Evidence map›Paper›PMID 21482623›Full record

ArticleGenome research2011

Characterization of metalloproteins by high-throughput X-ray absorption spectroscopy.

Wuxian Shi, Marco Punta, Jen Bohon, J Michael Sauder, Rhijuta D'Mello, Mike Sullivan, John Toomey, Don Abel, Marco Lippi, Andrea Passerini and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Genome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  12. Frontiers in microbiology · 2018
    Article
  13. Computational approaches forBioscience reports · 2017
    Review
  14. Research in pharmaceutical sciences · 2017
    Article
  15. Review
  16. Review
  17. 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 6 institutions in 3 countries.

Wuxian ShiNew York SGX Research Center for Structural Genomics (NYSGXRC), Case Western Reserve University, Center for Proteomics and Bioinformatics, Case Center for Synchrotron Biosciences, Upton, New York 11973, USA. wushi@bnl.gov
Marco Punta
Jen Bohon
J Michael Sauder
Rhijuta D'Mello
Mike Sullivan
John Toomey
Don Abel
Marco Lippi
Andrea Passerini
Paolo Frasconi
Stephen K Burley
Burkhard Rost
Mark R Chance
Joint Center for Structural Genomics · USEli Lilly (United States) · USUniversity of Florence · ITNew York Structural Biology Center · USTechnical University of Munich · DEUniversity of Trento · IT

Funding

SUBPROJECT 5U54GM074945 · NIGMS · SGX PHARMACEUTICALS, INC. · PI BURLEY, STEPHEN KEVIN · 2005 to 2009
$46.2M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
NIBIB NIH HHS P30 EB009998NIBIB NIH HHS P30-EB-09998NIGMS NIH HHS U54 GM074945NIGMS NIH HHS U54GM074945
6 · The paper itself

Abstract

High-throughput X-ray absorption spectroscopy was used to measure transition metal content based on quantitative detection of X-ray fluorescence signals for 3879 purified proteins from several hundred different protein families generated by the New York SGX Research Center for Structural Genomics. Approximately 9% of the proteins analyzed showed the presence of transition metal atoms (Zn, Cu, Ni, Co, Fe, or Mn) in stoichiometric amounts. The method is highly automated and highly reliable based on comparison of the results to crystal structure data derived from the same protein set. To leverage the experimental metalloprotein annotations, we used a sequence-based de novo prediction method, MetalDetector, to identify Cys and His residues that bind to transition metals for the redundancy reduced subset of 2411 sequences sharing <70% sequence identity and having at least one His or Cys. As the HT-XAS identifies metal type and protein binding, while the bioinformatics analysis identifies metal- binding residues, the results were combined to identify putative metal-binding sites in the proteins and their associated families. We explored the combination of this data with homology models to generate detailed structure models of metal-binding sites for representative proteins. Finally, we used extended X-ray absorption fine structure data from two of the purified Zn metalloproteins to validate predicted metalloprotein binding site structures. This combination of experimental and bioinformatics approaches provides comprehensive active site analysis on the genome scale for metalloproteins as a class, revealing new insights into metalloprotein structure and function.

Indexed as

SoftwareBinding SitesComputational BiologyFluorescenceGenomicsMetalloproteinsMetals, HeavySynchrotronsX-Ray Absorption SpectroscopyMetalloproteinsMetals, Heavy

Identifiers

PMID21482623
PMCPMC3106322
OpenAlexW2125801802

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.