Evidence map›Paper›PMID 22427982›Full record

ArticlePloS one2012

Robust, integrated computational control of NMR experiments to achieve optimal assignment by ADAPT-NMR.

Arash Bahrami, Marco Tonelli, Sarata C Sahu, Kiran K Singarapu, Hamid R Eghbalnia, John L Markley

Abstract read
In one paragraph

Article in PloS one, 2012. 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
–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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Biomolecular NMR: Past and future.Archives of biochemistry and biophysics · 2017
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Assignments of RNase A by ADAPT-NMR and enhancer.Biomolecular NMR assignments · 2015
    Article
  10. Fast automated protein NMR data collection and assignment by ADAPT-NMR on Bruker spectrometers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013
    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

6 authors.

Arash BahramiNational Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin - Madison, Madison, Wisconsin, United States of America.
Marco Tonelli
Sarata C Sahu
Kiran K Singarapu
Hamid R Eghbalnia
John L Markley

Funding

Specialized Center for Eukaryotic Structural GenomicsU54GM074901 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2005 to 2009
$18.9M
WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
NCRR NIH HHS 3P41RR02301-25S1NCRR NIH HHS P41 RR002301NCRR NIH HHS P41 RR02301NIGMS NIH HHS 1U54 GM74901NIGMS NIH HHS U54 GM074901
6 · The paper itself

Abstract

ADAPT-NMR (Assignment-directed Data collection Algorithm utilizing a Probabilistic Toolkit in NMR) represents a groundbreaking prototype for automated protein structure determination by nuclear magnetic resonance (NMR) spectroscopy. With a [(13)C,(15)N]-labeled protein sample loaded into the NMR spectrometer, ADAPT-NMR delivers complete backbone resonance assignments and secondary structure in an optimal fashion without human intervention. ADAPT-NMR achieves this by implementing a strategy in which the goal of optimal assignment in each step determines the subsequent step by analyzing the current sum of available data. ADAPT-NMR is the first iterative and fully automated approach designed specifically for the optimal assignment of proteins with fast data collection as a byproduct of this goal. ADAPT-NMR evaluates the current spectral information, and uses a goal-directed objective function to select the optimal next data collection step(s) and then directs the NMR spectrometer to collect the selected data set. ADAPT-NMR extracts peak positions from the newly collected data and uses this information in updating the analysis resonance assignments and secondary structure. The goal-directed objective function then defines the next data collection step. The procedure continues until the collected data support comprehensive peak identification, resonance assignments at the desired level of completeness, and protein secondary structure. We present test cases in which ADAPT-NMR achieved results in two days or less that would have taken two months or more by manual approaches.

Indexed as

AlgorithmsSoftwareCarbon IsotopesData CollectionNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProbabilityProtein Structure, SecondaryCarbon IsotopesNitrogen Isotopes

Identifiers

PMID22427982
PMCPMC3299752

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.