Evidence map›Paper›PMID 32031732›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Characterization of [2Fe-2S]-Cluster-Bridged Protein Complexes and Reaction Intermediates by use of Native Mass Spectrometric Methods.

Mengxuan Jia, Sambuddha Sen, Christine Wachnowsky, Insiya Fidai, James A Cowan, Vicki H Wysocki

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  11. 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.

Mengxuan JiaDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0001-9173-1084
Sambuddha SenDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0001-6079-0268
Christine WachnowskyDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.
Insiya FidaiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.
James A CowanDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0002-4686-6825
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0003-0495-2538

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
Novel Therapeutic Approaches to Pathogen InactivationR21AI072443 · NIAID · OHIO STATE UNIVERSITY · PI COWAN, JAMES A · 2009 to 2010
$398k
NIAID NIH HHS R21 AI072443NIGMS NIH HHS P41 GM128577
6 · The paper itself

Abstract

Many iron-sulfur proteins involved in cluster trafficking form [2Fe-2S]-cluster-bridged complexes that are often challenging to characterize because of the inherent instability of the cluster at the interface. Herein, we illustrate the use of fast, online buffer exchange coupled to a native mass spectrometry (OBE nMS) method to characterize [2Fe-2S]-cluster-bridged proteins and their transient cluster-transfer intermediates. The use of this mechanistic and protein-characterization tool is demonstrated with holo glutaredoxin 5 (GLRX5) homodimer and holo GLRX5:BolA-like protein 3 (BOLA3) heterodimer. Using the OBE nMS method, cluster-transfer reactions between the holo-dimers and apo-ferredoxin (FDX2) are monitored, and intermediate [2Fe-2S] species, such as (FDX2:GLRX5:[2Fe-2S]:GSH) and (FDX2:BOLA3:GLRX5:[2Fe-2S]:GSH) are detected. The OBE nMS method is a robust technique for characterizing iron-sulfur-cluster-bridged protein complexes and transient iron-sulfur-cluster transfer intermediates.

Indexed as

Mass SpectrometryGlutaredoxinsIron-Sulfur ProteinsMitochondrial ProteinsProtein MultimerizationProtein Structure, QuaternaryBolA3 protein, humanGlutaredoxinsIron-Sulfur ProteinsMitochondrial Proteinscofactorsiron-sulfur clustersnative mass spectrometryprotein complexesstructural biology

Identifiers

PMID32031732
PMCPMC7170024

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Registered trials

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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.