Evidence map›Paper›PMID 28028182›Full record

ArticleThe Journal of biological chemistry2017

Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function.

Adeleye J Afolayan, Maxwell Alexander, Rebecca L Holme, Teresa Michalkiewicz, Ujala Rana, Ru-Jeng Teng, Sara Zemanovic, Daisy Sahoo, Kirkwood A Pritchard, Girija G Konduri

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Heat therapy: mechanistic underpinnings and applications to cardiovascular health.Journal of applied physiology (Bethesda, Md. : 1985) · 2021
    Review
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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

10 authors at 1 institution in 2 countries.

Adeleye J AfolayanFrom the Department of Pediatrics, Cardiovascular Research Center, aafolaya@mcw.edu.
Maxwell AlexanderFrom the Department of Pediatrics, Cardiovascular Research Center.
Rebecca L HolmeChildren's Research Institute.
Teresa MichalkiewiczFrom the Department of Pediatrics, Cardiovascular Research Center.
Ujala RanaFrom the Department of Pediatrics, Cardiovascular Research Center.
Ru-Jeng TengFrom the Department of Pediatrics, Cardiovascular Research Center.
Sara ZemanovicFrom the Department of Pediatrics, Cardiovascular Research Center.
Daisy SahooChildren's Research Institute.
Kirkwood A PritchardChildren's Research Institute.
Girija G KonduriFrom the Department of Pediatrics, Cardiovascular Research Center.
Children's Hospital of Wisconsin · US

Funding

Mechanisms of Inflammation in Sickle Cell DiseaseR01HL128371 · NHLBI · MEDICAL COLLEGE OF WISCONSIN · PI PRITCHARD, KIRKWOOD ARTHUR · 2016 to 2024
$4.2M
Biophysics of HDL DysfunctionR01HL112270 · NHLBI · MEDICAL COLLEGE OF WISCONSIN · PI PRITCHARD, KIRKWOOD ARTHUR, SORCI-THOMAS, MARY G · 2012 to 2015
$2.5M
REGULATION OF PULMONARY CIRCULATION IN FETUS AND NEWBORNR01HL057268 · NHLBI · WAYNE STATE UNIVERSITY · PI KONDURI, GIRIJA G. · 1998 to 2013
$2.0M
Akt-mediated phosphorylation of hsp70 regulates mitochondrial localization of SOD2 and oxidative stress in pulmonary artery endothelial cells during postnatal transitionK08HL133379 · NHLBI · MEDICAL COLLEGE OF WISCONSIN · PI AFOLAYAN, ADELEYE J · 2016 to 2021
$821k
NHLBI NIH HHS K08 HL133379NHLBI NIH HHS R01 HL057268NHLBI NIH HHS R01 HL112270NHLBI NIH HHS R01 HL128371
6 · The paper itself

Abstract

Stress-inducible heat shock protein 70 (hsp70) interacts with superoxide dismutase 2 (SOD2) in the cytosol after synthesis to transfer the enzyme to the mitochondria for subsequent activation. However, the structural basis for this interaction remains to be defined. To map the SOD2-binding site in hsp70, mutants of hsp70 were made and tested for their ability to bind SOD2. These studies showed that SOD2 binds in the amino acid 393-537 region of the chaperone. To map the hsp70-binding site in SOD2, we used a series of pulldown assays and showed that hsp70 binds to the amino-terminal domain of SOD2. To better define the binding site, we used a series of decoy peptides derived from the primary amino acid sequence in the SOD2-binding site in hsp70. This study shows that SOD2 specifically binds to hsp70 at

Indexed as

Amino Acid SubstitutionAnimalsArginineBinding SitesCells, CulturedGlutamic AcidHSP70 Heat-Shock ProteinsMitochondriaRatsSheepSuperoxide DismutaseSuperoxide Dismutase 2SuperoxidesArginineGlutamic AcidHSP70 Heat-Shock ProteinsSuperoxide DismutaseSuperoxide Dismutase 2Superoxidesendothelial cellmitochondriaoxidative stressprotein importsuperoxide dismutase (SOD)

Identifiers

PMID28028182
PMCPMC5313107
OpenAlexW2565956713

What Socratic holds

Textmetadata
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 Socratic graph.