by multiple microscopic binding events.
  • Theoretical frameworks exist for understanding and predicting avidity.
  • Avidity significantly impacts intracellular signaling pathways.

Conclusions:

  • Avidity is crucial for understanding complex biomolecular interactions, especially at surfaces.
  • Further research is needed to fully elucidate avidity's role in intracellular processes.
  • Understanding avidity enhances predictions of biological binding phenomena.