Evidence map›Paper›PMID 34714071›Full record

ArticleJournal of the American Society for Mass Spectrometry2021

Influence of Primary Structure on Fragmentation of Native-Like Proteins by Ultraviolet Photodissociation.

Luis A Macias, Sarah N Sipe, Inês C Santos, Aarti Bashyal, M Rachel Mehaffey, Jennifer S Brodbelt

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors.

Luis A MaciasDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID https://orcid.org/0000-0003-1949-6029
Sarah N SipeDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Inês C SantosDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Aarti BashyalDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
M Rachel MehaffeyDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID https://orcid.org/0000-0003-3207-0217

Funding

Ultraviolet Photodissociation Mass Spectrometry for Characterization of Biological MoleculesR35GM139658 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2021 to 2025
$2.9M
UVPD Mass Spectrometry of Protein ComplexesR01GM121714 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2017 to 2020
$1.4M
Implementing Photodissociation Mass Spectrometry to study Disease and Lipid StructureF31CA257404 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MACIAS, LUIS A · 2021 to 2022
$49k
NCI NIH HHS F31 CA257404NIGMS NIH HHS R01 GM121714NIGMS NIH HHS R35 GM139658
6 · The paper itself

Abstract

Analysis of native-like protein structures in the gas phase via native mass spectrometry and auxiliary techniques has become a powerful tool for structural biology applications. In combination with ultraviolet photodissociation (UVPD), native top-down mass spectrometry informs backbone flexibility, topology, hydrogen bonding networks, and conformational changes in protein structure. Although it is known that the primary structure affects dissociation of peptides and proteins in the gas phase, its effect on the types and locations of backbone cleavages promoted by UVPD and concomitant influence on structural characterization of native-like proteins is not well understood. Here, trends in the fragmentation of native-like proteins were evaluated by tracking the propensity of 10 fragment types (

Indexed as

ProteinsMass SpectrometryPeptide FragmentsPhotolysisProtein ConformationUltraviolet RaysPeptide FragmentsProteins

Identifiers

PMID34714071
PMCPMC8639798

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.