Evidence map›Paper›PMID 28192979›Full record

ArticleAnalytical chemistry2017

Structural Characterization of Native Proteins and Protein Complexes by Electron Ionization Dissociation-Mass Spectrometry.

Huilin Li, Yuewei Sheng, William McGee, Michael Cammarata, Dustin Holden, Joseph A Loo

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
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  6. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for 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

6 authors.

Huilin LiDepartment of Biological Chemistry, David Geffen School of Medicine, University of California , Los Angeles, California 90095, United States.
Yuewei ShengDepartment of Chemistry and Biochemistry, UCLA/DOE Institute of Genomics and Proteomics, and UCLA Molecular Biology Institute, University of California , Los Angeles, California 90095, United States.
William McGeeDepartment of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Michael CammarataDepartment of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Dustin HoldenDepartment of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.
Joseph A LooDepartment of Biological Chemistry, David Geffen School of Medicine, University of California , Los Angeles, California 90095, United States.ORCID 0000-0001-9989-1437

Funding

UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
Ultra-High Resolution Mass Spectrometer for Biomedical ResearchS10RR028893 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2010 to 2010
$2.7M
NCRR NIH HHS S10 RR028893NIGMS NIH HHS R01 GM103479
6 · The paper itself

Abstract

Mass spectrometry (MS) has played an increasingly important role in the identification and structural and functional characterization of proteins. In particular, the use of tandem mass spectrometry has afforded one of the most versatile methods to acquire structural information for proteins and protein complexes. The unique nature of electron capture dissociation (ECD) for cleaving protein backbone bonds while preserving noncovalent interactions has made it especially suitable for the study of native protein structures. However, the intra- and intermolecular interactions stabilized by hydrogen bonds and salt bridges can hinder the separation of fragments even with preactivation, which has become particularly problematic for the study of large macromolecular proteins and protein complexes. Here, we describe the capabilities of another activation method, 30 eV electron ionization dissociation (EID), for the top-down MS characterization of native protein-ligand and protein-protein complexes. Rich structural information that cannot be delivered by ECD can be generated by EID. EID allowed for the comparison of the gas-phase and the solution-phase structural stability and unfolding process of human carbonic anhydrase I (HCA-I). In addition, the EID fragmentation patterns reflect the structural similarities and differences among apo-, Zn-, and Cu,Zn-superoxide dismutase (SOD1) dimers. In particular, the structural changes due to Cu-binding and a point mutation (G41D) were revealed by EID-MS. The performance of EID was also compared to that of 193 nm ultraviolet photodissociation (UVPD), which allowed us to explore their qualitative similarities and differences as potential valuable tools for the MS study of native proteins and protein complexes.

Indexed as

Carbonic Anhydrase IDimerizationHumansLigandsPhotolysisPoint MutationProtein UnfoldingSpectrometry, Mass, Electrospray IonizationSpectroscopy, Fourier Transform InfraredSuperoxide Dismutase-1Ultraviolet RaysCarbonic Anhydrase ILigandsSuperoxide Dismutase-1

Identifiers

PMID28192979
PMCPMC5495147

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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.