Evidence map›Paper›PMID 38929104›Full record

ReviewAntioxidants (Basel, Switzerland)2024

Nitric Oxide Binding Geometry in Heme-Proteins: Relevance for Signal Transduction.

Giovanna De Simone, Alessandra di Masi, Diego Sbardella, Paolo Ascenzi, Massimiliano Coletta

Abstract readReview
In one paragraph

Review in Antioxidants (Basel, Switzerland), 2024. 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
–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

2 citing papers in PubMed.

  1. Review
  2. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    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

5 authors.

Giovanna De SimoneDipartimento di Scienze, Università degli Studi Roma Tre, 00146 Rome, Italy.ORCID 0000-0002-9358-9891
Alessandra di MasiDipartimento di Scienze, Università degli Studi Roma Tre, 00146 Rome, Italy.ORCID 0000-0002-1122-8663
Diego SbardellaIRCCS Fondazione Bietti, Rome, Italy.
Paolo AscenziDipartimento di Scienze, Università degli Studi Roma Tre, 00146 Rome, Italy.ORCID 0000-0002-6449-2150
Massimiliano ColettaIRCCS Fondazione Bietti, Rome, Italy.ORCID 0000-0002-5489-9467

Funding

Ministery of University of italy Grant Dipartimenti di Eccellenza legge 232/2016 art.1 comma 314-337
6 · The paper itself

Abstract

Nitric oxide (NO) synthesis, signaling, and scavenging is associated to relevant physiological and pathological events. In all tissues and organs, NO levels and related functions are regulated at different levels, with heme proteins playing pivotal roles. Here, we focus on the structural changes related to the different binding modes of NO to heme-Fe(II), as well as the modulatory effects of this diatomic messenger on heme-protein functions. Specifically, the ability of heme proteins to bind NO at either the distal or proximal side of the heme and the transient interchanging of the binding site is reported. This sheds light on the regulation of O

Indexed as

cytochrome cheme model compoundsheme (protein) nitrosylationheme proteinshemoglobinmyoglobinnitric oxidesoluble guanylate cyclase

Identifiers

PMID38929104
PMCPMC11201058

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.