Evidence map›Paper›PMID 19997761›Full record

ReviewAmino acids2010

Structural biology of S-adenosylmethionine decarboxylase.

Shridhar Bale, Steven E Ealick

Open access · greenAbstract readReview
In one paragraph

Review in Amino acids, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 19% 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, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Functional polyamine metabolic enzymes and pathways encoded by the virosphere.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Review
  10. Review
  11. Review
  12. Polyamine Metabolism inMedical sciences (Basel, Switzerland) · 2022
    Review
  13. Review
  14. Polyamines in mammalian pathophysiology.Cellular and molecular life sciences : CMLS · 2019
    Review
  15. Article
  16. Article
  17. Extending enzyme molecular recognition with an expanded amino acid alphabet.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Shridhar BaleDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, 14853, USA.
Steven E Ealick
Cornell University · US

Funding

Rational Design of Inhibitors of Polyamine SynthesisP01CA094000 · NCI · CORNELL UNIVERSITY ITHACA · PI EALICK, STEVEN E · 2003 to 2007
$4.9M
NCI NIH HHS CA-94000NCI NIH HHS P01 CA094000
6 · The paper itself

Abstract

S-adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and a subject of many structural and biochemical investigations for anti-cancer and anti-parasitic therapy. The enzyme undergoes an internal serinolysis reaction as a post-translational modification to generate the active site pyruvoyl group for the decarboxylation process. The crystal structures of AdoMetDC from Homo sapiens, Solanum tuberosum, Thermotoga maritima, and Aquifex aeolicus have been determined. Numerous crystal structures of human AdoMetDC and mutants have provided insights into the mechanism of autoprocessing, putrescine activation, substrate specificity, and inhibitor design to the enzyme. The comparison of the human and potato enzyme with the T. maritima and A. aeolicus enzymes supports the hypothesis that the eukaryotic enzymes evolved by gene duplication and fusion. The residues implicated in processing and activity are structurally conserved in all forms of the enzyme, suggesting a divergent evolution of AdoMetDC.

Indexed as

Adenosylmethionine DecarboxylaseAnimalsBacteriaBacterial ProteinsCatalytic DomainEukaryotaHumansMolecular Sequence DataProtein Structure, SecondarySubstrate SpecificityAdenosylmethionine DecarboxylaseBacterial Proteins

Identifiers

PMID19997761
PMCPMC2847442
OpenAlexW2028178474

What OpenQuestion holds

Textmetadata
LicenceTDM
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.