Evidence map›Paper›PMID 24055473›Full record

ArticleFEBS letters2013

NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.

Theresa A Ramelot, Yunhuang Yang, Indra D Sahu, Hsiau-Wei Lee, Rong Xiao, Gary A Lorigan, Gaetano T Montelione, Michael A Kennedy

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Anilinopyrimidine Resistance inFrontiers in microbiology · 2017
    Article
  13. Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017
    Review
  14. 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

8 authors at 4 institutions in 1 country.

Theresa A RamelotDepartment of Chemistry and Biochemistry, Northeast Structural Genomics Consortium, Miami University, Oxford, OH 45056, USA. Electronic address: theresa.ramelot@miamiOH.edu.
Yunhuang Yang
Indra D Sahu
Hsiau-Wei Lee
Rong Xiao
Gary A Lorigan
Gaetano T Montelione
Michael A Kennedy
Miami University · USJohnson University · USJoint Center for Structural Genomics · USRutgers, The State University of New Jersey · US

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
Partnership for High-Throughput Enabled Biology of the Mitochondrial ProteomeU01GM094622 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2010 to 2014
$7.8M
NIGMS NIH HHS U01 GM094622NIGMS NIH HHS U01-GM094622NIGMS NIH HHS U54 GM094597NIGMS NIH HHS U54-GM094597
6 · The paper itself

Abstract

We have determined the solution NMR structure of the intermembrane space domain (IMSD) of the human mitochondrial ATPase associated with various activities (AAA) protease known as AFG3-like protein 2 (AFG3L2). Our structural analysis and molecular dynamics results indicate that the IMSD is peripherally bound to the membrane surface. This is a modification to the location of the six IMSDs in a model of the full length yeast hexaoligomeric homolog of AFG3L2 determined at low resolution by electron cryomicroscopy [1]. The predicted protein-protein interaction surface, located on the side furthest from the membrane, may mediate binding to substrates as well as prohibitins.

Indexed as

Adenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesATP-Dependent ProteasesCell MembraneCryoelectron MicroscopyHumansMitochondriaMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein MultimerizationAdenosine TriphosphatasesAFG3L2 protein, humanATPases Associated with Diverse Cellular ActivitiesATP-Dependent Proteasesm-AAA proteaseMolecular dynamicsNMR structure

Identifiers

PMID24055473
PMCPMC4043124
OpenAlexW2121762283

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.