Evidence map›Paper›PMID 16566839›Full record

ArticleBMC structural biology2006

Structural proteomics of minimal organisms: conservation of protein fold usage and evolutionary implications.

John-Marc Chandonia, Sung-Hou Kim

Open access · hybridAbstract read
In one paragraph

Article in BMC structural biology, 2006. 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
1.2field-weighted citation impact, top 24% 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, 11 citations in OpenAlex.

  1. Article
  2. The comprehensive microbial resource.Nucleic acids research · 2010
    Article
  3. Review
  4. Article
  5. Review
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.

John-Marc ChandoniaPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Sung-Hou Kim
Lawrence Berkeley National Laboratory · US

Funding

Target Selection, Structure Analysis and Data ManagementP50GM062412 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KIM, SUNG-HOU · 2000 to 2005
$32.5M
NIGMS NIH HHS 1-P50-GM62412NIGMS NIH HHS P50 GM062412
6 · The paper itself

Abstract

backgroundDetermining the complete repertoire of protein structures for all soluble, globular proteins in a single organism has been one of the major goals of several structural genomics projects in recent years.

resultsWe report that this goal has nearly been reached for several "minimal organisms"--parasites or symbionts with reduced genomes--for which over 95% of the soluble, globular proteins may now be assigned folds, overall 3-D backbone structures. We analyze the structures of these proteins as they relate to cellular functions, and compare conservation of fold usage between functional categories. We also compare patterns in the conservation of folds among minimal organisms and those observed between minimal organisms and other bacteria.

conclusionWe find that proteins performing essential cellular functions closely related to transcription and translation exhibit a higher degree of conservation in fold usage than proteins in other functional categories. Folds related to transcription and translation functional categories were also overrepresented in minimal organisms compared to other bacteria.

Indexed as

Conserved SequenceEvolution, MolecularProtein FoldingProteomicsBacterial ProteinsDatabases, ProteinGlobulinsProtein Structure, SecondaryProteomeSymbiosisBacterial ProteinsGlobulinsProteome

Identifiers

PMID16566839
PMCPMC1488858
OpenAlexW1518344608

What OpenQuestion holds

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LicenceCC BY
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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.