Evidence map›Paper›PMID 20655861›Full record

ArticleBiophysical journal2010

Force-induced lysozyme--HyHEL5 antibody dissociation and its analysis by means of a cooperative binding model.

Stefan Katletz, Cordula Stroh, Christian Rankl, Urbaan M Titulaer, Peter Hinterdorfer

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

5 authors at 2 institutions in 1 country.

Stefan KatletzInstitute for Theoretical Physics, Johannes Kepler University of Linz, Linz, Austria.
Cordula Stroh
Christian Rankl
Urbaan M Titulaer
Peter Hinterdorfer
Johannes Kepler University of Linz · ATAgilent Technologies (Austria) · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamic force spectroscopy probes the kinetic properties of molecules interacting with each other such as antibody-antigen, receptor-ligand, etc. In this article, a statistical model for the dissociation of such cooperative systems is presented. The partner molecules are assumed to be linked by a number of relatively weak bonds that can be grouped together into cooperative units. Single bonds are assumed to open and close statistically. Our model was used to analyze molecular recognition experiments of single receptor-ligand pairs in which the two molecules are brought into contact using an atomic force microscope, which leads to the formation of a strong and specific bond. Then a prescribed time-dependent force is applied to the complex and the statistical distribution of forces needed to pull the molecules completely apart is measured. This quantity is also calculated from our model. Furthermore, its dependence on the model parameters, such as binding free energy, number of bonds and groups, number of cooperative elementary bonds and degree of cooperativity within a group, influence of the force on the binding free energy, and the rate of change of the pulling force, is determined.

Indexed as

Microscopy, Atomic ForceModels, BiologicalAlanineAntibodiesCrystallography, X-RayKineticsMolecular Dynamics SimulationMuramidasePoint MutationProtein BindingAlanineAntibodiesMuramidase

Identifiers

PMID20655861
PMCPMC2908737
OpenAlexW2081969290

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.