Evidence map›Paper›PMID 32275426›Full record

ArticleJournal of the American Society for Mass Spectrometry2020

Structural Evaluation of Protein/Metal Complexes via Native Electrospray Ultraviolet Photodissociation Mass Spectrometry.

Christopher M Crittenden, Elisa T Novelli, M Rachel Mehaffey, Gulan N Xu, David H Giles, Whitney A Fies, Kevin N Dalby, Lauren J Webb, Jennifer S Brodbelt

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. 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

9 authors at 1 institution in 1 country.

Christopher M CrittendenDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.ORCID http://orcid.org/0000-0001-7792-2554
Elisa T NovelliDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.ORCID http://orcid.org/0000-0002-4046-1229
M Rachel MehaffeyDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.
Gulan N XuDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.
David H GilesDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712, United States.
Whitney A FiesDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.
Kevin N DalbyDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712, United States.ORCID http://orcid.org/0000-0001-9272-5129
Lauren J WebbDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.ORCID http://orcid.org/0000-0001-9999-5500
Jennifer S BrodbeltDepartment of Chemistry, University of Texas, Austin, Texas 78712, United States.ORCID http://orcid.org/0000-0003-3207-0217
The University of Texas at Austin · US

Funding

Regulation of eEF-2K an Energy and Nutrient SensorR01GM123252 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI DALBY, KEVIN N, GHOSE, RANAJEET · 2017 to 2024
$2.7M
UVPD Mass Spectrometry of Protein ComplexesR01GM121714 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2017 to 2020
$1.4M
NIGMS NIH HHS R01 GM121714NIGMS NIH HHS R01 GM123252
6 · The paper itself

Abstract

Ultraviolet photodissociation (UVPD) has emerged as a promising tool to characterize proteins with regard to not only their primary sequences and post-translational modifications, but also their tertiary structures. In this study, three metal-binding proteins, Staphylococcal nuclease, azurin, and calmodulin, are used to demonstrate the use of UVPD to elucidate metal-binding regions via comparisons between the fragmentation patterns of apo (metal-free) and holo (metal-bound) proteins. The binding of staphylococcal nuclease to calcium was evaluated, in addition to a series of lanthanide(III) ions which are expected to bind in a similar manner as calcium. On the basis of comparative analysis of the UVPD spectra, the binding region for calcium and the lanthanide ions was determined to extend from residues 40-50, aligning with the known crystal structure. Similar analysis was performed for both azurin (interrogating copper and silver binding) and calmodulin (four calcium binding sites). This work demonstrates the utility of UVPD methods for determining and analyzing the metal binding sites of a variety of classes of proteins.

Indexed as

Amino Acid SequenceAzurinBinding SitesCalciumCalmodulinLanthanoid Series ElementsMetalsMicrococcal NucleaseModels, MolecularSpectrometry, Mass, Electrospray IonizationAzurinCalciumCalmodulinLanthanoid Series ElementsMetalsMicrococcal Nucleaseprotein/metal complexesultraviolet photodissociation mass spectrometry

Identifiers

PMID32275426
PMCPMC7386362
OpenAlexW3015359929

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.