Evidence map›Paper›PMID 18390627›Full record

ArticleBiophysical journal2008

Measuring diffusion and binding kinetics by contact area FRAP.

Timothy P Tolentino, Jianhua Wu, Veronika I Zarnitsyna, Ying Fang, Michael L Dustin, Cheng Zhu

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Two-dimensional measurements of receptor-ligand interactions.Frontiers in molecular biosciences · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Relationship of 2D Affinity to T Cell Functional Outcomes.International journal of molecular sciences · 2020
    Review
  10. A modeling platform for the lymphatic system.Journal of theoretical biology · 2020
    Article
  11. Review
  12. Article
  13. [The preparation of supported lipid bilayers and its functional study].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2019
    Article
  14. Article
  15. Review
  16. Remarkably low affinity of CD4/peptide-major histocompatibility complex class II protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Review
  19. Linking 3D and 2D binding kinetics of membrane proteins by multiscale simulations.Protein science : a publication of the Protein Society · 2014
    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

6 authors at 2 institutions in 2 countries.

Timothy P TolentinoWallace H. Coulter Department of Biomedical Engineering and George W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Jianhua Wu
Veronika I Zarnitsyna
Ying Fang
Michael L Dustin
Cheng Zhu
Georgia Institute of Technology · USNew York University · US

Funding

Research Training Program Plan on Cell and Tissue Engineering (CTEng)T32GM008433 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI GARCIA, ANDRES J · 1991 to 2021
$7.1M
Ligand Binding Kinetics and Cell Adhesion by Fc ReceptorR01AI038282 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2001 to 2005
$1.9M
PHYSIOLOGICAL CHEMISTRY OF INTEGRIN FUNCTIONR01AI044931 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DUSTIN, MICHAEL LORAN · 1999 to 2007
$1.5M
Physiological Chemistry of Integrin FunctionR56AI044931 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DUSTIN, MICHAEL LORAN · 2009 to 2010
$474k
Kinetic analysis of ligand binding by TCR and CD8R56AI038282 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2012 to 2012
$389k
LIGAND BONDING FORCE AND CELL ADHESION BY CD16 ISOFORMSR29AI038282 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 1995 to 1999
–
NIAID NIH HHS AI38282NIAID NIH HHS AI44931NIAID NIH HHS R01 AI038282NIAID NIH HHS R01 AI044931NIAID NIH HHS R29 AI038282NIAID NIH HHS R56 AI038282NIAID NIH HHS R56 AI044931NIGMS NIH HHS GM08433NIGMS NIH HHS T32 GM008433
6 · The paper itself

Abstract

The immunological synapse is a stable intercellular structure that specializes in substance and signal transfer from one immune cell to another. Its formation is regulated in part by the diffusion of adhesion and signaling molecules into, and their binding of countermolecules in the contact area. The stability of immunological synapses allows receptor-ligand interactions to approximate chemical equilibrium despite other dynamic aspects. We have developed a mathematical model that describes the coupled reaction-diffusion process in an established immunological synapse. In this study, we extend a previously described contact area fluorescence recovery after photobleaching (FRAP) experiment to test the validity of the model. The receptor binding activity and lateral mobility of fluorescently labeled, lipid-anchored ligands in the bilayer resulted in their accumulation, as revealed by a much higher fluorescence intensity inside the contact area than outside. After complete photobleaching of the synapse, fluorescence recovery requires ligands to dissociate and rebind, and to diffuse in and out of the contact area. Such a FRAP time course consequently provides information on reaction and diffusion, which can be extracted by fitting the model solution to the data. Surprisingly, reverse rates in the two-dimensional contact area were at least 100-fold slower than in three-dimensional solution. As previously reported in immunological synapses, a significant nonrecoverable fraction of fluorescence was observed with one of two systems studied, suggesting some ligands either dissociated or diffused much more slowly compared with other ligands in the same synapse. The combined theory and experiment thus provides a new method for in situ measurements of kinetic rates, diffusion coefficients, and nonrecoverable fractions of interacting molecules in immunological synapses and other stable cell-bilayer junctions.

Indexed as

Models, BiologicalModels, ChemicalBinding SitesComputer SimulationDiffusionFluorescence Recovery After PhotobleachingKineticsProtein BindingProtein Interaction MappingProteinsProteins

Identifiers

PMID18390627
PMCPMC2440437
OpenAlexW2068838259

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.