Evidence map›Paper›PMID 18584152›Full record

ArticleArchives of microbiology2008

Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus hospitalis: the major cytosolic and membrane proteins.

Tillmann Burghardt, Manfred Saller, Sonja Gürster, Daniel Müller, Carolin Meyer, Ulrike Jahn, Eduard Hochmuth, Rainer Deutzmann, Frank Siedler, Patrick Babinger and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Archives of microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Functional compartmentalization and metabolic separation in a prokaryotic cell.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. A Complex Endomembrane System in the ArchaeonFrontiers in microbiology · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Energized outer membrane and spatial separation of metabolic processes in the hyperthermophilic Archaeon Ignicoccus hospitalis.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  9. Article
  10. Tolerance of thermophilic and hyperthermophilic microorganisms to desiccation.Extremophiles : life under extreme conditions · 2009
    Article
  11. Article
  12. 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

13 authors at 2 institutions in 1 country.

Tillmann BurghardtCentre for Electron Microscopy, Faculty for Biology and Preclinical Medicine, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Manfred Saller
Sonja Gürster
Daniel Müller
Carolin Meyer
Ulrike Jahn
Eduard Hochmuth
Rainer Deutzmann
Frank Siedler
Patrick Babinger
Reinhard Wirth
Harald Huber
Reinhard Rachel
University of Regensburg · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ignicoccus hospitalis, a hyperthermophilic, chemolithoautotrophic Crenarchaeon, is the host of Nanoarchaeum equitans. Together, they form an intimate association, the first among Archaea. Membranes are of fundamental importance for the interaction of I. hospitalis and N. equitans, as they harbour the proteins necessary for the transport of macromolecules like lipids, amino acids, and cofactors between these organisms. Here, we investigated the protein inventory of I. hospitalis cells, and were able to identify 20 proteins in total. Experimental evidence and predictions let us conclude that 11 are soluble cytosolic proteins, eight membrane or membrane-associated proteins, and a single one extracellular. The quantitatively dominating proteins in the cytoplasm (peroxiredoxin; thermosome) antagonize oxidative and temperature stress which I. hospitalis cells are exposed to at optimal growth conditions. Three abundant membrane protein complexes are found: the major protein of the outer membrane, which might protect the cell against the hostile environment, forms oligomeric complexes with pores of unknown selectivity; two other complexes of the cytoplasmic membrane, the hydrogenase and the ATP synthase, play a key role in energy production and conversion.

Indexed as

Archaeal ProteinsComputational BiologyCytosolDesulfurococcaceaeElectrophoresis, Polyacrylamide GelMembrane ProteinsProteomeSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryArchaeal ProteinsMembrane ProteinsProteome

Identifiers

PMID18584152
PMCPMC2755778
OpenAlexW2167967033

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.