Evidence map›Paper›PMID 40050111›Full record

ArticleJournal of the American Society for Mass Spectrometry2025

Computed Vibrational Heat Capacities for Gas-Phase Biomolecular Ions.

Lawren R Paris, Austin W Green, James S Prell

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Lawren R ParisDepartment of Chemistry and Biochemistry, 1253 University of Oregon, Eugene, Oregon 97403-1253, United States.
Austin W GreenDepartment of Chemistry and Biochemistry, 1253 University of Oregon, Eugene, Oregon 97403-1253, United States.
James S PrellDepartment of Chemistry and Biochemistry, 1253 University of Oregon, Eugene, Oregon 97403-1253, United States.ORCID 0000-0002-7505-9168

Funding

Quantitative Determination of High-Order Protein Structure with Native Ion Mobility-Mass Spectrometry and Computational ChemistryR01GM144507 · NIGMS · UNIVERSITY OF OREGON · PI James Stephen Prell · 2022 to 2026
$1.2M
NIGMS NIH HHS R01 GM144507
6 · The paper itself

Abstract

Collision induced dissociation (CID) and collision induced unfolding (CIU) experiments are important tools for determining the structures of and differences between biomolecular complexes with mass spectrometry. However, quantitative comparison of CID/CIU data acquired on different platforms or even using different regions of the same instrument can be very challenging due to differences in gas identity and pressure, electric fields, and other experimental parameters. In principle, these can be reconciled by a detailed understanding of how ions heat, cool, and dissociate or unfold in time as a function of these parameters. Fundamental information needed to model these processes for different ion types and masses is their heat capacity as a function of the internal (

Indexed as

collision induced dissociationcollision induced unfoldingcomputational chemistrymass spectrometrythermochemistry

Identifiers

PMID40050111
PMCPMC12261789

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.