Evidence map›Paper›PMID 9726957›Full record

ArticleBiophysical journal1998

Measuring two-dimensional receptor-ligand binding kinetics by micropipette.

S E Chesla, P Selvaraj, C Zhu

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 206 papers.

0numbers the graph read from it
0cells of the map it votes in
206citing papers in PubMed
6.0field-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

206 citing papers in PubMed, 415 citations in OpenAlex.

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  12. Understanding Viral-Glycocalyx Interactions Using Brush-Linked to Cross-Linked Models.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  13. Conformational response of αStructure (London, England : 1993) · 2025
    Article
  14. Article
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146 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

S E CheslaGeorge W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta 30332-0405, USA.
P Selvaraj
C Zhu
Georgia Institute of Technology · USEmory 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
Kinetic analysis of ligand binding by TCR and CD8R56AI038282 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2012 to 2012
$389k
MEMBRANE ANCHORING AND FUNCTION OF CD16R29AI030631 · NIAID · EMORY UNIVERSITY · PI SELVARAJ, PERIASAMY · 1992 to 1996
–
LIGAND BONDING FORCE AND CELL ADHESION BY CD16 ISOFORMSR29AI038282 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 1995 to 1999
–
NIAID NIH HHS AI30631NIAID NIH HHS AI38282NIGMS NIH HHS GM08433
6 · The paper itself

Abstract

We report a novel method for measuring forward and reverse kinetic rate constants, kf0 and kr0, for the binding of individual receptors and ligands anchored to apposing surfaces in cell adhesion. Not only does the method examine adhesion between a single pair of cells; it also probes predominantly a single receptor-ligand bond. The idea is to quantify the dependence of adhesion probability on contact duration and densities of the receptors and ligands. The experiment was an extension of existing micropipette protocols. The analysis was based on analytical solutions to the probabilistic formulation of kinetics for small systems. This method was applied to examine the interaction between Fc gamma receptor IIIA (CD16A) expressed on Chinese hamster ovary cell transfectants and immunoglobulin G (IgG) of either human or rabbit origin coated on human erythrocytes, which were found to follow a monovalent biomolecular binding mechanism. The measured rate constants are Ackf0 = (2.6 +/- 0.32) x 10(-7) micron 4 s-1 and kr0 = (0.37 +/- 0.055) s-1 for the CD16A-hIgG interaction and Ackf0 = (5.7 +/- 0.31) X 10(-7) micron 4 s-1 and kr0 = (0.20 +/- 0.042) s-1 for the CD16A-rIgG interaction, respectively, where Ac is the contact area, estimated to be a few percent of 3 micron 2.

Indexed as

AnimalsBiophysicsCell AdhesionCHO CellsCricetinaeHumansImmunoglobulin GKineticsLigandsModels, BiologicalModels, StatisticalRabbitsReceptors, Cell SurfaceReceptors, IgGRecombinant ProteinsReproducibility of ResultsImmunoglobulin GLigandsReceptors, Cell SurfaceReceptors, IgGRecombinant Proteins

Identifiers

PMID9726957
PMCPMC1299830
OpenAlexW2001625690

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.