Evidence map›Paper›PMID 28755259›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Structural Characterization of a Thrombin-Aptamer Complex by High Resolution Native Top-Down Mass Spectrometry.

Jiang Zhang, Rachel R Ogorzalek Loo, Joseph A Loo

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

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  13. Characterizing Thermal Transitions of IgG with Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019
    Article
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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

3 authors at 1 institution in 1 country.

Jiang ZhangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, 90095, USA.
Rachel R Ogorzalek LooDepartment of Biological Chemistry, David Geffen School of Medicine at UCLA, Molecular Biology Institute, and UCLA/DOE Institute for Genomics and Proteomics, University of California, Los Angeles, CA, 90095, USA.
Joseph A LooDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, 90095, USA. JLoo@chem.ucla.edu.
University of California, Los Angeles · US

Funding

UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
Ultra-High Resolution Mass Spectrometer for Biomedical ResearchS10RR028893 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2010 to 2010
$2.7M
Foundation for the National Institutes of Health R01GM103479Foundation for the National Institutes of Health S10RR028893NCRR NIH HHS S10 RR028893NIGMS NIH HHS R01 GM103479U.S. Department of Energy DE-FC03-02ER63421
6 · The paper itself

Abstract

Native mass spectrometry (MS) with electrospray ionization (ESI) has evolved as an invaluable tool for the characterization of intact native proteins and non-covalently bound protein complexes. Here we report the structural characterization by high resolution native top-down MS of human thrombin and its complex with the Bock thrombin binding aptamer (TBA), a 15-nucleotide DNA with high specificity and affinity for thrombin. Accurate mass measurements revealed that the predominant form of native human α-thrombin contains a glycosylation mass of 2205 Da, corresponding to a sialylated symmetric biantennary oligosaccharide structure without fucosylation. Native MS showed that thrombin and TBA predominantly form a 1:1 complex under near physiological conditions (pH 6.8, 200 mM NH

Indexed as

Aptamers, NucleotideBinding SitesHumansMass SpectrometryModels, MolecularProtein BindingThrombinAptamers, NucleotideThrombinthrombin aptamerBinding interfaceElectron capture dissociationGas phase structureNative mass spectrometryProtein–DNA complex

Identifiers

PMID28755259
PMCPMC5711526
OpenAlexW2740464753

What OpenQuestion holds

Textmetadata
LicenceTDM
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.