Evidence map›Paper›PMID 17117882›Full record

ArticleJournal of the American Chemical Society2006

FAST-NMR: functional annotation screening technology using NMR spectroscopy.

Kelly A Mercier, Michael Baran, Viswanathan Ramanathan, Peter Revesz, Rong Xiao, Gaetano T Montelione, Robert Powers

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. NMR Metabolomics Protocols for Drug Discovery.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  3. AutomaticJournal of biomolecular NMR · 2018
    Article
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  12. Review
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  20. PROFESS: a PROtein function, evolution, structure and sequence database.Database : the journal of biological databases and curation · 2010
    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

7 authors at 2 institutions in 1 country.

Kelly A MercierDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, USA.
Michael Baran
Viswanathan Ramanathan
Peter Revesz
Rong Xiao
Gaetano T Montelione
Robert Powers
University of Nebraska–Lincoln · USRutgers, The State University of New Jersey · US

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI ARROWSMITH, CHERYL H · 2005 to 2009
$56.6M
EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR015468 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI PAUL, PREM S · 2000 to 2000
$2.0M
NCRR NIH HHS C06 RR015468NCRR NIH HHS RR015468-01NIGMS NIH HHS U54 GM074958
6 · The paper itself

Abstract

An abundance of protein structures emerging from structural genomics and the Protein Structure Initiative (PSI) are not amenable to ready functional assignment because of a lack of sequence and structural homology to proteins of known function. We describe a high-throughput NMR methodology (FAST-NMR) to annotate the biological function of novel proteins through the structural and sequence analysis of protein-ligand interactions. This is based on basic tenets of biochemistry where proteins with similar functions will have similar active sites and exhibit similar ligand binding interactions, despite global differences in sequence and structure. Protein-ligand interactions are determined through a tiered NMR screen using a library composed of compounds with known biological activity. A rapid co-structure is determined by combining the experimental identification of the ligand binding site from NMR chemical shift perturbations with the protein-ligand docking program AutoDock. Our CPASS (Comparison of Protein Active Site Structures) software and database are then used to compare this active site with proteins of known function. The methodology is demonstrated using unannotated protein SAV1430 from Staphylococcus aureus.

Indexed as

Amino Acid SequenceBacterial ProteinsComputational BiologyModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularStaphylococcus aureusBacterial Proteins

Identifiers

PMID17117882
PMCPMC2529462
OpenAlexW1968868342

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.