Evidence map›Paper›PMID 35073092›Full record

ArticleJournal of the American Society for Mass Spectrometry2022

Investigation of Charge-State-Dependent Compaction of Protein Ions with Native Ion Mobility-Mass Spectrometry and Theory.

Amber D Rolland, Lejla S Biberic, James S Prell

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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  5. Review
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  10. Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024
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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.

Amber D RollandDepartment of Chemistry and Biochemistry, University of Oregon, 1253 University of Oregon, Eugene, Oregon 97403-1253, United States.ORCID https://orcid.org/0000-0002-7905-8250
Lejla S BibericDepartment of Chemistry and Biochemistry, University of Oregon, 1253 University of Oregon, Eugene, Oregon 97403-1253, United States.
James S PrellDepartment of Chemistry and Biochemistry, University of Oregon, 1253 University of Oregon, Eugene, Oregon 97403-1253, United States.ORCID https://orcid.org/0000-0002-7505-9168

Funding

MOLECULAR BIOLOGY AND BIOPHYSICST32GM007759 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 1985 to 2021
$8.5M
Mass Spectrometry Analysis of Lipid-Protein Interactions and Structural Heterogeneity in the Anthrax Toxin PoreR21AI125804 · NIAID · UNIVERSITY OF OREGON · PI PRELL, JAMES STEPHEN · 2017 to 2018
$424k
NIAID NIH HHS R21 AI125804NIGMS NIH HHS T32 GM007759
6 · The paper itself

Abstract

The precise relationship between native gas-phase protein ion structure, charge, desolvation, and activation remains elusive. Much evidence supports the Charge Residue Model for native protein ions formed by electrospray ionization, but scaling laws derived from it relate only to overall ion size. Closer examination of drift tube CCSs across individual native protein ion charge state distributions (CSDs) reveals deviations from global trends. To investigate whether this is due to structure variation across CSDs or contributions of long-range charge-dipole interactions, we performed

Indexed as

Concanavalin AGasesGlutamate DehydrogenaseIon Mobility SpectrometryIonsLactoglobulinsMolecular Dynamics SimulationProtein ConformationConcanavalin AGasesGlutamate DehydrogenaseIonsLactoglobulins

Identifiers

PMID35073092
PMCPMC11404549

What OpenQuestion holds

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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.