Evidence map›Paper›PMID 28485817›Full record

ArticleFEBS letters2017

Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.

Manliang Feng, Zhongxin Ma, Breland F Crudup, Victor L Davidson

Open access · bronzeAbstract readLetter
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

0 citing papers in PubMed, 1 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

4 authors at 2 institutions in 1 country.

Manliang FengDepartment of Chemistry, Tougaloo College, MS, USA.
Zhongxin MaBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, USA.
Breland F CrudupDepartment of Chemistry, Tougaloo College, MS, USA.
Victor L DavidsonBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, USA.ORCID 0000-0002-1966-7302
Tougaloo College · USUniversity of Central Florida · US

Funding

Structure Function & Biosynthesis of Respiratory EnzymesR37GM041574 · NIGMS · UNIVERSITY OF MISSISSIPPI MED CTR · PI DAVIDSON, VICTOR L · 2009 to 2018
$3.4M
NIGMS NIH HHS R37 GM041574
6 · The paper itself

Abstract

The diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40 Å from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H

Indexed as

CatalysisHemeHydrogen PeroxideOxidoreductases Acting on CH-NH Group DonorsParacoccus denitrificansProtein BindingRhodobacter sphaeroidesSpectrum Analysis, RamanHemeHydrogen Peroxidemethylamine dehydrogenaseOxidoreductases Acting on CH-NH Group Donorselectron transferferryl hemeperoxidaseprotein-protein interactionproton transfer

Identifiers

PMID28485817
PMCPMC5905328
OpenAlexW2613217486

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.