Evidence map›Paper›PMID 21721569›Full record

ArticleAnalytical chemistry2011

Use of real-time, label-free analysis in revealing low-affinity binding to blood group antigens by Helicobacter pylori.

Y Y Fei, A Schmidt, G Bylund, D X Johansson, S Henriksson, C Lebrilla, J V Solnick, T Borén, X D Zhu

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 47 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. The Journal of biological chemistry · 2018
    Article
  5. Article
  6. Article
  7. Evaluation of Kinetics Using Label-Free Optical Biosensors.Instrumentation science & technology · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Carbohydrate microarrays.Chemical Society reviews · 2013
    Review
  16. Article
  17. Gut microbes
    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

9 authors at 5 institutions in 4 countries.

Y Y FeiDepartment of Physics, University of California, Davis, Davis, California 95616, United States.
A Schmidt
G Bylund
D X Johansson
S Henriksson
C Lebrilla
J V Solnick
T Borén
X D Zhu
Umeå University · SEInstitute of Applied Physics · RUInstitute of Molecular Medicine · INOffice of Infectious Diseases · USUniversity of California, Davis · US

Funding

Modulation of Outer Membrane Protein Expressin in Helicobacter pyloriR01AI070803 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SOLNICK, JAY V. · 2008 to 2012
$2.4M
High-Speed Label-Free Optical Detection System for Small-Molecule MicroarraysR01HG003827 · NHGRI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ZHU, XIANGDONG · 2006 to 2009
$2.2M
Studies of Naturally Occurring Structurally Modified CarbohydratesR01GM076360 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2006 to 2010
$1.9M
Role of H. pylori Outer Membrane Proteins in Colonization and Host ResponseR01AI081037 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SOLNICK, JAY V. · 2009 to 2013
$1.1M
NHGRI NIH HHS R01 HG003827NIAID NIH HHS R01 AI070803NIAID NIH HHS R01 AI081037NIGMS NIH HHS R01 GM076360NIGMS NIH HHS R01 GM076360-04S1
6 · The paper itself

Abstract

Infectious diseases are often initiated by microbial adherence that is mediated by the binding of attachment molecules, termed adhesins, to cell surface receptors on host cells. We present an experimental system, oblique-incidence reflectivity difference (OI-RD) microscopy, which allows the detection of novel, low-affinity microbial attachment mechanisms that may be essential for infectious processes. OI-RD microscopy was used to analyze direct binding of the oncopathogen, Helicobacter pylori ( H. pylori ) to immobilized glycoconjugates in real time with no need for labeling tags. The results suggest the presence of additional Lewis b blood group antigen (Le(b)) binding adhesins that have not been detected previously. OI-RD microscopy also confirmed the high-affinity binding of H. pylori outer-membrane protein BabA to Le(b). The OI-RD microscopy method is broadly applicable to real-time characterization of intact microbial binding to host receptors and offers new strategies to elucidate the molecular interactions of infectious agents with human host cells.

Indexed as

Bacterial AdhesionAdhesins, BacterialCloning, MolecularEscherichia coliGlycoconjugatesHelicobacter InfectionsHelicobacter pyloriHumansLewis Blood Group AntigensMicroscopyPlasmidsProtein BindingProtein Structure, TertiaryRecombinant ProteinsAdhesins, BacterialBabA protein, Helicobacter pyloriGlycoconjugatesLewis Blood Group AntigensRecombinant Proteins

Identifiers

PMID21721569
PMCPMC3155641
OpenAlexW2014695135

What OpenQuestion holds

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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.