Evidence map›Paper›PMID 7892265›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase.

T Nakashima, T Inoue, A Oka, T Nishino, T Osumi, S Hata

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-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

29 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Origin and Evolution of Polycyclic Triterpene Synthesis.Molecular biology and evolution · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Production of squalene by microbes: an update.World journal of microbiology & biotechnology · 2016
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

6 authors at 1 institution in 1 country.

T NakashimaFaculty of Science, Himeji Institute of Technology, Hyogo, Japan.
T Inoue
A Oka
T Nishino
T Osumi
S Hata
Himeji University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have isolated and characterized two overlapping cDNA clones for Arabidopsis thaliana squalene synthase. Their nucleotide sequences contained an open reading frame for a 410-amino acid polypeptide (calculated molecular mass, 47 kDa). The deduced amino acid sequence of the Arabidopsis polypeptide was significantly homologous (42-44% identical) to the sequences of known squalene synthases of several species, from yeast to man, but it was much less homologous to that of tomato phytoene synthase. To express the Arabidopsis enzyme in Escherichia coli, the entire coding region was subcloned into an expression vector. A cell-free extract of E. coli transformed with the recombinant plasmid, in the presence of NADPH and Mg2+, efficiently converted [14C]farnesyl diphosphate into squalene. On the other hand, in the absence of NADPH and the presence of Mn2+, the cell-free extract formed dehydrosqualene as a secondary product. Another E. coli extract expressing mouse squalene synthase showed the same activity as the Arabidopsis enzyme. Therefore, both the structure and reaction mechanism of squalene synthases are markedly conserved in taxonomically remote eukaryotes.

Indexed as

Alkyl and Aryl TransferasesPhylogenyAmino Acid SequenceAnimalsArabidopsisBase SequenceCloning, MolecularConsensus SequenceDNA, ComplementaryDNA PrimersEscherichia coliFarnesyl-Diphosphate FarnesyltransferaseGene ExpressionGenes, PlantGenetic VectorsGeranylgeranyl-Diphosphate GeranylgeranyltransferaseAlkyl and Aryl TransferasesDNA, ComplementaryDNA PrimersFarnesyl-Diphosphate FarnesyltransferaseGeranylgeranyl-Diphosphate GeranylgeranyltransferaseRecombinant ProteinsTransferases

Identifiers

PMID7892265
PMCPMC42476
OpenAlexW2087445881

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.