Evidence map›Paper›PMID 19850865›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Ligand migration through the internal hydrophobic cavities in human neuroglobin.

Stefania Abbruzzetti, Serena Faggiano, Stefano Bruno, Francesca Spyrakis, Andrea Mozzarelli, Sylvia Dewilde, Luc Moens, Cristiano Viappiani

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 50 citations in OpenAlex.

  1. Neuroglobin: A New Player in the Gut-Brain Axis.International journal of molecular sciences · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Unusually FastInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Neuroglobin, a Factor Playing for Nerve Cell Survival.International journal of molecular sciences · 2016
    Review
  13. Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
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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

8 authors at 5 institutions in 2 countries.

Stefania AbbruzzettiDipartimento di Fisica, National Enterprise for nanoScience and nanoTechnology CNR-INFM, Università degli Studi di Parma, 43100 Parma, Italy.
Serena Faggiano
Stefano Bruno
Francesca Spyrakis
Andrea Mozzarelli
Sylvia Dewilde
Luc Moens
Cristiano Viappiani
Biogem · ITNational Enterprise for NanoScience and NanoTechnology · ITUniversity of Antwerp · BEInstitute of Biostructure and Bioimaging · ITUniversity of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuroglobin (Ngb), a member of the globin superfamily, was found in the brain of vertebrates and is suggested to play a neuroprotective function under hypoxic conditions by scavenging nitrogen monoxide (NO) through a dioxygenase activity. In order for such a reaction to efficiently take place and to minimize the release of reactive intermediates in the cytosol, the cosubstrates O(2) and NO and other unstable reaction intermediates should bind sequentially to docking sites in the protein matrix. We have characterized the accessibility of these sites by analyzing the geminate CO rebinding kinetics to the heme moiety observed upon nanosecond flash photolysis of the Ngb-CO complex encapsulated in silica gels. The geminate rebinding phase showed a remarkable complexity, revealing the presence of a system of secondary docking sites where ligands are stored for hundreds of microseconds. Most kinetics steps display little temperature dependence, demonstrating that ligands can easily migrate through the cavities, except for the slowest reaction intermediate, possibly reflecting a structural conformational change reshaping the system of cavities. This conformational change is unrelated with distal His E7 binding to the heme, as it persists for the HE7L mutant. Overall, data are consistent with the presence of a discrete system of docking sites, possibly acting as reservoirs for the putative cosubstrates and for other reactive species involved in the physiologically relevant reaction.

Indexed as

Models, MolecularProtein ConformationCarbon MonoxideGlobinsHumansKineticsLigandsNerve Tissue ProteinsNeuroglobinNitric OxideOxygenSilica GelSilicon DioxideCarbon MonoxideGlobinsLigandsNerve Tissue ProteinsNeuroglobinNitric OxideOxygenSilica GelSilicon Dioxide

Identifiers

PMID19850865
PMCPMC2776452
OpenAlexW2123582509

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.