Evidence map›Paper›PMID 21949889›Full record

ArticlePloS one2011

A membrane-bound vertebrate globin.

Miriam Blank, Jessica Wollberg, Frank Gerlach, Katja Reimann, Anja Roesner, Thomas Hankeln, Angela Fago, Roy E Weber, Thorsten Burmester

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

30 citing papers in PubMed, 59 citations in OpenAlex.

  1. Insights into the function of cytoglobin.Biochemical Society transactions · 2023
    Review
  2. Article
  3. Review
  4. Structural modeling of a novel membrane-bound globin-coupled sensor inComputational and structural biotechnology journal · 2021
    Article
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  6. Review
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  8. Myoglobin as a versatile peroxidase: Implications for a more important role for vertebrate striated muscle in antioxidant defense.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · 2019
    Article
  9. The Zebrafish CytochromeBiochemistry · 2019
    Article
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  14. Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

9 authors at 3 institutions in 2 countries.

Miriam BlankBiocenter Grindel, University of Hamburg, Hamburg, Germany.
Jessica Wollberg
Frank Gerlach
Katja Reimann
Anja Roesner
Thomas Hankeln
Angela Fago
Roy E Weber
Thorsten Burmester
Universität Hamburg · DEAarhus University · DKJohannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The family of vertebrate globins includes hemoglobin, myoglobin, and other O(2)-binding proteins of yet unclear functions. Among these, globin X is restricted to fish and amphibians. Zebrafish (Danio rerio) globin X is expressed at low levels in neurons of the central nervous system and appears to be associated with the sensory system. The protein harbors a unique N-terminal extension with putative N-myristoylation and S-palmitoylation sites, suggesting membrane-association. Intracellular localization and transport of globin X was studied in 3T3 cells employing green fluorescence protein fusion constructs. Both myristoylation and palmitoylation sites are required for correct targeting and membrane localization of globin X. To the best of our knowledge, this is the first time that a vertebrate globin has been identified as component of the cell membrane. Globin X has a hexacoordinate binding scheme and displays cooperative O(2) binding with a variable affinity (P(50)∼1.3-12.5 torr), depending on buffer conditions. A respiratory function of globin X is unlikely, but analogous to some prokaryotic membrane-globins it may either protect the lipids in cell membrane from oxidation or may act as a redox-sensing or signaling protein.

Indexed as

Amino Acid SequenceAnimalsCell MembraneGene Expression Regulation, DevelopmentalGlobinsGreen Fluorescent ProteinsHemeImmunoglobulin GLipoylationMolecular Sequence DataOxygenRabbitsRecombinant ProteinsSequence Homology, Amino AcidSubcellular FractionsZebrafishGlobinsGreen Fluorescent ProteinsHemeImmunoglobulin GOxygenRecombinant Proteins

Identifiers

PMID21949889
PMCPMC3176823
OpenAlexW2062438924

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.