Evidence map›Paper›PMID 25450980›Full record

ReviewBiochimica et biophysica acta2015

Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.

Jin Hae Kim, Jameson R Bothe, T Reid Alderson, John L Markley

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. The NMR contribution to protein-protein networking in Fe-S protein maturation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Hybrid Methods in Iron-Sulfur Cluster Biogenesis.Frontiers in molecular biosciences · 2017
    Review
  15. Article
  16. Article
  17. Cleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe-2S cluster.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Functional implications of the interaction between HscB and IscU in the biosynthesis of FeS clusters.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    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

4 authors at 1 institution in 1 country.

Jin Hae KimBiochemistry Department, University of Wisconsin-Madison, Madison, WI 53706, USA.
Jameson R BotheBiochemistry Department, University of Wisconsin-Madison, Madison, WI 53706, USA.
T Reid AldersonBiochemistry Department, University of Wisconsin-Madison, Madison, WI 53706, USA.
John L MarkleyBiochemistry Department, University of Wisconsin-Madison, Madison, WI 53706, USA. Electronic address: jmarkley@wisc.edu.
University of Wisconsin–Madison · US

Funding

WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
Partnership for High-Throughput Enabled Biology of the Mitochondrial ProteomeU01GM094622 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2010 to 2014
$7.8M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Integrated state-of-the-art LC-MS/NMR system for the University of WisconsinS10RR025062 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$1.7M
Upgrade of the NMRFAM 750 MHz NMR SpectrometerS10RR029220 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2010 to 2010
$766k
NMR Spectrometer System Optimized for Direct 13C or 15N DetectionS10RR023438 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$500k
Energetic Insights into Protein Disorder and Function from the Scaffold IscUF32GM110939 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BOTHE, JAMESON R · 2014 to 2014
$19k
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISONS10RR002781 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1986 to 1986
–
NCRR NIH HHS P41 RR002301NCRR NIH HHS P41RR02301NCRR NIH HHS S10 RR002781NCRR NIH HHS S10 RR008438NCRR NIH HHS S10 RR023438NCRR NIH HHS S10RR023438NCRR NIH HHS S10 RR025062NCRR NIH HHS S10RR025062NCRR NIH HHS S10 RR029220NCRR NIH HHS S10RR029220NIGMS NIH HHS F32 GM110939NIGMS NIH HHS P41 GM066326NIGMS NIH HHS P41 GM103399NIGMS NIH HHS P41GM66326NIGMS NIH HHS U01 GM094622NIGMS NIH HHS U01 GM94622
6 · The paper itself

Abstract

Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have evolved machinery consisting of specialized proteins that operate together to assemble Fe-S clusters efficiently so as to minimize cellular exposure to their toxic constituents: iron and sulfide ions. To date, the best studied system is the iron-sulfur cluster (isc) operon of Escherichia coli, and the eight ISC proteins it encodes. Our investigations over the past five years have identified two functional conformational states for the scaffold protein (IscU) and have shown that the other ISC proteins that interact with IscU prefer to bind one conformational state or the other. From analyses of the NMR spectroscopy-derived network of interactions of ISC proteins, small-angle X-ray scattering (SAXS) data, chemical crosslinking experiments, and functional assays, we have constructed working models for Fe-S cluster assembly and delivery. Future work is needed to validate and refine what has been learned about the E. coli system and to extend these findings to the homologous Fe-S cluster biosynthetic machinery of yeast and human mitochondria. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.

Indexed as

Scattering, Small AngleCross-Linking ReagentsEscherichia coliEscherichia coli ProteinsHumansIron-Sulfur ProteinsMagnetic Resonance SpectroscopyOperonProtein BindingX-Ray DiffractionCross-Linking ReagentsEscherichia coli ProteinsIron-Sulfur ProteinsConformational equilibriaIron–sulfur cluster biosynthesisNuclear magnetic resonance (NMR) spectroscopyProtein–protein interactionsSmall-angle X-ray scattering (SAXS)

Identifiers

PMID25450980
PMCPMC4390431
OpenAlexW2023466257

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.