Evidence map›Paper›PMID 31025855›Full record

ArticleAnalytical chemistry2019

Illuminating Biological Interactions with in Vivo Protein Footprinting.

Jessica A Espino, Lisa M Jones

Open access · bronzeAbstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  8. Review
  9. Article
  10. Dimethylthiourea as a Quencher in Hydroxyl Radical Protein Footprinting Experiments.Journal of the American Society for Mass Spectrometry · 2023
    Article
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  13. Review
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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

2 authors at 1 institution in 1 country.

Jessica A EspinoDepartment of Pharmaceutical Sciences , University of Maryland , Baltimore , Maryland 21201 , United States.
Lisa M JonesDepartment of Pharmaceutical Sciences , University of Maryland , Baltimore , Maryland 21201 , United States.ORCID 0000-0001-8825-060X
University of Maryland, Baltimore · US

Funding

Development of an In Vivo Footprinting Method Coupled with Mass Spectrometry in C. elegansR01GM127595 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI JONES, LISA M · 2018 to 2021
$1.4M
Development of a novel pulse-chase in-cell footprinting method for protein folding analysisR01GM128985 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI JONES, LISA M · 2018 to 2021
$1.2M
NIGMS NIH HHS R01 GM127595NIGMS NIH HHS R01 GM128985
6 · The paper itself

Abstract

Protein footprinting coupled with mass spectrometry is being increasingly used for the study of protein interactions and conformations. The hydroxyl radical footprinting method, fast photochemical oxidation of proteins (FPOP), utilizes hydroxyl radicals to oxidatively modify solvent accessible amino acids. Here, we describe the further development of FPOP for protein structural analysis in vivo (IV-FPOP) with Caenorhabditis elegans. C. elegans, part of the nematode family, are used as model systems for many human diseases. The ability to perform structural studies in these worms would provide insight into the role of structure in disease pathogenesis. Many parameters were optimized for labeling within the worms including the microfluidic flow system and hydrogen peroxide concentration. IV-FPOP was able to modify several hundred proteins in various organs within the worms. The method successfully probed solvent accessibility similarily to in vitro FPOP, demonstrating its potential for use as a structural technique in a multiorgan system. The coupling of the method with mass spectrometry allows for amino-acid-residue-level structural information, a higher resolution than currently available in vivo methods.

Indexed as

AnimalsCaenorhabditis elegansChromatography, LiquidHydrogen PeroxideIndicators and ReagentsOxidation-ReductionProtein FootprintingProteinsTandem Mass SpectrometryHydrogen PeroxideIndicators and ReagentsProteins

Identifiers

PMID31025855
PMCPMC6533598
OpenAlexW2941471101

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.