Evidence map›Paper›PMID 34228963›Full record

ArticleArchives of biochemistry and biophysics2021

A structure and function relationship study to identify the impact of the R721G mutation in the human mitochondrial lon protease.

Zhou Sha, Monica M Montano, Kristy Rochon, Jason A Mears, Daniel Deredge, Patrick Wintrode, Luke Szweda, Natalie Mikita, Irene Lee

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Review
  2. Review
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 3 institutions in 1 country.

Zhou ShaDepartment of Chemistry, Case Western Reserve University, Cleveland, OH, 44106, USA.
Monica M MontanoDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106, USA.
Kristy RochonDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106, USA.
Jason A MearsDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106, USA; Center for Mitochondrial Diseases, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106, USA.
Daniel DeredgeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD, 21201, USA.
Patrick WintrodeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD, 21201, USA.
Luke SzwedaDepartment of Internal Medicine, Division of Cardiology, UT Southwestern Medical Center, Dallas, TX, 75390, USA.
Natalie MikitaDepartment of Chemistry, Case Western Reserve University, Cleveland, OH, 44106, USA; Department of Chemistry, Missouri Western State University, St. Joseph, MO, 64507, USA. Electronic address: nmikita@missouriwestern.edu.
Irene LeeDepartment of Chemistry, Case Western Reserve University, Cleveland, OH, 44106, USA. Electronic address: ixl13@case.edu.
Case Western Reserve University · USUniversity of Maryland, Baltimore · USSouthwestern Medical Center · US

Funding

Oxidative DNA Damage Regulates Cardiomyocyte ProliferationR01HL138983 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI SADEK, HESHAM, SZWEDA, LUKE IGNATIUS · 2018 to 2021
$3.1M
Supplement: Defining Molecular Interactions that Drive Mitochondrial FissionR01GM125844 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI Jason Mears · 2018 to 2026
$2.8M
HEXIM1 regulation of transcriptional networks critical for tumor suppressionR01CA195558 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MONTANO, MONICA · 2016 to 2020
$1.8M
Mitochondrial Dynamics in Brain TumorInitiating CellsR01CA208516 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MEARS, JASON · 2017 to 2021
$1.6M
Drp1 Structure: Regulatory Domains and Conformational FlexibilityF31GM139324 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI ROCHON, KRISTY · 2020 to 2022
$138k
NCI NIH HHS R01 CA195558NCI NIH HHS R01 CA208516NHLBI NIH HHS R01 HL138983NIGMS NIH HHS F31 GM139324NIGMS NIH HHS R01 GM125844
6 · The paper itself

Abstract

Lon is an ATP-dependent protease belonging to the "ATPase associated with diverse cellular activities" (AAA+) protein family. In humans, Lon is translated as a precursor and imported into the mitochondria matrix through deletion of the first 114 amino acid residues. In mice, embryonic knockout of lon is lethal. In humans, some dysfunctional lon mutations are tolerated but they cause a developmental disorder known as the CODAS syndrome. To gain a better understanding on the enzymology of human mitochondrial Lon, this study compares the structure-function relationship of the WT versus one of the CODAS mutants R721G to identify the mechanistic features in Lon catalysis that are affected. To this end, steady-state kinetics were used to quantify the difference in ATPase and ATP-dependent peptidase activities between WT and R721G. The K

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBiocatalysisB-LymphocytesCraniofacial AbnormalitiesEnzyme StabilityEye AbnormalitiesGrowth DisordersHip Dislocation, CongenitalHumansKineticsMiceMitochondriaModels, MolecularMolecular Dynamics SimulationMutant ProteinsPDK4 protein, humanProtease LaPyruvate Dehydrogenase Acetyl-Transferring KinaseRecombinant ProteinsCODASHydrogen-deuterium exchangeLon proteaseNucleotide induced conformational changesSteady-state kinetics

Identifiers

PMID34228963
PMCPMC9290781
OpenAlexW3178719386

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.