Evidence map›Paper›PMID 30799074›Full record

ArticleBiophysical journal2019

Force Spectroscopy Shows Dynamic Binding of Influenza Hemagglutinin and Neuraminidase to Sialic Acid.

Valentin Reiter-Scherer, Jose Luis Cuellar-Camacho, Sumati Bhatia, Rainer Haag, Andreas Herrmann, Daniel Lauster, Jürgen P Rabe

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Valentin Reiter-SchererDepartment of Physics and IRIS Adlershof, Humboldt-Universität zu Berlin, Berlin, Germany.
Jose Luis Cuellar-CamachoDepartment of Chemistry, Freie Universität Berlin, Berlin, Germany.
Sumati BhatiaDepartment of Chemistry, Freie Universität Berlin, Berlin, Germany.
Rainer HaagDepartment of Chemistry, Freie Universität Berlin, Berlin, Germany.
Andreas HerrmannDepartment of Biology and IRI Life Sciences, Humboldt-Universität zu Berlin, Berlin, Germany.
Daniel LausterDepartment of Biology and IRI Life Sciences, Humboldt-Universität zu Berlin, Berlin, Germany. Electronic address: daniel.lauster@biologie.hu-berlin.de.
Jürgen P RabeDepartment of Physics and IRIS Adlershof, Humboldt-Universität zu Berlin, Berlin, Germany. Electronic address: rabe@physik.hu-berlin.de.
Humboldt-Universität zu Berlin · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influenza A virus infects target cells through multivalent interactions of its major spike proteins, hemagglutinin (HA) and neuraminidase (NA), with the cellular receptor sialic acid (SA). HA is known to mediate the attachment of the virion to the cell, whereas NA enables the release of newly formed virions by cleaving SA from the cell. Because both proteins target the same receptor but have antagonistic functions, virus infection depends on a properly tuned balance of the kinetics of HA and NA activities for viral entry to and release from the host cell. Here, dynamic single-molecule force spectroscopy, based on scanning force microscopy, was employed to determine these bond-specific kinetics, characterized by the off rate k

Indexed as

Mechanical PhenomenaSpectrum AnalysisBiomechanical PhenomenaCell MembraneHemagglutinin Glycoproteins, Influenza VirusKineticsN-Acetylneuraminic AcidNeuraminidaseProtein BindingHemagglutinin Glycoproteins, Influenza VirusN-Acetylneuraminic AcidNeuraminidase

Identifiers

PMID30799074
PMCPMC6428919
OpenAlexW2912106058

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.