Evidence map›Paper›PMID 16513741›Full record

ArticleJournal of bacteriology2006

Transcriptional and biochemical analysis of starch metabolism in the hyperthermophilic archaeon Pyrococcus furiosus.

Han-Seung Lee, Keith R Shockley, Gerrit J Schut, Shannon B Conners, Clemente I Montero, Matthew R Johnson, Chung-Jung Chou, Stephanie L Bridger, Nathan Wigner, Scott D Brehm and 4 more

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

31 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Hot transcriptomics.Archaea (Vancouver, B.C.) · 2011
    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

14 authors at 2 institutions in 1 country.

Han-Seung LeeDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229, USA.
Keith R Shockley
Gerrit J Schut
Shannon B Conners
Clemente I Montero
Matthew R Johnson
Chung-Jung Chou
Stephanie L Bridger
Nathan Wigner
Scott D Brehm
Francis E Jenney
Donald A Comfort
Robert M Kelly
Michael W W Adams
North Carolina State University · USUniversity of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyrococcus furiosus utilizes starch and its degradation products, such as maltose, as primary carbon sources, but the pathways by which these alpha-glucans are processed have yet to be defined. For example, its genome contains genes proposed to encode five amylolytic enzymes (including a cyclodextrin glucanotransferase [CGTase] and amylopullulanase), as well as two transporters for maltose and maltodextrins (Mal-I and Mal-II), and a range of intracellular enzymes have been purified that reportedly metabolize maltodextrins and maltose. However, precisely which of these enzymes are involved in starch processing is not clear. In this study, starch metabolism in P. furiosus was examined by biochemical analyses in conjunction with global transcriptional response data for cells grown on a variety of glucans. In addition, DNA sequencing led to the correction of two key errors in the genome sequence, and these change the predicted properties of amylopullulanase (now designated PF1935*) and CGTase (PF0478*). Based on all of these data, a pathway is proposed that is specific for starch utilization that involves one transporter (Mal-II [PF1933 to PF1939]) and only three enzymes, amylopullulanase (PF1935*), 4-alpha-glucanotransferase (PF0272), and maltodextrin phosphorylase (PF1535). Their expression is upregulated on starch, and together they generate glucose and glucose-1-phosphate, which then feed into the novel glycolytic pathway of this organism. In addition, the results indicate that several hypothetical proteins encoded by three gene clusters are also involved in the transport and processing of alpha-glucan substrates by P. furiosus.

Indexed as

Gene Expression ProfilingGene Expression Regulation, ArchaealArchaeal ProteinsBacterial ProteinsDNA, ArchaealGlucoseGlucosephosphatesGlucosyltransferasesGlycogen Debranching Enzyme SystemGlycoside HydrolasesMonosaccharide Transport ProteinsOligonucleotide Array Sequence AnalysisPyrococcus furiosusSequence Analysis, DNAStarchSubstrate Specificity4 alpha-glucanotransferaseamylopullulanaseArchaeal ProteinsBacterial ProteinsDNA, ArchaealGlucoseglucose-1-phosphateGlucosephosphatesGlucosyltransferasesGlycogen Debranching Enzyme SystemGlycoside Hydrolasesmaltodextrin phosphorylaseMonosaccharide Transport ProteinsStarch

Identifiers

PMID16513741
PMCPMC1428126
OpenAlexW2090890915

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.