Evidence map›Paper›PMID 20944203›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

TOPSAN: use of a collaborative environment for annotating, analyzing and disseminating data on JCSG and PSI structures.

S Sri Krishna, Dana Weekes, Constantina Bakolitsa, Marc André Elsliger, Ian A Wilson, Adam Godzik, John Wooley

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Protein structure annotation resources.Methods in molecular biology (Clifton, N.J.) · 2015
    Review
  2. Article
  3. Article
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  6. Article
  7. Article
  8. Article
  9. Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  10. The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  11. Article
  12. Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  13. Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  14. Article
  15. The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  16. Article
  17. Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  18. The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory function.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  19. Ligands in PSI structures.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  20. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

S Sri KrishnaCenter for Research in Biological Systems, University of California, San Diego, La Jolla, California, USA.
Dana Weekes
Constantina Bakolitsa
Marc André Elsliger
Ian A Wilson
Adam Godzik
John Wooley

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2005 to 2009
$50.6M
NIGMS NIH HHS U54 GM074898
6 · The paper itself

Abstract

The NIH Protein Structure Initiative centers, such as the Joint Center for Structural Genomics (JCSG), have developed highly efficient technological platforms that are capable of experimentally determining the three-dimensional structures of hundreds of proteins per year. However, the overwhelming majority of the almost 5000 protein structures determined by these centers have yet to be described in the peer-reviewed literature. In a high-throughput structural genomics environment, the process of structure determination occurs independently of any associated experimental characterization of function, which creates a challenge for the annotation and analysis of structures and the publication of these results. This challenge has been addressed by developing TOPSAN (`The Open Protein Structure Annotation Network'), which enables the generation of knowledge via collaborations among globally distributed contributors supported by automated amalgamation of available information. TOPSAN currently provides annotations for all protein structures determined by the JCSG in addition to preliminary annotations on a large number of structures from the other PSI production centers. TOPSAN-enabled collaborations have resulted in insightful structure-function analysis for many proteins and have led to numerous peer-reviewed publications, as exemplified by the articles included in this issue of Acta Crystallographica Section F.

Indexed as

Databases, GeneticGenomicsHumansInternetProtein Conformation

Identifiers

PMID20944203
PMCPMC2954197

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.