Evidence map›Paper›PMID 25932775›Full record

ArticleBioengineered2015

A thermostable archaeal S-adenosylmethionine synthetase: a promising tool to improve the synthesis of adenosylmethionine analogs of biotechnological interest.

Marina Porcelli, Concetta Paola Ilisso, Laura Mosca, Giovanna Cacciapuoti

Open access · goldAbstract read
In one paragraph

Article in Bioengineered, 2015. 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
0.5field-weighted citation impact, top 35% 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, 8 citations in OpenAlex.

  1. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  2. Review
  3. Article
  4. 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

4 authors at 2 institutions in 2 countries.

Marina Porcellia Dipartimento di Biochimica; Biofisica e Patologia Generale ; Seconda Università di Napoli ; Napoli , Italy.
Concetta Paola Ilisso
Laura Mosca
Giovanna Cacciapuoti
Instituto Biofisika · ESIstituto Nazionale di Fisica Nucleare, Sezione di Napoli · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The naturally and widely occurring sulfonium compound, S-adenosylmethionine (AdoMet), one of nature's most versatile molecules, is biosynthesized from methionine and ATP by AdoMet synthetase or methionine adenosyltransferase (MAT) in a 2-step reaction in which the energy-rich sulfonium compound is formed by dephosphorylation of ATP. All living cells, with the only exception of some parasites and infectious agents, express MAT.

Indexed as

Industrial Microbiology5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseArchaeaATP Synthetase ComplexesChemical PhenomenaMethionine AdenosyltransferaseS-Adenosylmethionine5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseATP Synthetase ComplexesMethionine AdenosyltransferaseS-Adenosylmethionineadenosylmethionine synthetaseAdoMet, S-AdenosylmethionineArchaeaBsMAT, MAT from Bacillus subtilisDMSO, dimethylsulfoxide; MAT, adenosylmethionine synthetase or methionine adenosyltransferaseEcMAT, MAT from E. coli.hyperthermophilic enzymesmethionine adenosyltransferaseMjMAT, MAT from Methanococcus jannaschiiorganic solvent activity and thermostabilityPfMAT, MAT from Pyrococcus furiosusPyrococcus furiosusS-AdenosylmethionineSsMAT, MAT from Sulfolobus solfataricusTkMAT, MAT from Thermococcus kodakarensis

Identifiers

PMID25932775
PMCPMC4601474
OpenAlexW1555118901

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.