Evidence map›Paper›PMID 8842247›Full record

ArticleBiophysical journal1996

Kinetics and locus of failure of receptor-ligand-mediated adhesion between latex spheres. I. Protein-carbohydrate bond.

D F Tees, H L Goldsmith

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

13 citing papers in PubMed, 33 citations in OpenAlex.

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  11. Experimental study of the interaction range and association rate of surface-attached cadherin 11.Proceedings of the National Academy of Sciences of the United States of America · 1998
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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

2 authors at 1 institution in 1 country.

D F TeesMcGill University Medical Clinic, Montréal General Hospital Research Institute, Québec, Canada.
H L Goldsmith
Montreal General Hospital · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously described the use of a counter-rotating cone and plate rheoscope to measure the time and force dependence of break-up of doublets of sphered, swollen, and fixed red cells (SSRC) cross-linked by monoclonal IgM antibody. It has been shown that doublet break-up can occur by extraction of receptors from the membrane, rather than by antibody-antigen bond break-up, and is a stochastic process. We therefore prepared 4.62-microns carboxyl modified latex spheres with a covalently coupled synthetic blood group B antigen trisaccharide. Using a two-step carbodiimide process, ethylene diamine was covalently linked to the carboxyl modified latex spheres, and the trisaccharide, having an eight carbon spacer modified to bear a terminal carboxyl group, was linked to the ethylene diamine. Using these antigen spheres we carried out studies in Couette flow, in a transparent cone and plate rheoscope, of the shear-induced break-up of doublets cross-linked by monoclonal IgM anti-B antibody in 19% and 15% Dextran 40. As previously found with SSRC, over a range of normal force from 55 to 175 pN, there was a distribution in times to break-up. However, the fraction of antigen sphere doublets broken up, which increased from 0.08 to 0.43 at 75 pM IgM, and from 0.06 to 0.20 at 150 pM IgM, was significantly lower than that for the SSRC, where the fraction broken up at 150 pM IgM increased from 0.10 to 0.47. Thus, significantly higher forces were required to achieve the same degree of break-up for doublets of antigen-linked spheres than for SSRC. Computer simulation using a stochastic model of break-up showed that the differences between antigen sphere and SSRC doublet break-up were due to a change in bond character (the range and depth of the bond energy minimum) rather than to an increase in the number of bonds linking antigen-sphere doublets. This supports the notion that antibody-antigen bonds are ruptured in the case of antigen spheres, whereas antigen is able to be extracted from the membrane of SSRC, although changes of receptor substrate from cell to latex and the possibility of latex strand extraction from the microspheres are potential complicating factors.

Indexed as

MicrospheresABO Blood-Group SystemAnimalsAntibodies, MonoclonalAntigen-Antibody ComplexCarbohydrate SequenceDextransGoatsImmunoglobulin GImmunoglobulin MKineticsLatexMiceMolecular Sequence DataProtein BindingRabbitsABO Blood-Group SystemAntibodies, MonoclonalAntigen-Antibody ComplexDextransImmunoglobulin GImmunoglobulin MLatexSucroseTrisaccharides

Identifiers

PMID8842247
PMCPMC1233565
OpenAlexW4253883393

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.