Evidence map›Paper›PMID 21746908›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure.

John J Brady, Elizabeth J Judge, Robert J Levis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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
3.7field-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

17 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  4. Quantification of Protein-Ligand Interactions by Laser Electrospray Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018
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  10. Increasing protein charge state when using laser electrospray mass spectrometry.Journal of the American Society for Mass Spectrometry · 2015
    Article
  11. Article
  12. Article
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  15. Do charge state signatures guarantee protein conformations?Journal of the American Society for Mass Spectrometry · 2012
    Article
  16. Article
  17. Femtosecond laser vaporization that preserves protein-folded structure: an unproven idea.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

John J BradyDepartment of Chemistry, Temple University, Philadelphia, PA 19122, USA.
Elizabeth J Judge
Robert J Levis
Temple University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Femtosecond laser vaporization-based mass spectrometry can be used to measure protein conformation in vitro at atmospheric pressure. Cytochrome c and lysozyme are vaporized from the condensed phase into the gas phase intact when exposed to an intense (10(13) W/cm(2)), nonresonant (800 nm), ultrafast (75 fs) laser pulse. Electrospray postionization time-of-flight mass spectrometry reveals that the vaporized protein maintains the solution-phase conformation through measurement of the charge-state distribution and the collision-induced dissociation channels.

Indexed as

AnimalsChickensCytochromes cHorsesLasersMuramidaseProtein ConformationProtein FoldingProteinsSolutionsSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationVolatilizationWaterCytochromes cMuramidaseProteinsSolutionsWater

Identifiers

PMID21746908
PMCPMC3145716
OpenAlexW2042402300

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.