Evidence map›Paper›PMID 15115183›Full record

ArticleThe protein journal2004

Properties of the complex between recombinant human progastrin and ferric ions.

Graham S Baldwin

Abstract read
PubMed Publisher
In one paragraph

Article in The protein journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Ferric ions inhibit proteolytic processing of progastrin.Biochemical and biophysical research communications · 2011
    Article
  4. Stimulation of proliferation in the colorectal mucosa by gastrin precursors is blocked by desferrioxamine.American journal of physiology. Gastrointestinal and liver physiology · 2010
    Article
  5. 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

1 author at 1 institution in 1 country.

Graham S BaldwinUniversity of Melbourne, Department of Surgery, Austin Campus, Austin, Australia. grahamsb@unimelb.edu.au
University of Melbourne · AU

Funding

The biology of gastrin-ferric ion complexesR01GM065926 · NIGMS · UNIVERSITY OF MELBOURNE · PI BALDWIN, GRAHAM S · 2002 to 2009
$1.0M
NIGMS NIH HHS R01 GM065926
6 · The paper itself

Abstract

Binding of ferric ions to the hormone glycine-extended gastrin17 is essential for biological activity (Pannequin, J., et al. (2002). J. Biol. Chem. 277: 48602-48609). The aims of the current study were to determine the properties of the complex between recombinant human progastrin6-80 and ferric ions. The stoichiometry and affinity of ferric ion binding were determined by fluorescence spectroscopy. The selectivity of metal ion binding and the stability of the 59Fe(III) progastrin6-80 complex were determined by equilibrium dialysis. The stoichiometry of 2.5 +/- 0.1 moles Fe/mole progastrin, and the apparent dissociation constant of 2.2 +/- 0.1 microM, were similar to the values previously determined for glycine-extended gastrin17 at pH 4.0. Of the four trivalent and seven divalent metal ions tested, only ferrous and ferric ions bound to progastrin6-80. The ferric ion-progastrin complex was extremely stable, with a half-life of 117 +/- 8 days at pH 7.6 and 25 degrees C. We conclude that recombinant human progastrin6-80 selectively binds ferrous and ferric ions with high affinity in a stable 2:1 complex.

Indexed as

Binding SitesFerric CompoundsGastrinsHumansKineticsProtein BindingProtein PrecursorsRecombinant Proteinsbig gastrinFerric CompoundsGastrinsProtein PrecursorsRecombinant Proteins

Identifiers

PMID15115183
OpenAlexW1965358716

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.