Evidence map›Paper›PMID 30706146›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2019

Fluoride and azide binding to ferric human hemoglobin:haptoglobin complexes highlights the ligand-dependent inequivalence of the α and β hemoglobin chains.

Paolo Ascenzi, Alessandra di Masi, Giovanna De Simone, Magda Gioia, Massimo Coletta

Abstract read
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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2019. 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
0.6field-weighted citation impact, top 38% 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, 5 citations in OpenAlex.

  1. Article
  2. Kinetics of cyanide and carbon monoxide dissociation from ferrous human haptoglobin:hemoglobin(II) complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    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

5 authors at 2 institutions in 1 country.

Paolo AscenziInterdepartmental Laboratory for Electron Microscopy, Roma Tre University, Via della Vasca Navale 79, 00146, Roma, Italy. ascenzi@uniroma3.it.
Alessandra di MasiDepartment of Sciences, Roma Tre University, Viale Marconi 446, 00146, Roma, Italy.
Giovanna De SimoneDepartment of Sciences, Roma Tre University, Viale Marconi 446, 00146, Roma, Italy.
Magda GioiaDepartment of Clinical Sciences and Translational Medicine, University of Roma "Tor Vergata", Via Montpellier 1, 00133, Roma,, Italy.
Massimo ColettaDepartment of Clinical Sciences and Translational Medicine, University of Roma "Tor Vergata", Via Montpellier 1, 00133, Roma,, Italy.
Roma Tre University · ITConsorzio Interuniversitario Reattività Chimica e Catalisi · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Haptoglobin (Hp) binds human hemoglobin (Hb), contributing to prevent extra-erythrocytic Hb-induced damage. Hp forms preferentially complexes with αβ dimers, displaying heme-based reactivity. Here, kinetics and thermodynamics of fluoride and azide binding to ferric human Hb (Hb(III)) complexed with the human Hp phenotypes 1-1 and 2-2 (Hp1-1:Hb(III) and Hp2-2:Hb(III), respectively) are reported (pH 7.0 and 20.0 °C). Fluoride binds to Hp1-1:Hb(III) and Hp2-2:Hb(III) with a one-step kinetic and equilibrium behavior. In contrast, kinetics of azide binding to and dissociation from Hp1-1:Hb(III)(-N

Indexed as

AzidesBinding SitesFerric CompoundsFluoridesHaptoglobinsHemoglobinsHumansKineticsLigandsModels, MolecularThermodynamicsAzidesFerric CompoundsFluorideshaptoglobin-hemoglobin complexHaptoglobinsHemoglobinsLigandsAzide bindingFluoride bindingHuman haptoglobin 1-1:hemoglobin complexHuman haptoglobin 2-2:hemoglobin complexKineticsThermodynamics

Identifiers

PMID30706146
OpenAlexW2911896854

What OpenQuestion 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 OpenQuestion graph.