Evidence map›Paper›PMID 39208253›Full record

ArticleJournal of the American Society for Mass Spectrometry2024

Investigating Protein-Nucleic Acid Binding Interactions with Diethylpyrocarbonate Covalent Labeling-Mass Spectrometry.

Zachary J Kirsch, Jonathan Ashby, Richard W Vachet

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Zachary J KirschDepartment of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0000-0001-7788-6223
Jonathan AshbyDepartment of Chemistry, Trinity College, Hartford, Connecticut 06106, United States.
Richard W VachetDepartment of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0000-0003-4514-0210

Funding

Protein Amyloid Formation and Inhibition Studied by Mass SpectrometryR35GM145272 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RICHARD W VACHET · 2022 to 2026
$2.0M
Acquisition of an Orbitrap MSS10OD010645 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI EYLES, STEPHEN J. · 2013 to 2013
$600k
NIGMS NIH HHS R35 GM145272NIH HHS S10 OD010645
6 · The paper itself

Abstract

Nucleic acids are important biomolecules that facilitate numerous cellular functions and have in recent years become promising candidates for treating disease. Consequently, there is a need for methods to characterize protein interactions with these molecules. Here, we demonstrate that diethylpyrocarbonate (DEPC) covalent labeling-mass spectrometry (CL-MS) can provide structural information for protein-nucleic acid binding by characterizing the binding sites of two DNA aptamers specific to thrombin. Reductions in thrombin labeling are observed at the pair's binding interfaces. Furthermore, we find that binding of the aptamers causes changes in labeling at residues in the thrombin active site and known exosites for each aptamer, showcasing the sensitivity of DEPC CL-MS to significant allosteric changes.

Indexed as

Aptamers, NucleotideDiethyl PyrocarbonateMass SpectrometryProtein BindingThrombinBinding SitesHumansModels, MolecularAptamers, NucleotideDiethyl PyrocarbonateThrombin

Identifiers

PMID39208253
PMCPMC11497156

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Registered trials

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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.