Evidence map›Paper›PMID 10051573›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Inhibitory sites in enzymes: zinc removal and reactivation by thionein.

W Maret, C Jacob, B L Vallee, E H Fischer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
15.0field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 390 citations in OpenAlex.

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  12. Regulation of zinc-dependent enzymes by metal carrier proteins.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022
    Review
  13. Review
  14. Lysosomal ZnCell reports · 2021
    Article
  15. The Enigmatic Metallothioneins: A Case of Upward-Looking Research.International journal of molecular sciences · 2021
    Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

W MaretCenter for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Seeley G. Mudd Building, 250 Longwood Avenue, Boston, MA 02115, USA.
C Jacob
B L Vallee
E H Fischer
Harvard University · USUniversity of Washington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thionein (T) has not been isolated previously from biological material. However, it is generated transiently in situ by removal of zinc from metallothionein under oxidoreductive conditions, particularly in the presence of selenium compounds. T very rapidly activates a group of enzymes in which zinc is bound at an inhibitory site. The reaction is selective, as is apparent from the fact that T does not remove zinc from the catalytic sites of zinc metalloenzymes. T instantaneously reverses the zinc inhibition with a stoichiometry commensurate with its known capacity to bind seven zinc atoms in the form of clusters in metallothionein. The zinc inhibition is much more pronounced than was previously reported, with dissociation constants in the low nanomolar range. Thus, T is an effective, endogenous chelating agent, suggesting the existence of a hitherto unknown and unrecognized biological regulatory system. T removes the metal from an inhibitory zinc-specific enzymatic site with a resultant marked increase of activity. The potential significance of this system is supported by the demonstration of its operations in enzymes involved in glycolysis and signal transduction.

Indexed as

Enzyme InhibitorsAldehyde DehydrogenaseAnimalsBinding SitesCaspase 3Caspase InhibitorsCatalytic DomainEnzyme ActivationEnzymesFructose-BisphosphataseGlyceraldehyde-3-Phosphate DehydrogenasesKineticsLiverMetallothioneinOxidation-ReductionProtein Tyrosine PhosphatasesAldehyde DehydrogenaseCaspase 3Caspase InhibitorsEnzyme InhibitorsEnzymesFructose-BisphosphataseGlyceraldehyde-3-Phosphate DehydrogenasesMetallothioneinProtein Tyrosine PhosphatasesZinc

Identifiers

PMID10051573
PMCPMC26715
OpenAlexW2022218526

What OpenQuestion holds

Texttitle and abstract
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.