Evidence map›Paper›PMID 30347123›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Mechanisms of HNO Reactions with Ferric Heme Proteins.

Yelu Shi, Yong Zhang

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Insight into the preferential N-bindingDalton transactions (Cambridge, England : 2003) · 2021
    Article
  8. 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

2 authors.

Yelu ShiDepartment of Chemistry and Chemical Biology, Stevens Institute of Technology, 1 Castle Point on Hudson, Hoboken, NJ, 07030, USA.
Yong ZhangDepartment of Chemistry and Chemical Biology, Stevens Institute of Technology, 1 Castle Point on Hudson, Hoboken, NJ, 07030, USA.ORCID 0000-0001-7207-6416

Funding

Structure, Spectra, and Roles of Metal and Active Site in HNO Heme Protein CompleR15GM085774 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI ZHANG, YONG · 2008 to 2021
$1.4M
NIGMS NIH HHS R15 GM085774NIH HHS GM085774
6 · The paper itself

Abstract

Many HNO-scavenging pathways exist to regulate its biological and pharmacological activities. Such reactions often involve ferric heme proteins and form an important basis for HNO probe development. However, mechanisms of HNO reactions with ferric heme proteins are largely unknown. We performed a computational investigation using metmyoglobin and catalase as representative ferric heme proteins with neutral and negatively charged axial ligands to provide the first detailed pathways. The results reproduced experimental barriers well with an average error of 0.11 kcal mol

Indexed as

CatalaseLigandsMetmyoglobinNitrogen OxidesThermodynamicsCatalaseLigandsMetmyoglobinNitrogen Oxidesnitroxylbioinorganic chemistrycomputational chemistryheme proteinsnitrogen oxidesreaction mechanisms

Identifiers

PMID30347123
PMCPMC6522253

What OpenQuestion holds

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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.