Evidence map›Paper›PMID 20550917›Full record

ArticleBiophysical journal2010

Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy.

Antonia Göhler, Sabine André, Herbert Kaltner, Markus Sauer, Hans-Joachim Gabius, Sören Doose

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 16% 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, 39 citations in OpenAlex.

  1. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    Review
  2. Article
  3. Article
  4. Exploring functional pairing between surface glycoconjugates and human galectins using programmable glycodendrimersomes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Article
  7. Article
  8. Sweet complementarity: the functional pairing of glycans with lectins.Cellular and molecular life sciences : CMLS · 2016
    Review
  9. Article
  10. Article
  11. Adhesion/growth-regulatory galectins in the human eye: localization profiles and tissue reactivities as a standard to detect disease-associated alterations.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2012
    Article
  12. Article
  13. 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 1 country.

Antonia GöhlerApplied Laser Physics and Laser Spectroscopy, Bielefeld University, Bielefeld, Germany.
Sabine André
Herbert Kaltner
Markus Sauer
Hans-Joachim Gabius
Sören Doose
Bielefeld University · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescence correlation spectroscopy is applied on homologous human lectins (i.e., adhesion/growth-regulatory galectins) to detect influence of ligand binding and presence of the linker peptide in tandem-repeat-type proteins on hydrodynamic properties. Among five tested proteins, lactose binding increased the diffusion constant only in the cases of homodimeric galectin-1 and the linkerless variant of tandem-repeat-type galectin-4. To our knowledge, the close structural similarity among galectins does not translate into identical response to ligand binding. Kinetic measurements show association and dissociation rate constants in the order of 1 to 10(3) M(-1) s(-1) and 10(-4) s(-1), respectively. Presence of the linker peptide in tandem-repeat-type protein leads to anomalous scaling with molecular mass. These results provide what we believe to be new insights into lectin responses to glycan binding, detectable so far only by small angle neutron scattering, and the structural relevance of the linker peptide. Methodologically, fluorescence correlation spectroscopy is shown to be a rather simple technical tool to characterize hydrodynamic properties of these proteins at a high level of sensitivity.

Indexed as

AnimalsDiffusionGalectinsHumansKineticsLactoseLigandsModels, MolecularMolecular WeightNeutron DiffractionProtein MultimerizationProtein Structure, QuaternaryScattering, Small AngleSequence DeletionSpectrometry, FluorescenceTandem Repeat SequencesGalectinsLactoseLigands

Identifiers

PMID20550917
PMCPMC2884264
OpenAlexW1994173859

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.