Evidence map›Paper›PMID 36309885›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2022

Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy.

Brianne E Lewis, Courtney J Campbell, Andria Rodrigues, Lindsey Thompson, Ashutosh K Pandey, Sarah N Gallagher, Debkumar Pain, Andrew Dancis, Timothy L Stemmler

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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 4 institutions in 1 country.

Brianne E LewisDepartment of Foundational Medical Studies, Oakland University William Beaumont School of Medicine, Rochester, MI, 48309, USA.
Courtney J CampbellDepartment of Pharmaceutical Science, Wayne State University, 259 Mack Avenue, Detroit, MI, 48201, USA.
Andria RodriguesDepartment of Pharmaceutical Science, Wayne State University, 259 Mack Avenue, Detroit, MI, 48201, USA.
Lindsey ThompsonDepartment of Pharmaceutical Science, Wayne State University, 259 Mack Avenue, Detroit, MI, 48201, USA.
Ashutosh K PandeyDepartment of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, 07103, USA.
Sarah N GallagherDepartment of Pharmaceutical Science, Wayne State University, 259 Mack Avenue, Detroit, MI, 48201, USA.
Debkumar PainDepartment of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, 07103, USA.
Andrew DancisDivision of Hematology-Oncology, Perelman School of Medicine, Department of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Timothy L StemmlerDepartment of Pharmaceutical Science, Wayne State University, 259 Mack Avenue, Detroit, MI, 48201, USA. timothy.stemmler@wayne.edu.
Wayne State University · USRutgers, The State University of New Jersey · USOakland University · USUniversity of Pennsylvania · US

Funding

Mitochondria-cytoplasm interactions for cytosolic Fe-S cluster assemblyR01GM107542 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI DANCIS, ANDREW B., PAIN, DEBKUMAR · 2014 to 2023
$4.5M
Structural Insights into the Function of FrataxinR01DK068139 · NIDDK · WAYNE STATE UNIVERSITY · PI STEMMLER, TIMOTHY LOUIS · 2005 to 2015
$3.5M
NIDDK NIH HHS R01 DK068139NIDDK NIH HHS R01DK068139NIDDK NIH HHS R01GM107542NIDDK NIH HHS T32HL12082205NIGMS NIH HHS R01 GM107542
6 · The paper itself

Abstract

Mitochondrial [2Fe-2S] cluster biosynthesis is driven by the coordinated activities of the Iron-Sulfur Cluster (ISC) pathway protein machinery. Within the ISC machinery, the protein that provides a structural scaffold on which [2Fe-2S] clusters are assembled is the ISCU protein in humans; this protein is referred to as the "Scaffold" protein. Truncation of the C-terminal portion of ISCU causes the fatal disease "ISCU Myopathy", which exhibits phenotypes of reduced Fe-S cluster assembly in cells. In this report, the yeast ISCU ortholog "Isu1" has been characterized to gain a better understanding of the role of the scaffold protein in relation to [2Fe-2S] assembly and ISCU Myopathy. Here we explored the biophysical characteristics of the C-terminal region of Isu1, the segment of the protein that is truncated on the human ortholog during the disease ISCU Myopathy. We characterized the role of this region in relation to iron binding, protein stability, assembly of the ISC multiprotein complex required to accomplish Fe-S cluster assembly, and finally on overall cell viability. We determined the Isu1 C-terminus is essential for the completion of the Fe-S cluster assembly but serves a function independent of protein iron binding.

Indexed as

Iron-Sulfur ProteinsMuscular DiseasesSaccharomyces cerevisiae ProteinsHumansIronMitochondrial ProteinsSaccharomyces cerevisiaeSulfonylurea CompoundsIronIron-Sulfur ProteinsISCU protein, humanISU1 protein, S cerevisiaeMitochondrial ProteinsSaccharomyces cerevisiae ProteinsSulfonylurea Compoundssulofenur[2Fe-2S] clustersIron–Sulfur Cluster Assembly PathwayIsu1Scaffold protein

Identifiers

PMID36309885
PMCPMC13374633
OpenAlexW4307621458

What OpenQuestion holds

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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.